In enzymology, a 1-pyrroline-5-carboxylate dehydrogenase () is an enzyme that catalyzes the chemical reaction

(S)-1-pyrroline-5-carboxylate + NAD⁺ + 2 H₂O \rightleftharpoons L-glutamate + NADH + H⁺

The three substrates of this enzyme are (S)-1-pyrroline-5-carboxylate, NAD⁺, and H₂O, whereas its three products are glutamate, NADH, and H⁺.

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 , , , , , , , , , , , , , and .

References

it:1-pirrolina-5-carbossilato deidrogenasi ja:1- -5-