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(2E)-3-(1-benzofuran-2-yl)prop-2-enoic acid
-
-
(2E)-3-(1-benzofuran-3-yl)prop-2-enoic acid
-
-
(2E)-3-(1-benzothiophen-2-yl)prop-2-enoic acid
-
-
(2E)-3-(1-benzothiophen-3-yl)prop-2-enoic acid
-
-
(2E)-3-(1-methyl-1H-indol-3-yl)prop-2-enoic acid
-
-
(2E)-3-(1H-indol-3-yl)prop-2-enoic acid
-
-
(2E)-3-(3-methylfuran-2-yl)prop-2-enoic acid
-
-
(2E)-3-(3-methylthiophen-2-yl)prop-2-enoic acid
-
-
(2E)-3-furan-2-ylprop-2-enoic acid
-
-
(2E)-3-thiophen-2-ylprop-2-enoic acid
-
-
1,2,4-triazole-DL-alanine
Achromobacter liquidum
-
competitive
1-amino-2-imidazol-4'-ylethylphosphonic acid
-
reversible, competitive, 1 mM: complete inhibition
2-mercaptoethanol
-
inhibition at concentrations above 10 mM, reversed by addition of metal ion
2-methyl-DL-histidine
Achromobacter liquidum
-
competitive
2-thiazolyl-DL-alanine
Achromobacter liquidum
-
competitive
3-(1-benzofuran-2-yl)alanine
-
-
3-(1-benzofuran-3-yl)alanine
-
-
3-(1-benzothiophen-2-yl)alanine
-
-
3-(1-benzothiophen-3-yl)alanine
-
-
3-(3-methylthiophen-2-yl)alanine
-
-
3-methyl-L-histidine
Achromobacter liquidum
-
competitive
3-thiophen-2-ylalanine
-
-
4-nitro-L-histidine
-
competitive
5,5'-dithiobis(2-nitrobenzoic acid)
8-methoxypsoralen
-
noncompetitive. Irradiation of 8-methoxypsoralen with broadband UVA and broadband UVA/UVB results in uncompetitive inhibition due to psoralen-oxidized photoproducts
all-trans retinoic acid
-
1 microM suppresses histidase expression almost completely, levels of histidase mRNA expression in the presence of all-trans retinoic acid are significantly lower on day 2 of post-confluence and at all later time points during keratinocyte differentiation
alpha-methyl-DL-histidine
Achromobacter liquidum
-
competitive
Ba2+
Achromobacter liquidum
-
1 mM
beta-imidazole lactic acid
Achromobacter liquidum
-
competitive
Co3+
-
0.1 mM, 95% inhibition
Cu2+
-
0.1 mM, 70% inhibition
cyanide
-
50 mM histidinol phosphate, 5 mM L-histidine and 5 mM Mn2+ protects
D-alpha-hydrazinohistidine
-
competitive
D-alpha-hydrazinoimidazolylpropionic acid
D-cysteine
-
in the presence of Cd2+
DL-alpha-hydrazinoimidazolylpropionic acid
-
70% irreversible inactivation in vivo
DL-pyrazolyl-3-alanine
-
5.0 mM
Fe2+
-
0.1 mM, 60% inhibition
formyl-L-histidine
Achromobacter liquidum
-
competitive
H2O2
Achromobacter liquidum
-
-
histidinol phosphate
-
competitive
hydroxymethylimidazole
Achromobacter liquidum
-
competitive
-
imidazol-3-ylpyruvate
-
uncompetitive
imidazole
Achromobacter liquidum
-
noncompetitive
interleukin-1alpha
-
treatment of IL-1a reduces histidase expression, the suppressive effect can be reverted by concomitant treatment with interleukin-1alpha receptor antagonist
-
L-1-methylhistidine
-
5.0 mM
L-alpha-hydrazinoimidazolylpropionic acid
-
competitive
L-histidine hydrazide
Achromobacter liquidum
-
noncompetitive
L-homocysteine
-
irreversible in the presence of O2 and high pH
L-N-gamma-methylhistidine
-
weak competitive
L-tyrosine
-
heat-purified enzyme, at low concentrations, pH 7-8
N-acetyl-L-histidine
-
