EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.2.1.29 | 4-hydroxy-3-methoxybenzaldehyde + NAD+ + H2O |
4-hydroxy-3-methoxybenzaldehyde i.e. vanillin |
Phanerodontia chrysosporium |
4-hydroxy-3-methoxybenzoic acid + NADH + H+ |
- |
? |
1.2.1.29 | 4-hydroxybenzaldehyde + NAD+ + H2O |
- |
Phanerodontia chrysosporium |
4-hydroxybenzoic acid + NADH + H+ |
- |
? |
1.2.1.29 | more |
the enzyme is capable of catalysing the oxidation of a number of aromatic aldehydes, but not aliphatic aldehydes |
Oryctolagus cuniculus |
? |
- |
? |
1.2.1.29 | more |
ALDH catalysis involves acylation and deacylation. During acylation, a cysteine nucleophile interacts with the carbonyl carbon of aldehyde forming a thiohemiacetal intermediate, followed by hydride transfer from a tetrahedral thiohemiacetal intermediate to the pyridine ring of NAD(P)+. Then, deacylation occurs involving hydrolysis of the resulting thioester intermediate. Glu268 and Cys296 of PcALDH are potential active site residues |
Trametes cinnabarina |
? |
- |
? |
1.2.1.29 | more |
ALDH catalysis involves acylation and deacylation. During acylation, a cysteine nucleophile interacts with the carbonyl carbon of aldehyde forming a thiohemiacetal intermediate, followed by hydride transfer from a tetrahedral thiohemiacetal intermediate to the pyridine ring of NAD(P)+. Then, deacylation occurs involving hydrolysis of the resulting thioester intermediate. Glu268 and Cys296 of PcALDH are potential active site residues |
Trametes cinnabarina MUCL 39533 |
? |
- |
? |
1.2.1.29 | aromatic aldehydes + NAD+ + H2O |
- |
Oryctolagus cuniculus |
aromatic acids + NADH |
- |
? |
1.2.1.29 | benzaldehyde + NAD+ + H2O |
- |
Phanerodontia chrysosporium |
benzoic acid + NADH + H+ |
- |
? |
1.2.1.29 | gentisaldehyde + NAD+ |
- |
Oryctolagus cuniculus |
gentisic acid + NADH |
- |
? |
1.2.1.29 | vanillin + NAD+ |
- |
Trametes cinnabarina |
vanillinic acid + NADH + H+ |
- |
r |
1.2.1.29 | vanillin + NAD+ |
- |
Trametes cinnabarina MUCL 39533 |
vanillinic acid + NADH + H+ |
- |
r |