CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.40 | 3-Layer(aba) Sandwich | |
3.40.309 | Aldehyde Dehydrogenase; Chain A, domain 2 | |
3.40.309.10 | Aldehyde Dehydrogenase; Chain A, domain 2 |
Domain Context
CATH Clusters
Superfamily | Aldehyde Dehydrogenase; Chain A, domain 2 |
Functional Family | 1-pyrroline-5-carboxylate dehydrogenase 1 |
Enzyme Information
1.2.1.88 |
L-glutamate gamma-semialdehyde dehydrogenase.
based on mapping to UniProt P07275
L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH.
-!- This enzyme catalyzes the irreversible oxidation of glutamate-gamma- semialdehyde to glutamate as part of the proline degradation pathway. -!- (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde. -!- In many bacterial species, both activities are carried out by a single bifunctional enzyme. -!- The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1- pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)- 1-pyrroline-5-carboxylate is converted into D-glutamate. -!- NADP(+) can also act as acceptor, but with lower activity. -!- Formerly EC 1.5.1.12.
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UniProtKB Entries (1)
P07275 |
PUT2_YEAST
Saccharomyces cerevisiae S288C
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
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PDB Structure
PDB | 4OE4 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structural Studies of Yeast Delta (1)-Pyrroline-5-carboxylate Dehydrogenase (ALDH4A1): Active Site Flexibility and Oligomeric State.
Biochemistry
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