5.0 mM
N-ethylmaleimide
-
1 mM, partial
p-hydroxyphenylpyruvate
-
heat-purified enzyme, at low concentrations, pH 7-8
Pb2+
Achromobacter liquidum
-
1 mM
Phenylglyoxal
-
protection by histidinol phosphate
TGF-alpha
-
most pronounced effect, leads to almost complete suppression of histidase expression
-
TNF-alpha
-
suppresses the expression of histidase
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
protection of reduced enzyme by Cd2+ against inactivation
5-fluoro-L-histidine
-
competitive
5-fluoro-L-histidine
-
competitive
bisulfite
-
-
bisulfite
-
10 mM, 95% loss of activity after 90 min, 0.1 mM 1-amino-2-imidazol-4'-ylethylphosphoric acid protects
bisulfite
-
sodiumbisulfite
CN-
-
0.01 M, 40% inhibition
D-alpha-hydrazinoimidazolylpropionic acid
-
strong
D-alpha-hydrazinoimidazolylpropionic acid
-
inactivates in vivo
D-histidine
-
competitive
D-histidine
-
competitive
D-histidine
-
cloned enzyme, reversible competitive
D-histidine
-
competitive
D-histidine
-
competitive
dithiothreitol
-
-
dithiothreitol
-
20 mM, liver and epidermal enzyme, restored by addition with Zn2+
EDTA
-
0.001 mM: 50% inhibition, 0.01 mM, complete inhibition
EDTA
-
0.04 mM, liver and epidermal enzyme, restored by incubation with Zn2+
EDTA
-
0.005 mM, 75% decrease of activity
EDTA
-
potent inhibitor of the reduced enzyme; reduced enzyme
EDTA
-
reversed by addition of divalent cations
EDTA
-
reversed by addition of divalent cations
Fe3+
Achromobacter liquidum
-
1 mM
Fe3+
-
0.1 mM, 60% inhibition
glycine
-
0.02 M glycine buffer, 40% inhibition. Inhibition can be overcome by addition of cations, including Mn2+, Ca2+, and Mg2+
L-cysteine
Achromobacter liquidum
-
-
L-cysteine
-
competitive, cloned enzyme
L-cysteine
-
irreversible
L-cysteine
-
irreversible in the presence of O2
L-cysteine
10 mM, irreversible inactivation
L-cysteine
-
10 mM, complete inactivation after 3 h under aerobic conditions
L-cysteine
-
50 mM, complete inaction at basic pH in the presence of O2 is due to a covalent modification of the enzyme
L-cysteine
10 mM, complete inactivation at pH higher than 10 in the presence of O2
L-cysteine
-
competitive in the presence of EDTA; in the presence of Cd2+; irreversible in the presence of O2
L-histidine hydroxamate
Achromobacter liquidum
-
competitive
L-histidine hydroxamate
-
competitive
L-histidine hydroxamate
-
competitive
L-histidine hydroxamate
-
competitive; strong
L-histidinemethyl ester
Achromobacter liquidum
-
-
L-histidinemethyl ester
-
-
L-histidinemethyl ester
-
5.0 mM
L-histidinol
Achromobacter liquidum
-
competitive
L-histidinol
-
competitive
NaBH4
Achromobacter liquidum
-
-
Nitromethane
-
-
Nitromethane
-
inactivates enzyme in vivo
p-mercuribenzoate
-
inhibits mercaptoethanol-activated enzyme
p-mercuribenzoate
-
0.01 mM, complete inhibition, partially reversed by addition of histidine
Urocanate
-
-
Urocanate
-
heat-purified enzyme, at low concentrations, pH 7-8
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
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Consevage, M.W.; Porter, R.D.; Phillips, A.T.
