CATH Classification

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.

UniProtKB Entries (1)

P07275
PUT2_YEAST
Saccharomyces cerevisiae S288C
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial

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.
Pemberton, T.A., Srivastava, D., Sanyal, N., Henzl, M.T., Becker, D.F., Tanner, J.J.
Biochemistry