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1-Pyrroline-5-carboxylate dehydrogenase
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Class of enzymes
1-pyrroline-5-carboxylate dehydrogenase 1.2.1.88 9054-82-4 0003842
In enzymology, 1-pyrroline-5-carboxylate dehydrogenase (1.2.1.88) is an enzyme that catalyzes the chemical reaction
65% Q27105294 (S)-1-pyrroline-5-carboxylic acid
reversible
Q2823261 L-glutamate-5-semialdehyde
+ NAD+
reversible H2O H+ H+ H2O
Q26995161 L-glutamic acid
+ NADH
The three substrates of this enzyme are (S)-1-pyrroline-5-carboxylate, nicotinamide adenine dinucleotide (NAD+), and water. The starting material is in chemical equilibrium with L-glutamate-5-semialdehyde, which is oxidised to L-glutamic acid, giving reduced NADH, and a proton.1.2.1.88 Adams E, Goldstone A Hydroxyproline metabolism. IV. Enzymatic synthesis of gamma-hydroxyglutamate from Delta 1-pyrroline-3-hydroxy-5-carboxylate The Journal of Biological Chemistry 235 3504–12 December 1960 12 10.1016/S0021-9258(18)64498-9 13681370 free Strecker HJ 1960 The interconversion of glutamic acid proline. III Delta1-Pyrroline-5-carboxylic acid dehydrogenase J. Biol. Chem. 235 3218–3223 10.1016/S0021-9258(20)81340-4 free
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-1-pyrroline-5-carboxylate:NAD+ oxidoreductase. Other names in common use include delta-1-pyrroline-5-carboxylate dehydrogenase, 1-pyrroline dehydrogenase, pyrroline-5-carboxylate dehydrogenase, pyrroline-5-carboxylic acid dehydrogenase, L-pyrroline-5-carboxylate-NAD+ oxidoreductase, and 1-pyrroline-5-carboxylate:NAD+ oxidoreductase. This enzyme participates in glutamate metabolism and arginine and proline metabolism.
Structural studies
As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes 2BHP, 2BHQ, 2BJA, 2BJK, 2EHQ, 2EHU, 2EII, 2EIT, 2EIW, 2EJ6, 2EJD, 2EJL, 2IY6, and 2J40.
Human gene
In human, the protein is encoded by ALDH4A1 gene.
References
Biology no
Category:EC 1.2.1
Category:Aldehyde dehydrogenases