Cloning and expression in Escherichia coli of histidine utilization genes from Pseudomonas putida
J. Bacteriol.
162
138-146
1985
Pseudomonas putida
brenda
Hanson, K.R.; Havir, E.A.
The enzymic elimination of ammonia
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
7
75-166
1972
Klebsiella aerogenes, Bacillus subtilis, Comamonas testosteroni, Homo sapiens, Pseudomonas sp., Pseudomonas aeruginosa, Pseudomonas fluorescens, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium, toad, Pseudomonas fluorescens A.3.12
-
brenda
Mehler, A.H.; Tabor, H.
Deamination of histidine to form urocanic acid in liver
J. Biol. Chem.
201
775-784
1953
Cavia porcellus, Pseudomonas fluorescens
brenda
Klee, C.B.
Metal activation of histidine ammonia-lyase. Metal ion-sulfhydryl group relationship
J. Biol. Chem.
247
1398-1406
1972
Pseudomonas sp.
brenda
Klee, C.B.
Histidine ammonia-lyase (Pseudomonas)
Methods Enzymol.
17B
69-73
1971
Pseudomonas sp.
-
brenda
Rechler, M.M.; Tabor, H.
Histidine ammonia-lyase (Pseudomonas)
Methods Enzymol.
17B
63-69
1971
Pseudomonas sp., Pseudomonas aeruginosa, Pseudomonas putida
-
brenda
Magasanik, B.; Kaminskas, E.; Kimhi, Y.
Histidase (histidine ammonia-lyase) (Bacillus subtilis)
Methods Enzymol.
17B
47-50
1971
Klebsiella aerogenes, Bacillus subtilis, Salmonella enterica subsp. enterica serovar Typhimurium, Bacillus subtilis W23G
-
brenda
Hassall, H.
Use of L-histidine ammonia-lyase for the determination of L-histidine
Methods Enzymol.
17B
895-897
1971
Homo sapiens, Pseudomonas sp., Pseudomonas putida
-
brenda
La Du, B.N.
L-Histidine ammonia-lyase (human stratum corneum)
Methods Enzymol.
17B
891-894
1971
Homo sapiens
-
brenda
Morris, M.L.; Lee, S.C.; Harper, A.E.
Influence of differential induction of histidine catabolic enzymes on histidine degradation in vivo
J. Biol. Chem.
247
5793-5804
1972
Rattus norvegicus
brenda
Hug, D.H.; Hunter, J.K.
Effect of temperature on histidine ammonia-lyase from a psychrophile, Pseudomonas putida
J. Bacteriol.
119
92-97
1974
Pseudomonas putida, Rattus norvegicus, Pseudomonas putida A.3.12
brenda
Okamura, H.; Nishida, T.; Nakagawa, H.
L-histidine ammonia-lyase in rat liver. I. Purification and general characteristics
J. Biochem.
75
139-152
1974
Cavia porcellus, Rattus norvegicus
brenda
Klee, C.B.
Stereospecific irreversible inhibition of histidine ammonia-lyase by L-cysteine
Biochemistry
13
4501-4507
1974
Pseudomonas sp.
brenda
Klee, C.B.; Kirk, K.L.; Cohen, L.A.; McPhie, P.
Histidine ammonia-lyase. The use of 4-fluorohistidine in identification of the rate-determining step
J. Biol. Chem.
250
5033-5040
1975
Pseudomonas sp.
brenda
Shibatani, T.; Kakimoto, T.; Chibata, I.
Crystalline L-histidine ammonia-lyase of Achromobacter liquidum. Crystallization and enzymic properties
Eur. J. Biochem.
55
263-269
1975
Achromobacter liquidum, Bacillus cereus, Bacillus subtilis, Comamonas testosteroni, Helianthus sp., Mycobacterium avium, Pseudomonas sp., Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas fluorescens, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium, Spinacia oleracea, Vibrio cholerae serotype O1, Achromobacter liquidum IAM 1667
brenda
Brand, L.M.; Harper, A.E.
