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1,5-diaminopentane + O2 + H2O
?
-
-
-
-
?
1,5-diaminopentane + O2 + H2O
? + NH3 + H2O2
6,6-dideutrolysine + O2 + H2O
? + NH3 + H2O2
agmatine + O2 + H2O
?
-
-
-
?
benzylamine + O2 + H2O
benzaldehyde + NH3 + H2O2
-
-
-
-
?
collagen + H2O + O2
allysyl-collagen + NH3 + H2O2
collagen + O2 + H2O
?
-
collagen type I, II, III, IV, VI, VIII and X
-
-
?
collagen 2a1 + O2 + H2O
?
-
-
-
?
collagen III + O2 + H2O
allysyl-collagen III + NH3 + H2O2
-
-
-
-
?
dichlorodihydrofluorescein diacetate + O2 + H2O
? + NH3 + H2O2
-
-
-
-
?
elastin + H2O + O2
allysyl-elastin + NH3 + H2O2
elastin + O2 + H2O
?
-
-
-
-
?
histamine + O2 + H2O
?
-
-
-
?
histone H2 + O2 + H2O
?
-
recombinant mature LOX and C-terminally deleted enzyme
-
-
?
lysine + O2 + H2O
?
-
-
-
?
lysine:tyrosine (4:1) heteropolymer + O2 + H2O
? + NH3 + H2O2
n-alkylamine + O2 + H2O
aldehyde + NH3 + H2O2
peptide acK685 + O2 + H2O
? + NH3 + H2O2
-
-
-
-
?
peptidyl-L-hydroxylysyl-peptide + O2 + H2O
peptidyl-L-2-amino-5-hydroxy-6-oxohexanoyl-peptide + NH3 + H2O2
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
polylysine + O2 + H2O
allysine + H2O2 + NH3
-
-
-
-
?
putrescine + O2 + H2O
?
-
-
-
?
spermidine + O2 + H2O
?
-
-
-
?
spermine + O2 + H2O
?
-
-
-
?
tropoelastin + ?
?
-
LOXL1 catalyzes the polymerization of tropoelastin
-
-
?
tropoelastin + H2O + O2
?
-
-
-
?
tropoelastin + O2 + H2O
?
-
-
-
?
tropoelastin + O2 + H2O
? + H2O2 + NH3
-
oxidation of L-lysine residues, substrate from mammalia
-
-
?
[collagen]-L-lysine + O2 + H2O
[collagen]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
[elastin]-L-lysine + O2 + H2O
[elastin]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
the enzyme catalyzes the oxidative deamination of lysine residues of extracellular matrix proteins such as elastins and collagens and generate aldehyde groups. The oxidative deamination of lysine represents the foundational step for the cross-linking of elastin and collagen and thus is crucial for modeling of extracellular matrix
-
-
?
additional information
?
-
1,5-diaminopentane + O2 + H2O
? + NH3 + H2O2
-
-
-
-
?
1,5-diaminopentane + O2 + H2O
? + NH3 + H2O2
-
-
-
?
6,6-dideutrolysine + O2 + H2O
? + NH3 + H2O2
-
-
-
-
?
6,6-dideutrolysine + O2 + H2O
? + NH3 + H2O2
-
-
-
-
?
cadaverine + O2 + H2O
?
-
-
-
-
?
cadaverine + O2 + H2O
?
-
-
-
?
collagen + H2O + O2
allysyl-collagen + NH3 + H2O2
-
-
-
?
collagen + H2O + O2
allysyl-collagen + NH3 + H2O2
-
the enzyme initiates the enzymatic stage of collagen and elastin cross-linking. Lysyl oxidase activity is essential for the integrity maintenance of the dermis and for the homeostasis of the epidermis. The LOX protein plays a role in the skin carcinomas and invasion but not through its enzymatic activity
-
-
?
elastin + H2O + O2
allysyl-elastin + NH3 + H2O2
-
-
-
?
elastin + H2O + O2
allysyl-elastin + NH3 + H2O2
-
-
-
-
?
elastin + H2O + O2
allysyl-elastin + NH3 + H2O2
-
the enzyme initiates the enzymatic stage of collagen and elastin cross-linking. Lysyl oxidase activity is essential for the integrity maintenance of the dermis and for the homeostasis of the epidermis. The LOX protein plays a role in the skin carcinomas and invasion but not through its enzymatic activity
-
-
?
histone H1 + O2 + H2O
?
-
L-lysine residues in histone H1
-
-
?
histone H1 + O2 + H2O
?
-
L-lysine residues in histone H1
-
-
?
histone H1 + O2 + H2O
?
-
recombinant mature LOX and C-terminally deleted enzyme
-
-
?
histone H1 + O2 + H2O
?
-
L-lysine residues in histone H1
-
-
?
lysine:tyrosine (4:1) heteropolymer + O2 + H2O
? + NH3 + H2O2
-
-
-
-
?
lysine:tyrosine (4:1) heteropolymer + O2 + H2O
? + NH3 + H2O2
-
-
-
-
?
n-alkylamine + O2 + H2O
aldehyde + NH3 + H2O2
-
synthetic substrates
-
-
?
n-alkylamine + O2 + H2O
aldehyde + NH3 + H2O2
-
synthetic substrates
-
-
?
n-alkylamine + O2 + H2O
aldehyde + NH3 + H2O2
-
synthetic substrates
-
-
?
peptidyl-L-hydroxylysyl-peptide + O2 + H2O
peptidyl-L-2-amino-5-hydroxy-6-oxohexanoyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-hydroxylysyl-peptide + O2 + H2O
peptidyl-L-2-amino-5-hydroxy-6-oxohexanoyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-hydroxylysyl-peptide + O2 + H2O
peptidyl-L-2-amino-5-hydroxy-6-oxohexanoyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-hydroxylysyl-peptide + O2 + H2O
peptidyl-L-2-amino-5-hydroxy-6-oxohexanoyl-peptide + NH3 + H2O2
-
part of tropocollagen and tropoelastin
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
deamination of lysyl and hydroxylysyl residues is part of the pyridinoline biosynthetic pathway, pyridinoline is involved in formation of intracellular and extracellular collagen cross-links responsible for aging of connective tissue
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
in a variety of basic globular proteins
i.e. peptidyl-L-alpha-aminoadipic-delta-semialdehyde
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
key enzyme in formation of lysine cross-links in side collagen and elastin molecules
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
substrates are proteins of the extracellular matrix
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
in a variatey of basic globular proteins
i.e. peptidyl-L-alpha-aminoadipic-delta-semialdehyde
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
in collagen and elastin fibrills
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
657782, 658189, 659197, 659751, 685940, 685949, 685981, 686366, 686392, 687919, 724520 -
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
formation of cross-links in mature fibrillar collagen and elastin fibers in the extracellular space
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
initiation of covalent intermolecular cross-linking of collagen by the enzyme action on telopeptidyl lysine and hydroxylysine residues
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
lysyl oxidase plays a critical role in the formation of the extracellular matrix, and its activity is required for the normal maturation and cross-linking of collagen and elastin
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
in a variatey of basic globular proteins
i.e. peptidyl-L-alpha-aminoadipic-delta-semialdehyde
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
part of tropocollagen and tropoelastin
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
part of elastin and collagen
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
part of elastin and collagen
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-L-allysyl-peptide + NH3 + H2O2
-
crosslinkage in fibrillar collagen and elastin
-
-
?
