CATH Classification

Domain Context

CATH Clusters

Superfamily Aldehyde Dehydrogenase; Chain A, domain 1
Functional Family

Enzyme Information

1.2.1.88
L-glutamate gamma-semialdehyde dehydrogenase.
based on mapping to UniProt Q8CHT0
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)

Q8CHT0
AL4A1_MOUSE
Mus musculus
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial

PDB Structure

PDB 4LH3
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural basis of substrate selectivity of Delta (1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): Semialdehyde chain length.
Pemberton, T.A., Tanner, J.J.
Arch.Biochem.Biophys.
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