Histidine ammonia-lyase from rat liver. Purification, properties, and inhibition by substrate analogues
Biochemistry
15
1814-1821
1976
Pseudomonas fluorescens, Rattus norvegicus
brenda
Brand L.M.; Harper, A.E.
DL-alpha-Hydrazinoimidazolylpropionic acid: an irreversible inhibitor of hepatic histidine ammonia-lyase in vivo
Arch. Biochem. Biophys.
177
123-132
1976
Rattus norvegicus
brenda
Kamel, M.Y.; Maksoud, S.A.
Co-factor requirements and factors affecting L-histidine ammonia-lyase activity in Vicia faba
Z. Pflanzenphysiol.
88
255-262
1978
Vicia faba
-
brenda
Walters, R.R.; Johnson, P.A.; Buck, R.P.
Histidine ammonia-lyase enzyme electrode for determination of L-histidine
Anal. Chem.
52
1684-1690
1980
Pseudomonas sp.
-
brenda
Polkinghorne, M.A.; Hynes, M.J.
L-Histidine utilization in Aspergillus nidulans
J. Bacteriol.
149
931-940
1982
Aspergillus nidulans
brenda
Allen, R.L.; Clark, N.J.; Phipps, D.A.
Histidine ammonia-lyase from kidney of rainbow trout (Salmo gairdnerii Richardson)
Biochem. Soc. Trans.
11
350
1983
Scombridae, Oncorhynchus mykiss
-
brenda
Allen, R.L.; Hopewell, R.; Prottey, C.
Histidine ammonia-lyase in guinea-pig liver and epidermis
Biochem. Soc. Trans.
11
349-350
1983
Cavia porcellus
-
brenda
Fuchs, R.L.; Kane, J.F.
In vivo synthesis of histidine by a cloned histidine ammonia-lyase in Escherichia coli
J. Bacteriol.
162
98-101
1985
Klebsiella pneumoniae subsp. pneumoniae
brenda
Oda, M.; Sugishita, A.; Furukawa, K.
Cloning and nucleotide sequences of histidase and regulatory genes in the Bacillus subtilis hut operon and positive regulation of the operon
J. Bacteriol.
170
3199-3205
1988
Bacillus subtilis, Bacillus subtilis Marburg 168
brenda
Kroening, T.A.; Kendrick, K.E.
Cascading regulation of histidase activity in Streptomyces griseus
J. Bacteriol.
171
1100-1105
1989
Streptomyces griseus
brenda
Khanna, R.; Chang, T.M.S.
Characterization of L-histidine ammonia-lyase immobilized by microencapsulation in artificial cells: preparation, kinetics, stability, and in vitro depletion of histidine
Int. J. Artif. Organs
13
189-195
1990
Pseudomonas fluorescens
brenda
Burton, D.L.; McGill, W.B.
Inductive and repressive effects of carbon and nitrogen on L-histidine ammonia-lyase activity in a black chernozemic soil
Soil Biol. Biochem.
23
939-946
1991
unidentified
brenda
Wu, P.C.; Kroening, T.A.; White, P.J.; Kendrick, K.E.
Histidine ammonia-lyase from Streptomyces griseus
Gene
115
19-25
1992
Streptomyces griseus, Streptomyces griseus NRRL B-2682
brenda
Hernandez, D.; Phillips, A.T.
Purification and Characterization of Pseudomonas putida histidine ammonia-lyase expressed in Escherichia coli
Protein Expr. Purif.
4
473-478
1993
Pseudomonas sp., Pseudomonas putida, Pseudomonas putida PRS1
brenda
White, P.J.; Kendrick, K.E.
Inactivation of histidine ammonia-lyase from Streptomyces griseus by dicarbonyl reagents
Biochim. Biophys. Acta
1163
273-279
1993
Streptomyces griseus
brenda
Ahmed, H.K.; Mitchell, W.J.; Priest, F.G.
Catabolite repression of histidase biosynthesis in Bacillus sphaericus by acetate
FEMS Microbiol. Lett.