[collagen]-L-lysine + O2 + H2O
[collagen]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
-
-
-
?
[collagen]-L-lysine + O2 + H2O
[collagen]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
the enzyme catalyzes the oxidative deamination of lysine residues of extracellular matrix proteins such as elastins and collagens and generate aldehyde groups. The oxidative deamination of lysine represents the foundational step for the cross-linking of elastin and collagen and thus is crucial for modeling of extracellular matrix
-
-
?
additional information
?
-
-
enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments
-
-
?
additional information
?
-
-
enzyme contains a cytokine receptor domain, substrate specificity, preference for the L-lysine residues in the sequence N-acetyl-(Gly)4-Glu-Lys-(Gly)5-amide, enzyme is tightly associated to the substrates in connective tissue
-
-
?
additional information
?
-
-
the enzyme does not affect smooth muscle cell proliferation nor elastin precursor, tropoelastin, synthesis, nor total elastin synthesis in a per-cell-basis
-
-
?
additional information
?
-
-
critical role for lysyl oxidase in zebrafish notochord morphogenesis
-
-
?
additional information
?
-
LOX induced chromatin changes, mechanism via histone deamination
-
-
?
additional information
?
-
LOX induced chromatin changes, mechanism via histone deamination
-
-
?
additional information
?
-
lysyl oxidase gene family. Enzyme seems to be involved in binding and crosslinking to other cell-surface and extracellular-matrix proteins
-
-
?
additional information
?
-
-
lysyl oxidase gene family. Enzyme seems to be involved in binding and crosslinking to other cell-surface and extracellular-matrix proteins
-
-
?
additional information
?
-
-
enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments, enzyme expression in downregulated in Menkes disease, a disorder of copper transport
-
-
?
additional information
?
-
-
LOX induced chromatin changes, mechanism via histone deamination
-
-
?
additional information
?
-
-
the enzyme forms are differently involved in tumor suppression, cellular senescence, and chemotaxis
-
-
?
additional information
?
-
-
enzyme contains a cytokine receptor domain, substrate specificity, preference for the L-lysine residues in the sequence N-acetyl-(Gly)4-Glu-Lys-(Gly)5-amide, enzyme is tightly associated to the substrates in connective tissue
-
-
?
additional information
?
-
-
lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 all contain a cytokine receptor-like domain
-
-
?
additional information
?
-
-
lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 all contain a cytokine receptor-like domain
-
-
?
additional information
?
-
-
potential role of lysyl oxidase/placental lactogen interactions in breast epithelial cell proliferation and migration
-
-
?
additional information
?
-
-
LOXL3 encodes two variants, LOXL3 and LOXL3-sv1, both of which function as amine oxidases with distinct tissue and substrate specificities
-
-
?
additional information
?
-
-
catalyzes the cross-linking of collagens or elastin in the extracellular compartment, thereby regulating the tensile strength of tissues
-
-
?
additional information
?
-
-
purifiedLOXreadily oxidizes peptidyl lysines in basic globular proteins with isoelectric points greater than pH 8, whereas no oxidation is detected in neutral or acidic proteins with isoelectric points less than pH 8
-
-
?
additional information
?
-
-
LOX is a copper-dependent amine oxidase that initiates the covalent cross-linking of collagen and elastin side chains and thereby contributes to extracellular matrix integrity
-
-
?
additional information
?
-
-
LOX is an extracellular matrix-remodeling enzyme involved in regulation of tumor metastasis
-
-
?
additional information
?
-
-
LOX secreted by hypoxic breast tumor cells accumulates at premetastatic sites, crosslinks collagen IV in the basement membrane, and is essential for CD11b+ myeloid cell recruitment. LOX inhibition prevents CD11b+ cell recruitment and metastatic growth. CD11b+ cells and LOX also colocalize in biopsies of human metastases, detailed overview
-
-
?
additional information
?
-
apparent lysyl oxidase isozymes contain a highly conserved LOX active site sequence in the nuclei of PC12 cells
-
-
?
additional information
?
-
-
apparent lysyl oxidase isozymes contain a highly conserved LOX active site sequence in the nuclei of PC12 cells
-
-
?
additional information
?
-
-
enzymatic activity is assayed using a peroxide-coupled assay and the nonpeptidyl substrate 1,5-diaminopentane producing the corresponding aldehyde
-
-
?
additional information
?
-
-
enzyme is responsible for the cross-linking of collagen and elastin, and is required for vascular and diaphragmatic development during embryogenesis
-
-
?
additional information
?
-
-
expression of isozymes LOXL1,3,4 during osteoblast differentiation is highly regulated due to their distinct roles in collagen matrix stabilization and subsequent mineralization
-
-
?
additional information
?
-
-
LOX is essential for collagen and elastin matrix stability and newborn animal survival
-
-
?
additional information
?
-
-
lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 all contain a cytokine receptor-like domain
-
-
?
additional information
?
-
-
lysyl oxidase is essential for normal development and function of the respiratory system and for the integrity of elastic and collagen fibers in various tissues
-
-
?
additional information
?
-
-
catalyzes the cross-linking of collagens or elastin in the extracellular compartment, thereby regulating the tensile strength of tissues
-
-
?
additional information
?
-
-
purified LOX readily oxidizes peptidyl lysines in basic globular proteins with isoelectric points greater than pH 8, whereas no oxidation is detected in neutral or acidic proteins with isoelectric points less than pH 8
-
-
?
additional information
?
-
-
lysyl oxidase, an amine oxidase, is critical for the initiation of collagen and elastin cross-linking, binds transforming growth factor-beta, and regulates its signaling via amine oxidase activity, mechanism, overview. LOX suppresses TGF-beta1-induced Smad3 phosphorylation likely through its amine oxidase activity
-
-
?
additional information
?
-
-
the enzyme forms desmosine crosslinking structures in elastic fibers contributing to the elasticity
-
-
?
additional information
?
-
-
enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments
-
-
?
additional information
?
-
-
enzyme contains a cytokine receptor domain, substrate specificity, preference for the L-lysine residues in the sequence N-acetyl-(Gly)4-Glu-Lys-(Gly)5-amide, enzyme is tightly associated to the substrates in connective tissue
-
-
?
additional information
?
-
-
lysyl oxidase is a copper-dependent amine oxidase that catalyzes the crosslinking of collagens and elastin, and is thus critical for the stability of the extracellular matrix
-
-
?
additional information
?
