ExplorEnz: EC 1.5.1.21

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1.5.1.21

Accepted name:

1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH)

Reaction:

(1) L-pipecolate + NADP⁺ = 1-piperideine-2-carboxylate + NADPH + H⁺
(2) L-proline + NADP⁺ = 1-pyrroline-2-carboxylate + NADPH + H⁺

Glossary:

1-piperideine-2-carboxylate = 3,4,5,6-tetrahydropyridine-2-carboxylate

Other name(s):

Pyr2C reductase; 1,2-didehydropipecolate reductase; P₂C reductase; 1,2-didehydropipecolic reductase; DELTA1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (ambiguous); L-pipecolate:NADP⁺ 2-oxidoreductase; DELTA1-piperideine-2-carboxylate reductase; Δ¹-piperideine-2-carboxylate reductase

Systematic name:

L-pipecolate/L-proline:NADP⁺ 2-oxidoreductase

Comments:

The enzyme is involved in the catabolism of D-lysine and D-proline in bacteria that belong to the Pseudomonas genus. In contrast to EC 1.5.1.1, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H], which shows similar activity with NADPH and NADH, this enzyme is specific for NADPH.

Links to other databases:

BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 52037-88-4

References:

1.	Payton, C.W. and Chang, Y.-F. Δ¹-Piperideine-2-carboxylate reductase of Pseudomonas putida. J. Bacteriol. 149 (1982) 864–871. [PMID: 6801013]
2.	Muramatsu, H., Mihara, H., Kakutani, R., Yasuda, M., Ueda, M., Kurihara, T. and Esaki, N. The putative malate/lactate dehydrogenase from Pseudomonas putida is an NADPH-dependent Δ¹-piperideine-2-carboxylate/Δ¹-pyrroline-2-carboxylate reductase involved in the catabolism of D-lysine and D-proline. J. Biol. Chem. 280 (2005) 5329–5335. [DOI] [PMID: 15561717]
3.	Watanabe, S., Tanimoto, Y., Yamauchi, S., Tozawa, Y., Sawayama, S. and Watanabe, Y. Identification and characterization of trans-3-hydroxy-L-proline dehydratase and Δ¹-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-L-proline metabolism of bacteria. FEBS Open Bio 4 (2014) 240–250. [DOI] [PMID: 24649405]

[EC 1.5.1.21 created 1984 (EC 1.5.1.14 created 1976, incorporated 1989), modified 2015]