Literature summary for 1.5.1.1 extracted from

Goto, M.; Muramatsu, H.; Mihara, H.; Kurihara, T.; Esaki, N.; Omi, R.; Miyahara, I.; Hirotsu, K.
Crystal structures of DELTA1-piperideine-2-carboxylate/DELTA1-pyrroline-2-carboxylate reductase belonging to a new family of NAD(P)H-dependent oxidoreductases: conformational change, substrate recognition, and stereochemistry of the reaction (2005), J. Biol. Chem., 280, 40875-40884.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
unliganded enzyme, in complex with NADPH, and in complex with NADPH and pyrrole-2-carboxylate	Pseudomonas syringae

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas syringae	Q4U331	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+	Mobile domains I and II of protein change their conformations to produce the catalytic form. Preference for NADPH over NADH is explained by the cofactor binding site architecture	Pseudomonas syringae	a

Subunits

Subunits	Comment	Organism
dimer	crystallization data	Pseudomonas syringae

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	preference for NADPH over NADH	Pseudomonas syringae
NADPH	preference for NADPH over NADH	Pseudomonas syringae

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Release 2023.1 (January 2023)