-
apparent lysyl oxidase isozymes contain a highly conserved LOX active site sequence in the nuclei of PC-12 cells
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
collagen + H2O + O2
allysyl-collagen + NH3 + H2O2
collagen III + O2 + H2O
allysyl-collagen III + NH3 + H2O2
-
-
-
-
?
elastin + H2O + O2
allysyl-elastin + NH3 + H2O2
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
[collagen]-L-lysine + O2 + H2O
[collagen]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
[elastin]-L-lysine + O2 + H2O
[elastin]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
the enzyme catalyzes the oxidative deamination of lysine residues of extracellular matrix proteins such as elastins and collagens and generate aldehyde groups. The oxidative deamination of lysine represents the foundational step for the cross-linking of elastin and collagen and thus is crucial for modeling of extracellular matrix
-
-
?
additional information
?
-
collagen + H2O + O2
allysyl-collagen + NH3 + H2O2
-
-
-
?
collagen + H2O + O2
allysyl-collagen + NH3 + H2O2
-
the enzyme initiates the enzymatic stage of collagen and elastin cross-linking. Lysyl oxidase activity is essential for the integrity maintenance of the dermis and for the homeostasis of the epidermis. The LOX protein plays a role in the skin carcinomas and invasion but not through its enzymatic activity
-
-
?
elastin + H2O + O2
allysyl-elastin + NH3 + H2O2
-
-
-
?
elastin + H2O + O2
allysyl-elastin + NH3 + H2O2
-
-
-
-
?
elastin + H2O + O2
allysyl-elastin + NH3 + H2O2
-
the enzyme initiates the enzymatic stage of collagen and elastin cross-linking. Lysyl oxidase activity is essential for the integrity maintenance of the dermis and for the homeostasis of the epidermis. The LOX protein plays a role in the skin carcinomas and invasion but not through its enzymatic activity
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
deamination of lysyl and hydroxylysyl residues is part of the pyridinoline biosynthetic pathway, pyridinoline is involved in formation of intracellular and extracellular collagen cross-links responsible for aging of connective tissue
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
key enzyme in formation of lysine cross-links in side collagen and elastin molecules
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
substrates are proteins of the extracellular matrix
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
formation of cross-links in mature fibrillar collagen and elastin fibers in the extracellular space
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
initiation of covalent intermolecular cross-linking of collagen by the enzyme action on telopeptidyl lysine and hydroxylysine residues
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
-
-
-
?
peptidyl-L-lysyl-peptide + O2 + H2O
peptidyl-allysyl-peptide + NH3 + H2O2
-
enzyme plays a critical role in the formation and repair of extracellular matrix, formation of cross-links in fibrillar collagen and elastin, only in fibrillar aggregates
-
-
?
[collagen]-L-lysine + O2 + H2O
[collagen]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
-
-
-
?
[collagen]-L-lysine + O2 + H2O
[collagen]-(S)-2-amino-6-oxohexanoate + NH3 + H2O2
the enzyme catalyzes the oxidative deamination of lysine residues of extracellular matrix proteins such as elastins and collagens and generate aldehyde groups. The oxidative deamination of lysine represents the foundational step for the cross-linking of elastin and collagen and thus is crucial for modeling of extracellular matrix
-
-
?
additional information
?
-
-
enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments
-
-
?
additional information
?
-
-
the enzyme does not affect smooth muscle cell proliferation nor elastin precursor, tropoelastin, synthesis, nor total elastin synthesis in a per-cell-basis
-
-
?
additional information
?
-
-
critical role for lysyl oxidase in zebrafish notochord morphogenesis
-
-
?
additional information
?
-
LOX induced chromatin changes, mechanism via histone deamination
-
-
?
additional information
?
-
LOX induced chromatin changes, mechanism via histone deamination
-
-
?
additional information
?
-
lysyl oxidase gene family. Enzyme seems to be involved in binding and crosslinking to other cell-surface and extracellular-matrix proteins
-
-
?
additional information
?
-
-
lysyl oxidase gene family. Enzyme seems to be involved in binding and crosslinking to other cell-surface and extracellular-matrix proteins
-
-
?
additional information
?
-
-
enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments, enzyme expression in downregulated in Menkes disease, a disorder of copper transport
-
-
?
additional information
?
-
-
LOX induced chromatin changes, mechanism via histone deamination
-
-
?
additional information
?
-
-
the enzyme forms are differently involved in tumor suppression, cellular senescence, and chemotaxis
-
-
?
additional information
?
-
-
potential role of lysyl oxidase/placental lactogen interactions in breast epithelial cell proliferation and migration
-
-
?
additional information
?
-
-
LOX is a copper-dependent amine oxidase that initiates the covalent cross-linking of collagen and elastin side chains and thereby contributes to extracellular matrix integrity
-
-
?
additional information
?
-
-
LOX is an extracellular matrix-remodeling enzyme involved in regulation of tumor metastasis
-
-
?
additional information
?
-
-
LOX secreted by hypoxic breast tumor cells accumulates at premetastatic sites, crosslinks collagen IV in the basement membrane, and is essential for CD11b+ myeloid cell recruitment. LOX inhibition prevents CD11b+ cell recruitment and metastatic growth. CD11b+ cells and LOX also colocalize in biopsies of human metastases, detailed overview
-
-
?
additional information
?
-
-
enzyme is responsible for the cross-linking of collagen and elastin, and is required for vascular and diaphragmatic development during embryogenesis
-
-
?
additional information
?
-
-
expression of isozymes LOXL1,3,4 during osteoblast differentiation is highly regulated due to their distinct roles in collagen matrix stabilization and subsequent mineralization
-
-
?
additional information
?
-
-
LOX is essential for collagen and elastin matrix stability and newborn animal survival
-
-
?
additional information
?
-
-
lysyl oxidase is essential for normal development and function of the respiratory system and for the integrity of elastic and collagen fibers in various tissues
-
-
?
additional information
?
-
-
lysyl oxidase, an amine oxidase, is critical for the initiation of collagen and elastin cross-linking, binds transforming growth factor-beta, and regulates its signaling via amine oxidase activity, mechanism, overview. LOX suppresses TGF-beta1-induced Smad3 phosphorylation likely through its amine oxidase activity
-
-
?
additional information
?
-
-
the enzyme forms desmosine crosslinking structures in elastic fibers contributing to the elasticity
-
-
?
additional information
?
-
-
enzyme modifies cellular activity and can function as a messenger shuttling information between the intra- and extracellular compartments
-
-
?
additional information
?
-
-
lysyl oxidase is a copper-dependent amine oxidase that catalyzes the crosslinking of collagens and elastin, and is thus critical for the stability of the extracellular matrix
-
-
?
