CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.720 | NAD(P)-binding Rossmann-like Domain |
Domain Context
CATH Clusters
| Superfamily | NAD(P)-binding Rossmann-like Domain |
| Functional Family | NADP-dependent L-serine/L-allo-threonine dehydrogenase |
Enzyme Information
| 1.1.1.381 |
3-hydroxy acid dehydrogenase.
based on mapping to UniProt Q05016
L-allo-threonine + NADP(+) = aminoacetone + CO(2) + NADPH.
-!- The enzyme, purified from the bacterium Escherichia coli and the yeast Saccharomyces cerevisiae, shows activity with a range of 3- and 4-carbon 3-hydroxy acids. -!- The highest activity is seen with L-allo-threonine and D-threonine. -!- The enzyme from E.coli also shows high activity with L-serine, D-serine, (S)-3-hydroxy-2-methylpropanoate and (R)-3-hydroxy-2- methylpropanoate. -!- The enzyme has no activity with NAD(+) or L-threonine (cf. EC 1.1.1.103).
|
UniProtKB Entries (1)
| Q05016 |
YM71_YEAST
Saccharomyces cerevisiae S288C
NADP-dependent 3-hydroxy acid dehydrogenase
|
PDB Structure
| PDB | 3RKU |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Substrate Fingerprint and the Structure of NADP+ Dependent Serine Dehydrogenase from Saccharomyces cerevisiae complexed with NADP+
To be Published
|