106
71-75
1993
Bacillus subtilis, Lysinibacillus sphaericus, Klebsiella pneumoniae subsp. pneumoniae, Lysinibacillus sphaericus 2362
-
brenda
Hernandez, D.; Phillips, A.T.; Zon, J.
1-amino-2-imidazol-4 -ylethylphosphonic acid is a potent reversible inhibitor of Pseudomonas putida histidine ammonia-lyase
Biochem. Mol. Biol. Int.
32
189-194
1994
Pseudomonas putida
brenda
Hernandez, D.; Phillips, A.T.
Ser-143 is an essential active site residue in histidine ammonia-lyase of Pseudomonas putida
Biochem. Biophys. Res. Commun.
201
1433-1438
1994
Pseudomonas putida
brenda
Weber, K.; Retey, J.
On the nature of the irreversible inhibition of histidine ammonia lyase by cysteine and dioxygen
Bioorg. Med. Chem.
4
1001-1006
1996
Pseudomonas putida
brenda
Sano, H.; Tada, T.; Moriyama, A.; Ogawa, H.; Asai, K.; Kawai, Y.; Hodgson, M.E.; Kato, T.; Wada, Y.; Suchi, M.
Isolation of a rat histidase cDNA sequence and expression in Escherichia coli--evidence of extrahepatic/epidermal distribution
Eur. J. Biochem.
250
212-221
1997
Mus musculus, Rattus norvegicus
brenda
Schwede, T.F.; Baedeker, M.; Langer, M.; Retey, J.; Schulz, G.E.
Homogenization and crystallization of histidine ammonia-lyase by exchange of a surface cysteine residue
Protein Eng.
12
151-153
1999
Pseudomonas putida
brenda
Schwede, T.F.; Retey, J.; Schulz, G.E.
Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile
Biochemistry
38
5355-5361
1999
Pseudomonas putida (P21310), Pseudomonas putida
brenda
Rother, D.; Poppe, L.; Viergutz, S.; Langer, B.; Retey, J.
Characterization of the active site of histidine ammonia-lyase from Pseudomonas putida
Eur. J. Biochem.
268
6011-6019
2001
Pseudomonas putida (P21310), Pseudomonas putida
brenda
Merkel, D.; Retey, J.
Further insight into the mechanism of the irreversible inhibition of histidine ammonia-lyase by L-cysteine and dioxygen
Helv. Chim. Acta
83
1151-1160
2000
Pseudomonas putida
-
brenda
Galpin, J.D.; Ellis, B.E.; Tanner, M.E.
The Inactivation of Histidine Ammonia-Lyase by L-Cysteine and Oxygen: Modification of the Electrophilic Center
J. Am. Chem. Soc.
121
10840-10841
1999
Pseudomonas putida
-
brenda
Donnelly, M.; Fedeles, F.; Wirstam, M.; Siegbahn, P.E.; Zimmer, M.
Computational analysis of the autocatalytic posttranslational cyclization observed in histidine ammonia-lyase. A comparison with green fluorescent protein
J. Am. Chem. Soc.
123
4679-4686
2001
Homo sapiens
brenda
Ascencio, C.; Tovar, A.R.; Medina-Campos, O.N.; Pedraza-Chaverri, J.; Torres, N.
Hepatic histidase and muscle branched chain aminotransferase gene expression in experimental nephrosis
Life Sci.
67
2775-2784
2000
Rattus norvegicus
brenda
Baedeker, M.; Schulz, G.E.
Autocatalytic peptide cyclization during chain folding of histidine ammonia-lyase
Structure
10
61-67
2002
Pseudomonas putida (P21310)
brenda
Asano, Y.; Kato, Y.; Levy, C.; Baker, P.; Rice, D.
Structure and Function of Amino Acid Ammonia-lyases
Biocatal. Biotransform.