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(1Z)-butanal thiosemicarbazone
-
-
(2-chloropyridin-4-yl)methanamine
-
-
1-(2-chloropyridin-4-yl)methanamine
-
-
1-(2-fluoropyridin-4-yl)methanamine
-
-
1-(2-methoxypyridin-4-yl)methanamine
-
-
1-(2-phenoxypyridin-4-yl)methanamine
-
-
1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride
-
1-(3-fluoropyridin-4-yl)methanamine
-
-
1-(4-fluorophenyl)methanamine
-
-
1-(4-methoxyphenyl)methanamine
-
-
1-(4-nitrophenyl)methanamine
-
-
1-(pyridin-4-yl)methanamine
-
-
1-(quinolin-4-yl)methanamine
-
-
1-([2,3'-bipyridin]-4-yl)methanamine
-
-
1-[2-(1H-imidazol-1-yl)pyridin-4-yl]methanamine
-
-
1-[2-(trifluoromethyl)pyridin-4-yl]methanamine
-
-
1-[3-(benzyloxy)-5-ethoxypyridin-4-yl]methanamine dihydrochloride
-
1-[3-(hydrazinylmethyl)phenyl]methanamine
-
-
1-[4-(1,3-thiazol-2-yl)phenyl]methanamine
-
-
1-[4-(hydrazinylmethyl)phenyl]methanamine
-
-
1-[5-(trifluoromethyl)[2,3'-bipyridin]-4-yl]methanamine
-
-
2-(pyridin-4-yl)ethan-1-amine
-
-
2-Aminopropionitrile
i.e. BAPN, is an irreversible inhibitor of LOX, involved in regulating the metastatic colonization potential of the human breast cancer cell line MDAMB-231
2-mercaptoethanol
-
weakly inhibitory
2-mercaptopyridine-N-oxide
2-phenylcyclopropan-1-amine
-
-
2-phenylethan-1-amine
-
-
3,3'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dipropan-1-ol dihydrochloride
-
3,4-dihydroxybenzoate
-
-
4,4'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dibutan-1-ol dihydrochloride
-
4-(aminomethyl)aniline
-
-
4-(aminomethyl)benzonitrile
-
-
4-deoxypyridoxine
-
pyridoxal analogue, 50% inhibition at 3 mM
alpha2-Macroglobulin
-
-
-
ascorbic acid
-
inhibits the purified enzyme in vitro, and the formation of cross-linked collagen
basic fibroblast growth factor
-
reduces enzyme expression in osteogenic cells
-
cyclohexanone thiosemicarbazone
-
-
cyclopentanone thiosemicarbazone
-
-
diethyldithiocarbamate
-
-
Disulfiram
-
a dithiocarbamate and Cu2+-chelator, inhibits the enzyme and causes teratogenic effects, malformations, distorted notochord development, and shortened anterior to posterior axis in zebrafish, overview
erythorbic acid
-
stereoisomer of ascorbic acid
glutathione
-
slight inhibition
Isonicotinic acid hydrazide
low-density lipoprotein
-
methyl 3-(aminomethyl)benzoate
-
-
methyl 4-(aminomethyl)benzoate
-
-
N-[2-([2-[(1-oxidopyridin-2-yl)sulfanyl]ethyl]amino)ethyl]-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide
-
fully effective at 0.02 mM
tert-butyl [2-[(1-oxidopyridin-2-yl)sulfanyl]ethyl]carbamate
-
fully effective at 0.002 mM
thiram
-
a dithiocarbamate and Cu2+-chelator, inhibits the enzyme and causes teratogenic effects, malformations, distorted notochord development, and shortened anterior to posterior axis in zebrafish, overview
tumor necrosis factor-alpha
-
VE-statin/egfl7 protein
-
interacts with the catalytic domain of lysyl oxidase thereby preventing the crosslink of tropoelastin molecules into mature elastin polymers and regulating vascular elastogenesis
-
Zn2+
-
slightly inhibitory
2-mercaptopyridine-N-oxide
-
fully effective at 200 nM
2-mercaptopyridine-N-oxide
-
-
3-aminopropanenitrile
-
3-aminopropanenitrile
-
irreversible LOX inhibitor
3-aminopropanenitrile
-
-
beta-aminopropionitrile
-
80% inhibition at 0.5 mM
beta-aminopropionitrile
-
beta-aminopropionitrile
-
-
beta-aminopropionitrile
inhibition of LOXL-1
beta-aminopropionitrile
-
lathyrogen, organic nitrile group, blocks active site irreversibly and binds covalently
beta-aminopropionitrile
-
irreversible
beta-aminopropionitrile
-
total inhibition at 1 mM
beta-aminopropionitrile
-
-
beta-aminopropionitrile
-
selective inhibition of mammalian LOX
beta-aminopropionitrile
-
inhibition of active recombinant LOX, LOXL1, and LOXL2, specific
beta-aminopropionitrile
-
irreversible, competitive inhibitor
beta-aminopropionitrile
-
0.1-0.3 mM, specific inhibitor
beta-aminopropionitrile
-
0.5 mM
beta-aminopropionitrile
a specific lysyl oxidase inhibitor, diminishes the metastatic colonization potential of circulating breast cancer cells, detailed overview
beta-aminopropionitrile
a highly specific lysyl oxidase inhibitor that reportedly blocks LOX inhibition of Ras-induced oocyte maturation
beta-aminopropionitrile
a specific LOX inhibitor
beta-aminopropionitrile
-
LOX activity is inhibited by 0.5 mM and above concentrations
beta-aminopropionitrile
-
-
beta-aminopropionitrile
-
complete inhibition at 0.5 mM
beta-aminopropionitrile
-
competitive inhibitor
beta-aminopropionitrile
0.4 mM, 20% inhibition
beta-aminopropionitrile
-
selective inhibition of mammalian LOX
beta-aminopropionitrile
-
-
beta-aminopropionitrile
-
0.1 mM, irreversible inhibition
beta-aminopropionitrile
-
irreversible, competitive inhibitor
beta-aminopropionitrile
-
-
beta-aminopropionitrile
-
-
beta-aminopropionitrile
-
irreversible inhibitor
beta-aminopropionitrile
-
-
beta-aminopropionitrile
-
0.1 mM, irreversible inhibition
beta-aminopropionitrile
-
reduces LOX activity and significantly increases MCP-1 secretion in vascular smooth uscle cells
beta-aminopropionitrile
a highly specific lysyl oxidase inhibitor that reportedly blocks LOX inhibition of Ras-induced oocyte maturation
beta-aminopropionitrile
-
-
cycloheximide
-
inhibits incorporation of lysine and Cu2+ into enzyme, blocks activating process
cycloheximide
-
prevents stimulation by transforming growth factor-beta1
homocysteine
0.03 mM, up to 50% inhibition
homocysteine
-
down-regulates LOX mRNA and transcriptional activity
homocysteine
-
down-regulates LOX mRNA and transcriptional activity
homocysteine thiolactone
-
-
homocysteine thiolactone
-
-
homocysteine thiolactone
-
-
Isonicotinic acid hydrazide
-
lathyrogen, hydrazide group
Isonicotinic acid hydrazide
-
reversible, 61.8% of full activity restored by pyridoxal or 30.1% by pyrroloquinoline-quinone
low-density lipoprotein
-
decreases lysyl oxidase mRNA levels in endothelial cells
-
low-density lipoprotein
-
down-regulates LOX expression
-
low-density lipoprotein
-
-
-
low-density lipoprotein
-
-
-
phenylhydrazine
-
-
Semicarbazide
-
lathyrogen, ureide group
Semicarbazide
-
reversible, 21.2% of full activity restored by pyridoxal or 10% by pyrroloquinoline-quinone
TNFalpha
-
TNFalpha decreases LOX mRNA levels in endothelial cells in a dose- and time-dependent manner (2fold at 1 ng/ml and maximum at 2.5 ng/ml) and endothelial LOX enzymatic activity
-
TNFalpha
-
TNFalpha decreases LOX mRNA levels in endothelial cells in a dose- and time-dependent manner (2fold at 1 ng/ml and maximum at 2.5 ng/ml) and decreases endothelial LOX enzymatic activity
-
TNFalpha
-
TNFalpha decreases LOX mRNA levels in endothelial cells in a dose- and time-dependent manner (2fold at 1 ng/ml and maximum at 2.5 ng/ml) and endothelial LOX enzymatic activity
-
TNFalpha
-
TNFalpha decreases LOX mRNA levels in endothelial cells in a dose- and time-dependent manner (2fold at 1 ng/ml and maximum at 2.5 ng/ml) and endothelial LOX enzymatic activity
-
tumor necrosis factor-alpha
-
down-regulates LOX expression
-
tumor necrosis factor-alpha
-
inhibits LOX mRNA transcription and LOX activity
-
tumor necrosis factor-alpha
-
inhibits LOX mRNA transcription and LOX activity
-
additional information
-
no inhibition by dehydroascorbic acid
-
additional information
-
LOXL4 suppresses the expression of laminins and alpha3 integrin and the activity of matrix metalloproteinase-2
-
additional information
-
