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Literature summary for 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.
    View publication on PubMed

Crystallization (Commentary)

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


Organism UniProt Comment Textmining
Pseudomonas syringae Q4U331


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


Subunits Comment Organism
dimer crystallization data Pseudomonas syringae


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