22
131-138
2004
Pseudomonas putida
-
brenda
Kawai, Y.; Moriyama, A.; Asai, K.; Coleman-Campbell, C.M.; Sumi, S.; Morishita, H.; Suchi, M.
Molecular characterization of histidinemia: identification of four missense mutations in the histidase gene
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116
340-346
2005
Homo sapiens
brenda
Hellio, C.; Veron, B.; Le Gal, Y.
Amino acid utilization by Chlamydomonas reinhardtii: Specific study of histidine
Plant Physiol. Biochem.
42
257-264
2004
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii CCAP 11/32A
brenda
Ortiz, V.; Torres, N.; Tovar, A.R.
Production of recombinant rat hepatic histidase
Rev. Invest. Clin.
56
43-50
2004
Rattus norvegicus
brenda
Katona, A.; Tosa, M.I.; Paizs, C.; Retey, J.
Inhibition of histidine ammonia lyase by heteroaryl-alanines and acrylates
Chem. Biodivers.
3
502-508
2006
Pseudomonas putida
brenda
Welsh, M.M.; Karagas, M.R.; Applebaum, K.M.; Spencer, S.K.; Perry, A.E.; Nelson, H.H.
A role for ultraviolet radiation immunosuppression in non-melanoma skin cancer as evidenced by gene-environment interactions
Carcinogenesis
29
1950-1954
2008
Homo sapiens
brenda
Eckhart, L.; Schmidt, M.; Mildner, M.; Mlitz, V.; Abtin, A.; Ballaun, C.; Fischer, H.; Mrass, P.; Tschachler, E.
Histidase expression in human epidermal keratinocytes: regulation by differentiation status and all-trans retinoic acid
J. Dermatol. Sci.
50
209-215
2008
Homo sapiens
brenda
Seff, A.L.; Pilbak, S.; Silaghi-Dumitrescu, I.; Poppe, L.
Computational investigation of the histidine ammonia-lyase reaction: a modified loop conformation and the role of the zinc(II) ion
J. Mol. Model.
17
1551-1563
2011
Pseudomonas putida
brenda
Reilly, J.T.; Troester, K.A.; Tyner, T.T.; Vitale, D.A.; Risher, T.R.
Inhibition of histidine ammonia lyase by 8-methoxypsoralen and psoralen-oxidized photoproducts
Photochem. Photobiol.
86
1272-1277
2010
Pseudomonas putida
brenda
Luu, N.; Wen, L.; Fu, L.; Fujimoto, K.; Shi, Y.B.; Sun, G.
Differential regulation of two histidine ammonia-lyase genes during Xenopus development implicates distinct functions during thyroid hormone-induced formation of adult stem cells
Cell Biosci.
3
43
2013
Xenopus tropicalis (F6RBJ7), Xenopus tropicalis (Q6AZU6), Xenopus laevis (Q0VGW8), Xenopus laevis (Q6AZU6), Xenopus laevis
brenda
Sanchez-Murcia, P.A.; Bueren-Calabuig, J.A.; Camacho-Artacho, M.; Cortes-Cabrera, A.; Gago, F.
Stepwise simulation of 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) biogenesis in histidine ammonia-lyase
Biochemistry
55
5854-5864
2016
Pseudomonas putida (P21310), Pseudomonas putida
brenda
Yamaguchi, K.; Zhu, C.; Ohsugi, T.; Yamaguchi, Y.; Ikenoue, T.; Furukawa, Y.
Bidirectional reporter assay using HAL promoter and TOPFLASH improves specificity in high-throughput screening of Wnt inhibitors
Biotechnol. Bioeng.
114
2868-2882
2017
Homo sapiens (P42357)
brenda
Luu, N.; Fu, L.; Fujimoto, K.; Shi, Y.B.
Direct regulation of histidine ammonia-lyase 2 gene by thyroid hormone in the developing adult intestinal stem cells
Endocrinology
158
1022-1033
2017
Xenopus tropicalis (F6RBJ7), Xenopus laevis (Q0VGW8), Xenopus laevis
brenda