LOX propeptide expression in Her-2/neu-driven breast cancer cells in culture suppresses Akt, extracellular signal-regulated kinase, and nuclear factor-kappaB activation
-
additional information
-
not inhibited by berenil
-
additional information
-
not inhibited by berenil
-
additional information
-
TNF-alpha-stimulated matrix metalloproteinase-9 expression and Erk1/2 activation are both significantly inhibited by LOX-PP
-
additional information
-
hypercholesterolemia down-regulates LOX expression and activity
-
additional information
alkylamino derivatives of 4-aminomethylpyridine, substrate-like, reversible inhibitors
-
additional information
-
hypercholesterolemia down-regulates LOX expression and activity
-
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0.000126
(2-chloropyridin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000126
1-(2-chloropyridin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000385
1-(2-fluoropyridin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00118
1-(2-methoxypyridin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000309
1-(2-phenoxypyridin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000431
1-(3-fluoropyridin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.026
1-(4-fluorophenyl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.035
1-(4-methoxyphenyl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000719
1-(4-nitrophenyl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00122
1-(pyridin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00604
1-(quinolin-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000321
1-([2,3'-bipyridin]-4-yl)methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.0647
1-phenylmethanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000203
1-[2-(1H-imidazol-1-yl)pyridin-4-yl]methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000999
1-[2-(trifluoromethyl)pyridin-4-yl]methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00497
1-[3-(hydrazinylmethyl)phenyl]methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000902
1-[4-(1,3-thiazol-2-yl)phenyl]methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00111
1-[4-(hydrazinylmethyl)phenyl]methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.031
1-[5-(trifluoromethyl)[2,3'-bipyridin]-4-yl]methanamine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00821
2-(pyridin-4-yl)ethan-1-amine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.1
2-phenylcyclopropan-1-amine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.0601
2-phenylethan-1-amine
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.1
3,3'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dipropan-1-ol dihydrochloride
Sus scrofa
-
0.000066
3-aminopropanenitrile
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.1
4,4'-[[4-(aminomethyl)pyridine-3,5-diyl]bis(oxy)]dibutan-1-ol dihydrochloride
Sus scrofa
-
0.047
4-(aminomethyl)aniline
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00067
4-(aminomethyl)benzonitrile
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.000066
beta-aminopropionitrile
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00354
methyl 3-(aminomethyl)benzoate
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
0.00362
methyl 4-(aminomethyl)benzoate
Homo sapiens
-
LOXL2 protein, at pH 8.0 and 37°C
additional information
additional information
Sus scrofa
above 1.0 mM for 1-(3,5-diethoxypyridin-4-yl)methanamine dihydrochloride and 1-[3-(benzyloxy)-5-ethoxypyridin-4-yl]methanamine dihydrochloride
-
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-
-
brenda
-
-
brenda
-
LOX is highly expressed in early gestational amnion tissue (12-14 weeks)
brenda
-
highly expressed in vascular lesions
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
leg
brenda
-
-
brenda
-
mineral-associated fraction
brenda
-
-
brenda
-
LOX and LOXL
brenda
-
LOX and LOXL
brenda
-
-
brenda
-
-
brenda
-
LOX on the surface of pyramidal cells in the grey matter, LOXL in the nuclei of cortex cells and in the cytosol of capillary endothelial cells
brenda
-
-
brenda
-
localization of LOX and LOXL in different tissue areas
brenda
-
mature form of LOXL1 and polymerized LOXL1protein forms
brenda
-
-
brenda
-
polymerized LOXL1protein forms
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
of lung: LOX and LOXL, renal tubules: only LOXL, intestinal: only LOXL
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
of the stomach, mainly LOXL, mucous-secreting cells
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
including dermal papillae, follicular sheaths, sebaceous glands
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
pyramidal cells: LOXL, not LOX
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
epithelial cells, LOXL
brenda
-
mature form of LOXL1 and polymerized LOXL1protein forms
brenda
-
LOX and LOXL, of skin epidermis and hair follicles
brenda
-
-
brenda
-
determination of LOX activity and expression in donor ocular tissues
brenda
-
-
brenda
-
LOX gene expression is reduced in lung cancer cells
brenda
-
fetal
brenda
-
-
brenda
-
-
brenda
-
in MCF-10A normal breast epithelial cells stably expressing lysyl oxidase LOX has no effect on cell proliferation. Coexpression of lysyl oxidase and placental lactogen leads to a 121% increase in cell proliferation
brenda
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
polymerized LOXL1protein forms
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
LOX mRNA is upregulated in OSCC cells
brenda
-
-
brenda
-
-
brenda
-
LOX gene expression is reduced in pancreatic cancer cells
brenda
-
brenda
apparent lysyl oxidase isozymes contain a highly conserved LOX active site sequence in the nuclei of PC-12 cells
brenda
-
pepsin-secreting, in the basal part of the stomach, only LOX, no LOXL
brenda
-
-
brenda
-
-
brenda
-
LOXL2, LOX, LOXL
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
LOXL
brenda
-
determination of LOX activity and expression in donor ocular tissues
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
localization of LOX and LOXL in different tissue areas
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
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-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
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-
brenda
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-
brenda
-
-
brenda
-
-
brenda
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-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
proliferating cell, LOXL expression, adult tissues
brenda
-
determination of LOX activity and expression in donor ocular tissues
brenda
-
-
brenda
smooth muscle cells
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
LOX, LOXL, LOXL3, low expression level of LOXL2
brenda
-
co-localization of LOX and LOXL
brenda
-
-
brenda
-
-
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different spatial and temporal expression of LOX and LOXL1 during growth and aging, expression analysis of LOXL1 and LOX in the aorta during the development, growth, and aging of LOU rats, overview
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subluminal stroma surrounding the implanting blastocyst on day 5 of pregnancy
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subluminal stroma surrounding the implanting blastocyst on day 5 of pregnancy
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localization of LOX and LOXL in different tissue areas
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circulating
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lymph node-negative breast adenocarcinoma cell
