EC 22.214.171.124 - L-glutamate γ-semialdehyde dehydrogenase
IntEnz Enzyme Nomenclature
pyrroline-5-carboxylic acid dehydrogenase
Δ1-pyrroline-5-carboxylic acid dehydrogenase
- L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
This enzyme catalyses the irreversible oxidation of glutamate-γ-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 126.96.36.199, proline dehydrogenase) is in spontaneous equilibrium with its tautomer L-glutamate γ-semialdehyde. In many bacterial species, both activities are carried out by a single bifunctional enzyme [3,4].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 .
Links to other databases
Hydroxyproline metabolism. IV. Enzymatic synthesis of γ-hydroxyglutamate from Δ1-pyrroline-3-hydroxy-5-carboxylate.J. Biol. Chem. 235 : 3504-3512 (1960). [PMID: 13681370]
The interconversion of glutamic acid and proline. III. Δ1-Pyrroline-5-carboxylic acid dehydrogenase.J. Biol. Chem. 235 : 3218-3223 (1960).
Δ1-Pyrroline-5-carboxylate dehydrogenase from cultured cells of potato. Purification and Properties.Plant Physiol. 113 : 1413-1418 (1997). [PMID: 12223682]
Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli.J. Biol. Chem. 267 : 13086-13092 (1992). [PMID: 1618807]
New insights into the binding mode of coenzymes: structure of Thermus thermophilus Δ1-pyrroline-5-carboxylate dehydrogenase complexed with NADP+.Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 : 462-465 (2007). [PMID: 17554163]
[EC 188.8.131.52 created 1972 as 184.108.40.206, modified 2008, transferred 2013 to EC 220.127.116.11]