EC Number |
General Information |
Reference |
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1.1.1.387 | metabolism |
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 |
725474 |
1.1.1.387 | more |
catalytic domain fold of the Pyrobaculum calidifontis enzyme shows similarity with that of Pseudomonas aeruginosa L-SerDH, but the active site structure significantly differs between the two enzymes. Based on the structure of the tartrate, L- and D-serine and 3-hydroxypropionate molecules are modeled into the active site and the substrate binding modes are estimated. The wide cavity at the substrate binding site is likely responsible for the high reactivity of the enzyme toward both L- and D-serine enantiomers. Analysis of the substrate binding mechanism of L-SerDH, and detailed enzyme structure analysis, overview |
763006 |
1.1.1.387 | physiological function |
L-serine 3-dehydrogenase acts at the beta-carbon (C3) position of L-serine. The product of this reaction is supposed to be 2-aminomalonate semialdehyde, which nonenzymatically decomposes into 2-aminoacetaldehyde and CO2 |
763006 |