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hypoxic
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co-localization of LOX and LOXL
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localization of LOX and LOXL in different tissue areas, LOXL is found in the apical surface of columnar absorbing cells, LOX is located in the submucosa
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from days 6 to 8 of pregnancy, the signals for Lox mRNA and protein are strongly detected in the decidual cells
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from days 6 to 8 of pregnancy, the signals for Lox mRNA and protein are strongly detected in the decidual cells
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LOXL-1
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LOXL-1, no expression of LOXL-2
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of skin: LOX and LOXL
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secretion of free soluble enzyme
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secretion of free soluble enzyme
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secretion of free soluble enzyme
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only in fetal heart, LOXL2, very low expression level of LOXL3
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lysyl oxidase protein expression is very scarce in normal hearts, it is highly expressed in failing hearts
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co-localization of LOX and LOXL
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overexpressed in head and neck squamous cell carcinoma compared to normal squamous epithelium
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LOXL4, LOX, LOXL
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localization of LOX and LOXL in different tissue areas
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LOXL-1
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LOXL-1, no expression of LOXL-2
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polymerized LOXL1protein forms
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co-localization of LOX and LOXL
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LOXL4, LOX, LOXL
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co-localization of LOX and LOXL in alveoli and the epithelia of bronchus and bronchiole
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osteoblastic cell, CRL-2593, expression of LOXL1, 3, and 4, not 2, expression patterns during cell differentiatin and matrix mineralization, 4 weeks, overview
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from mantle, fins and arms. Fins show the highest LOX activity
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expression of isozymes during osteoblast differentiation is highly regulated due to their distinct roles in collagen matrix stabilization and subsequent mineralization
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LOXL4, LOX, LOXL
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stromal tissue and ovarian follicle, polycystic ovarian tissue
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localization of LOX and LOXL in different tissue areas
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LOXL4, LOX, LOXL
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LOXL4, LOXL2, LOX, LOXL
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LOXL-1
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LOXL-1, no expression of LOXL-2
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localization of LOX and LOXL in different tissue areas, LOX is located in the inner surface of the pigmented epithelia in the photoreceptor layer, LOXL is located in the inner nuclear layer within the outer plexiform layer and in the ganglion cells
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extract obtained from dill stimulates the LOXL gene expression in dermal equivalents. The stimulation by the dill extract is correlated with increased elastin detection, suggesting an increase in elastogenesis efficiency
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co-localization of LOX and LOXL
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LOXL, lamia propria and straited border, not of Goblet cells
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neural crest- and mesoderm-derived smooth muscle
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nucleus
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LOXL4, LOX, LOXL
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localization of LOX and LOXL in different tissue areas
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LOXL2, LOX, LOXL
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additional information
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not expressed in the embryonic notochord
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additional information
adult fly: LOXL and LOXL-2, the latter occurs exclusively in adult flies, developmental expression analysis of LOX-like proteins LOXL and LOXL2 in embryos, larvae, pupae, and adult flies, no expression of LOXL-2 in larvae, pupae, and embryos, overview
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additional information
adult fly: LOXL and LOXL-2, the latter occurs exclusively in adult flies, developmental expression analysis of LOX-like proteins LOXL and LOXL2 in embryos, larvae, pupae, and adult flies, no expression of LOXL-2 in larvae, pupae, and embryos, overview
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additional information
adult fly: LOXL and LOXL-2, the latter occurs exclusively in adult flies, developmental expression analysis of LOX-like proteins LOXL and LOXL2 in embryos, larvae, pupae, and adult flies, overview
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additional information
adult fly: LOXL and LOXL-2, the latter occurs exclusively in adult flies, developmental expression analysis of LOX-like proteins LOXL and LOXL2 in embryos, larvae, pupae, and adult flies, overview
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additional information
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lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 show individual, developmentally regulated tissue and cell-specific expression and localization, expression patterns, LOX and LOXL are expressed in most tissues
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additional information
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no LOXL1 expression in retina
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additional information
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lysyl oxidase and 4 LOX-like proteins LOXL, LOXL2, LOXL3, and LOXL4 show individual, developmentally regulated tissue and cell-specific expression and localization
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additional information
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nearly no enzyme content in blood vessels, expression level of LOX and LOXL in different tissues during development from embryonic, newborn, and young to adult mice, overview
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additional information
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high aortic LOX expression early in the development, i.e. embryonic day 15, followed by a drastic reduction in adulthood, whereas LOXL1 is mainly detectable in the intima and media and is expressed throughout life in the LOU rat
