CATH Classification

Domain Context

CATH Clusters

Superfamily Aldehyde Dehydrogenase; Chain A, domain 2
Functional Family Delta-1-Pyrroline-5-carboxylate dehydrogenase 1, isoform A

Enzyme Information

1.2.1.88
L-glutamate gamma-semialdehyde dehydrogenase.
based on mapping to UniProt P30038
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)

P30038
AL4A1_HUMAN
Homo sapiens
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial

PDB Structure

PDB 3V9G
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The Three-Dimensional Structural Basis of Type II Hyperprolinemia.
Srivastava, D., Singh, R.K., Moxley, M.A., Henzl, M.T., Becker, D.F., Tanner, J.J.
J.Mol.Biol.