EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.1.1.387 | 2-aminomalonate semialdehyde |
spontaneous |
Pyrobaculum calidifontis |
2-aminoacetaldehyde + CO2 |
- |
? |
1.1.1.387 | D-serine + NAD+ |
overall reaction, 5% of the relative activity observed with L-serine |
Pyrobaculum calidifontis |
2-aminoacetaldehyde + CO2 + NADH + H+ |
- |
? |
1.1.1.387 | L-serine + NAD+ |
overall reaction, NAD+ is the preferred cofactor |
Pyrobaculum calidifontis |
2-aminoacetaldehyde + CO2 + NADH + H+ |
- |
? |
1.1.1.387 | L-serine + NADP+ |
overall reaction, low activity with NADP+ |
Pyrobaculum calidifontis |
2-aminoacetaldehyde + CO2 + NADPH + H+ |
- |
? |
1.1.1.387 | L-serine + NAD(P)+ |
- |
Pyrobaculum calidifontis |
2-aminomalonate semialdehyde + NAD(P)H + H+ |
- |
? |
1.1.1.387 | D-glycerate + NAD+ |
- |
Pseudomonas aeruginosa |
? |
- |
? |
1.1.1.387 | DL-threonine + NAD+ |
- |
Pseudomonas aeruginosa |
? |
- |
? |
1.1.1.387 | L-serine + NAD+ |
the enzyme might be involved in serine/threonine degradation. Since growth experiments with various nitrogen and carbon sources (including L-serine) reveal no difference between the Pseudomonas aeruginosa wild-type and PA0743 deletion strains, it is suggested hat this organism might contain other (complementing) serine dehydrogenases |
Pseudomonas aeruginosa |
? |
- |
? |
1.1.1.387 | L-serine + NAD+ |
the enzyme might be involved in serine/methylserine degradation. Since growth experiments with various nitrogen and carbon sources (including L-serine) reveal no difference between the Pseudomonas aeruginosa wild-type and PA0743 deletion strains, it is suggested hat this organism might contain other (complementing) serine dehydrogenases |
Pseudomonas aeruginosa |
? |
- |
? |
1.1.1.387 | methyl 2,2-dimethyl-3-hydroxypropionate + NAD+ |
- |
Pseudomonas aeruginosa |
? |
- |
? |