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additional information
quantitative expression analysis of LOX isozymes in different subcellular compartments in PC-12 cells, overview
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drug target
the enzyme is a promising therapeutic target for the progression of cancer and fibrosis
evolution
J9NZK5
the protein is very well conserved throughout the course of evolution
malfunction
-
association between enzyme polymorphisms and oral submucous fibrosis in older male areca chewers
malfunction
-
excess collagen deposition in ovarian stroma in polycystic ovary syndrome involves increased enzyme activity due to stimulation by advenced glycation end products
malfunction
-
reduced enzyme expression is involved in the vitreous of proliferative diabetic retinopathy, PDR, and rhegmatogenous retinal detachment, RRD
malfunction
-
the enzyme regulates collagen cross-linking, which is increased in heart failure patients compared with healthy hearts. Enzyme overexpression is associated with enhanced collagen cross-linking in the failing human heart. Ability of torasemide to correct both lysyl oxidase overexpression and enhanced collagen cross-linking
malfunction
-
enzyme inhibition stops early mechanical development of tendon constructs and leads to irregularly shaped collagen fibrils
malfunction
-
inhibition of lysyl oxidase activity stabilizes oncogenic stress-induced senescence, delays tumorigenesis, and increases survival
metabolism
-
the enzyme is linked to crosslinking of elastin and collagen, it enhances tropoelastin crosslinking into matrix structures and elastin matrix yield, overview
metabolism
-
the enzyme is linked to crosslinking of elastin and collagen, it enhances tropoelastin crosslinking into matrix structures and elastin synthesis and matrix yield, overview
metabolism
-
by deacetylating and deacetyliminating Stat3 on multiple acetyl-lysine sites in nuclei, the enzyme regulates Stat3 dimerization and transcriptional activity. Furthermore, CD4+ T cell differentiation in inflammatory responses is regulated by the enzyme-Stat3 signaling pathway
metabolism
co-overexpression of specific protein 1 (SP1) and LOXL2 significantly correlates with poor prognosis in patients with pancreatic cancer
metabolism
the enzyme catalyzes cross-linking of collagen and elastin in the extracellular matrix
metabolism
-
the enzyme catalyzes cross-linking of collagen and elastin in the extracellular matrix
-
physiological function
-
LOX cross-links the side chain of collagen and elastin and thereby contributes to extracellular matrix integrity
physiological function
-
LOX is a copper-activated enzyme critical for collagen cross-linking and organization of extracellular matrix
physiological function
-
lysyl oxidase acts as both a matrix modifying enzyme and an oncogene suppressor
physiological function
-
lysyl oxidase is a copper-dependent amine oxidase that catalyzes the crosslinking of collagens and elastin, and is thus critical for the stability of the extracellular matrix. LOX mediates suppression of MCP-1, one of the highly upregulated chemokines, and subsequent inflammatory responses, overview
physiological function
-
lysyl oxidases play a critical role in matrix assembly by crosslinking elastin and collagen monomers into fibers
physiological function
-
overall survival rates of the patients with esophageal squamous cell carcinoma with high LOX expression are significantly lower than those of the patients with esophageal squamous cell carcinoma with low LOX expression
physiological function
-
role for lysyl oxidase-like, LOXL1, in adult elastin synthesis and a role for its isoform, lysyl oxidase, LOX, in the synthesis of both collagens and elastin during development. Specific roles for LOX and LOXL1 in the synthesis and remodeling of elastic and collagen fibers, overview
physiological function
-
the enzyme binds to mature TGF-beta1 and enzymatically regulates its signaling in bone and plays an important role in bone maintenance and remodeling
physiological function
-
the enzyme is involved n collagen synthesis. It catalyzes the collagen and elastin cross-linking and plays an essential role in coordinating the control of ovarian extracellular matrix during ovarian follicle development, overview
physiological function
-
the enzyme regulates collagen cross-linking
physiological function
the extracellular matrix remodeling enzyme has a role in promoting breast cancer cell motility and invasiveness. LOX activity is required during extravasation and/or initial tissue colonization by circulating MDA-MB-231 cells, metastasis model and drug administration study in mice, overview
physiological function
LOX is the principal enzyme involved in crosslinking of collagen. Nuclear lysyl oxidase probably regulates nuclear growth, and thereby modulates cell proliferation, overview
physiological function
LOX is the principal enzyme involved in crosslinking of collagen. Nuclear lysyl oxidase probably regulates nuclear growth, and thereby modulates cell proliferation, overview
physiological function
the enzyme induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion
physiological function
-
the lysyl oxidases LOX and LOXL2 are necessary and sufficient to repress E-cadherin in hypoxia, thereby inducing epithelial to mesenchymal transition
physiological function
-
enzyme activity contributes to collagen stabilization during liver fibrosis progression and limits spontaneous fibrosis reversal
physiological function
-
lysyl oxidase activity is required for ordered collagen fibrillogenesis by tendon cells
physiological function
-
the enzyme participates in primary tumor growth by directly impacting the senescence stability
physiological function
-
the enzyme restricts Stat3-dependent cell proliferation and immune cell differentiation and inflammatory response
physiological function
crucial role of Lox in endometrial stromal cells
physiological function
J9NZK5
role in interlinking of collagen and elastin by oxidizing lysine residues
physiological function
the enzyme catalyzes the oxidative deamination of lysine residues of extracellular matrix proteins such as elastins and collagens and generate aldehyde groups. The oxidative deamination of lysine represents the foundational step for the cross-linking of elastin and collagen and thus is crucial for modeling of extracellular matrix
physiological function
-
crucial role of Lox in endometrial stromal cells
-
additional information
LOX expression opposes the effect of mutationally activated Ras, which is present in about 30% of human cancers. Proliferating cells dramatically increase their nuclear protein content when exposed to beta-aminopropionitrile, a highly specific lysyl oxidase inhibitor that reportedly blocks LOX inhibition of Ras-induced oocyte maturation
additional information
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LOX expression opposes the effect of mutationally activated Ras, which is present in about 30% of human cancers. Proliferating cells dramatically increase their nuclear protein content when exposed to beta-aminopropionitrile, a highly specific lysyl oxidase inhibitor that reportedly blocks LOX inhibition of Ras-induced oocyte maturation
additional information
