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Literature summary for 1.2.1.8 extracted from

  • Munoz-Bacasehua, C.; Rosas-Rodriguez, J.; Arvizu-Flores, A.; Stephens-Camacho, A.; Sonanez-Organis, J.; Figueroa-Soto, C.; Valenzuela-Soto, E.
    Heterogeneity of active sites in recombinant betaine aldehyde dehydrogenase is modulated by potassium (2020), J. Mol. Recognit., 33, e2869 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene BADH, sequence comparisons, recombinant expression of the enzyme in Escherichia coli strain ER2566 Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information thermodynamcis Sus scrofa

Metals/Ions

Metals/Ions Comment Organism Structure
K+ presence of K+ stabilizes the enzyme secondary structure and maintains its alpha-helix content. K+ increases the thermal stability of the pkBADHNAD+ complex by 5.3°C Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
224000
-
recombinant enzyme, gel filtration Sus scrofa
232000
-
recombinant enzyme, native PAGE Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
betaine aldehyde + NAD+ + H2O Sus scrofa
-
betaine + NADH + 2 H+
-
?

Organism

Organism UniProt Comment Textmining
Sus scrofa A0A6M5K8J2
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain ER2566 by chitin affinity chromatography Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
betaine aldehyde + NAD+ + H2O
-
Sus scrofa betaine + NADH + 2 H+
-
?

Subunits

Subunits Comment Organism
More enzyme secondary structrue analysis, pkBADH/NAD+ interaction analysis by circular dichroism (CD) and by isothermal titration calorimetry (ITC) by titrating the enzyme with NAD+, overview. pkBADH shows 17% of unordered structure, 41% of alpha-helix, and 29% of beta-sheet Sus scrofa
tetramer 4 * 53940, about, sequence calculation, 4 * 54000, recombinant enzyme, SDS-PAGE Sus scrofa

Synonyms

Synonyms Comment Organism
BADH
-
Sus scrofa
betaine aldehyde dehydrogenase
-
Sus scrofa
pkBADH
-
Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Sus scrofa

Cofactor

Cofactor Comment Organism Structure
NAD+ pkBADH/NAD+ interaction analysis by circular dichroism (CD) and by isothermal titration calorimetry (ITC) by titrating the enzyme with NAD+ Sus scrofa

pI Value

Organism Comment pI Value Maximum pI Value
Sus scrofa sequence calculation
-
5.85

General Information

General Information Comment Organism
additional information pkBADH/NAD+ interaction analysis by circular dichroism (CD) and by isothermal titration calorimetry (ITC) by titrating the enzyme with NAD+. Binding of NAD+ to the enzyme causes changes in its secondary structure, the presence of K+ helps maintain its alpha-helix content. BADH enzyme structure homology modeing using the human ALDH9A1 structure (HsALDH9A1, PDB ID 6QAK) as template. The conserved catalytic residues C288, G285, N157, and E254 and the decapeptide VTLELGGKSP are identified Sus scrofa