LOX is a hypoxia-inducible amine oxidase, the activity of which enhances breast cancer cell invasion in vitro and in vivo. Specific inhibition of LOX activity by beta-aminopropionitrile or small interfering RNA decreased the invasiveness of T-47D and MCF-7 breast cancer cells attenuated for Pdcd4 function. Tumor suppressor Pdcd4 inhibits breast cancer cell migration and invasion in vitro. Loss of Pdcd4 in human nonmetastatic breast cancer cells increases the expression of lysyl oxidase mRNA
additional information
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LOX is a hypoxia-inducible amine oxidase, the activity of which enhances breast cancer cell invasion in vitro and in vivo. Specific inhibition of LOX activity by beta-aminopropionitrile or small interfering RNA decreased the invasiveness of T-47D and MCF-7 breast cancer cells attenuated for Pdcd4 function. Tumor suppressor Pdcd4 inhibits breast cancer cell migration and invasion in vitro. Loss of Pdcd4 in human nonmetastatic breast cancer cells increases the expression of lysyl oxidase mRNA
additional information
-
lysyl oxidase inhibitor, beta-aminopropionitrile, diminishes the metastatic colonization potential of circulating breast cancer cells, detailed overview. LOX inhibition might be useful in metastasis prevention
additional information
lysyl oxidase inhibitor, beta-aminopropionitrile, diminishes the metastatic colonization potential of circulating breast cancer cells, detailed overview. LOX inhibition might be useful in metastasis prevention
additional information
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partial knockdown of three LOX genes, lox,loxl1 and loxl5b, sensitizes the developing embryo to dithiocarbamate exposure
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130000
-
polymerized LOXL1 precursor protein, SDS-PAGE
36000
-
x * 36000, recombinant processed LOX, SDS-PAGE, x * 51000, recombinant processed LOXL1, SDS-PAGE, x * 29000, recombinant processed LOXL2, SDS-PAGE
42000
-
mature enzyme, SDS-PAGE
49500
x * 49500, calculated from amino acid sequence
51000
-
x * 36000, recombinant processed LOX, SDS-PAGE, x * 51000, recombinant processed LOXL1, SDS-PAGE, x * 29000, recombinant processed LOXL2, SDS-PAGE
52000
-
x * 52000, extracellular LOXL, SDS-PAGE
59000
-
x * 59000, x * 61000, SDS-PAGE, may be isoenzymes or heterologous subunits
60000
-
x * 60000, SDS-PAGE
61000
-
x * 59000, x * 61000, SDS-PAGE, may be isoenzymes or heterologous subunits
80000
-
polymerized enzyme, SDS-PAGE
83600
x * 97000, including V5-epitope and histidine tag of 2.3 kDa, Western-Blot, x * 83600, calculated
85000
-
predicted molecular mass
97000
x * 97000, including V5-epitope and histidine tag of 2.3 kDa, Western-Blot, x * 83600, calculated
18000
-
LOX propeptide, SDS-PAGE
18000
-
x * 34000, recombinant mature LOX, SDS-PAGE, x * 18000, recombinant C-terminally deleted LOX, SDS-PAGE
28000
-
x * 28000, SDS-PAGE
28000
-
x * 46000, proenzyme form, DNA sequence calculation, x * 28000, active enzyme, SDS-PAGE
29000
SDS-PAGE
29000
-
x * 36000, recombinant processed LOX, SDS-PAGE, x * 51000, recombinant processed LOXL1, SDS-PAGE, x * 29000, recombinant processed LOXL2, SDS-PAGE
29000
-
x * 29000, active mature protein
30000
-
mature enzyme, SDS-PAGE
30000
-
mature enzyme, SDS-PAGE
30000
-
x * 30000, SDS-PAGE
32000
-
active enzyme, SDS-PAGE
32000
-
active enzyme, SDS-PAGE
32000
-
mature enzyme, SDS-PAGE
32000
-
mature enzyme, SDS-PAGE
32000
-
mature and catalytically active enzyme, SDS-PAGE
32000
-
mature LOX, SDS-PAGE
32000
-
mature LOX, SDS-PAGE
32000
-
ProLOX is subsequently cleaved into its catalytically mature 32000Da protein (LOX) and an 18000 Da LOX-propeptide
32000
-
ProLOX is subsequently cleaved into its catalytically mature 32000Da protein (LOX) and an 18000 Da LOX-propeptide
32000
-
x * 46000, predicted, x * 32000, SDS-PAGE
32000
-
x * 32000, catalytically active enzyme after proteolytic cleavage
32000
-
x * 32000, catalytically active enzyme after proteolytic cleavage
32000
-
x * 32000, active enzyme, SDS-PAGE
32000
-
x * 50000, proenzyme form, DNA sequence calculation, x * 32000, active enzyme, SDS-PAGE
34000
-
x * 34000, SDS-PAGE
34000
-
x * 34000, recombinant mature LOX, SDS-PAGE, x * 18000, recombinant C-terminally deleted LOX, SDS-PAGE
34000
-
truncated enzyme without the N-terminal peptide, SDS-PAGE
35000
-
LOX propeptide, SDS-PAGE
35000
-
x * 35000, SDS-PAGE
46000
J9NZK5
-
46000
-
x * 46000, predicted, x * 32000, SDS-PAGE
46000
-
x * 46000, proenzyme form, DNA sequence calculation, x * 28000, active enzyme, SDS-PAGE
46000
-
x * 46000, LOXL3-sv1, SDS-PAGE
50000
-
proenzyme, SDS-PAGE
50000
-
immature enzyme, SDS-PAGE
50000
-
glycosylated immature protein, SDS-PAGE
50000
-
immature proLOX, SDS-PAGE
50000
-
inactive proenzyme, SDS-PAGE
50000
-
N-glycosylated and secreted from the cell as a catalytically inactive 50000 Da proenzyme protein (proLOX)
50000
-
N-glycosylated and secreted from the cell as a catalytically inactive 50000 Da proenzyme protein (proLOX)
50000
-
precursor Pro-LOX, SDS-PAGE
50000
-
x * 50000, preproprotein
50000
-
x * 50000, proenzyme form, DNA sequence calculation, x * 32000, active enzyme, SDS-PAGE
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dimer
-
homodimer, subunit interface structure, overview
?
-
x * 34000, SDS-PAGE
?
-
x * 46000, predicted, x * 32000, SDS-PAGE
?
-
x * 32000, active enzyme, SDS-PAGE
?
-
x * 59000, x * 61000, SDS-PAGE, may be isoenzymes or heterologous subunits
?
x * 97000, including V5-epitope and histidine tag of 2.3 kDa, Western-Blot, x * 83600, calculated
?
-
x * 34000, recombinant mature LOX, SDS-PAGE, x * 18000, recombinant C-terminally deleted LOX, SDS-PAGE
?
-
x * 36000, recombinant processed LOX, SDS-PAGE, x * 51000, recombinant processed LOXL1, SDS-PAGE, x * 29000, recombinant processed LOXL2, SDS-PAGE
?
-
x * 46000, proenzyme form, DNA sequence calculation, x * 28000, active enzyme, SDS-PAGE
?
-
x * 46000, LOXL3-sv1, SDS-PAGE
?
-
x * 29000, active mature protein
?
x * 49500, calculated from amino acid sequence
?
-
x * 29000, active mature enzyme, SDS-PAGE
?
-
x * 30000, LOX protein, SDS-PAGE
?
-
x * 50000, pre-proenzyme, SDS-PAGE
?
-
x * 80000, LOXL2 protein, SDS-PAGE
?
-
x * 32000, catalytically active enzyme after proteolytic cleavage
?
-
x * 50000, preproprotein
?
-
x * 52000, extracellular LOXL, SDS-PAGE
?
-
x * 32000, catalytically active enzyme after proteolytic cleavage
?
-
x * 50000, proenzyme form, DNA sequence calculation, x * 32000, active enzyme, SDS-PAGE
additional information
-
structural implications of primary sequence, overview
additional information
domain structure of LOX-like protein
additional information
domain structure of LOX-like protein
additional information
domain structure of LOX-like protein, LOXL-1 and LOXL-2 contain SRCR domains
additional information
domain structure of LOX-like protein, LOXL-1 and LOXL-2 contain SRCR domains
additional information
-
different molecular forms of enzyme exist
additional information
-
domain structure, overview
additional information
-
structural implications of primary sequence, profile of ionic residues in LO and LOXL-1, overview
additional information
-
the enzymes contain SRCR domains
additional information
-
the enzymes' tertiary and quarternary fold is similar but the active site structure is more exposed and accesible compared to the structure of other quinone-containing copper amine oxidases
additional information
-
LOX and LOXL are immunologically distinct, specific antibodies do not cross-react
additional information
-
structural implications of primary sequence, profile of ionic residues, overview
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