EC |
1.5.1.1 |
Accepted name: |
1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H] |
Reaction: |
(1) L-pipecolate + NAD(P)+ = 1-piperideine-2-carboxylate + NAD(P)H + H+ (2) L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+
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Other name(s): |
Δ1-pyrroline-2-carboxylate reductase; DELTA1-pyrroline-2-carboxylate reductase; DELTA1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (ambiguous); AbLhpI; pyrroline-2-carboxylate reductase; L-proline:NAD(P)+ 2-oxidoreductase |
Systematic name: |
L-pipecolate/L-proline:NAD(P)+ 2-oxidoreductase |
Comments: |
The enzymes, characterized from the bacterium Azospirillum brasilense, is involved in trans-3-hydroxy-L-proline metabolism. In contrast to EC 1.5.1.21, 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH), which is specific for NADPH, this enzyme shows similar activity with NADPH and NADH. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9029-16-7 |
References: |
1. |
Meister, A., Radhakrishnan, A.N. and Buckley, S.D. Enzymatic synthesis of L-pipecolic acid and L-proline. J. Biol. Chem. 229 (1957) 789–800. [PMID: 13502341] |
2. |
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] |
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[EC 1.5.1.1 created 1961, modified 2015] |
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EC |
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] |
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[EC 1.5.1.21 created 1984 (EC 1.5.1.14 created 1976, incorporated 1989), modified 2015] |
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EC |
1.5.1.49 |
Accepted name: |
1-pyrroline-2-carboxylate reductase [NAD(P)H] |
Reaction: |
L-proline + NAD(P)+ = 1-pyrroline-2-carboxylate + NAD(P)H + H+ |
Systematic name: |
L-proline:NAD(P)+ 2-oxidoreductase |
Comments: |
The enzyme from the bacterium Colwellia psychrerythraea is involved in trans-3-hydroxy-L-proline metabolism. 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 1-piperideine-2-carboxylate and 1-pyrroline-2-carboxylate, this enzyme is specific for the latter. While the enzyme is active with both NADH and NADPH, activity is higher with NADPH. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
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] |
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[EC 1.5.1.49 created 2015] |
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EC |
1.5.99.13 |
Accepted name: |
D-proline dehydrogenase |
Reaction: |
D-proline + acceptor = 1-pyrroline-2-carboxylate + reduced acceptor |
Other name(s): |
D-Pro DH; D-Pro dehydrogenase; dye-linked D-proline dehydrogenase |
Systematic name: |
D-proline:acceptor oxidoreductase |
Comments: |
A flavoprotein (FAD). The enzyme prefers D-proline and acts on other D-amino acids with lower efficiency. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Tani, Y., Tanaka, K., Yabutani, T., Mishima, Y., Sakuraba, H., Ohshima, T. and Motonaka, J. Development of a D-amino acids electrochemical sensor based on immobilization of thermostable D-proline dehydrogenase within agar gel membrane. Anal. Chim. Acta 619 (2008) 215–220. [DOI] [PMID: 18558115] |
2. |
Satomura, T., Kawakami, R., Sakuraba, H. and Ohshima, T. Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase. J. Biol. Chem. 277 (2002) 12861–12867. [DOI] [PMID: 11823469] |
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[EC 1.5.99.13 created 2010, modified 2011] |
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EC |
4.2.1.77 |
Accepted name: |
trans-L-3-hydroxyproline dehydratase |
Reaction: |
trans-3-hydroxy-L-proline = 1-pyrroline 2-carboxylate + H2O |
Other name(s): |
trans-L-3-hydroxyproline hydro-lyase |
Systematic name: |
trans-3-hydroxy-L-proline hydro-lyase (1-pyrroline-2-carboxylate-forming) |
Comments: |
Highly specific. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Ramaswamy, S.G. Conversion of 3-hydroxyproline to proline in the rat requires reduced pyridine-nucleotides. Fed. Proc. 42 (1983) 2232. |
2. |
Visser, W.F., Verhoeven-Duif, N.M. and de Koning, T.J. Identification of a human trans-3-hydroxy-L-proline dehydratase, the first characterized member of a novel family of proline racemase-like enzymes. J. Biol. Chem. 287 (2012) 21654–21662. [DOI] [PMID: 22528483] |
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[EC 4.2.1.77 created 1984] |
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EC |
4.2.1.171 |
Accepted name: |
cis-L-3-hydroxyproline dehydratase |
Reaction: |
cis-3-hydroxy-L-proline = 1-pyrroline-2-carboxylate + H2O |
Glossary: |
1-pyrroline-2-carboxylate = 4,5-dihydro-3H-pyrrole-2-carboxylate |
Other name(s): |
cis-L-3-hydroxyproline hydro-lyase; c3LHypD |
Systematic name: |
cis-3-hydroxy-L-proline hydro-lyase (1-pyrroline-2-carboxylate-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Zhang, X., Kumar, R., Vetting, M.W., Zhao, S., Jacobson, M.P., Almo, S.C. and Gerlt, J.A. A unique cis-3-hydroxy-L-proline dehydratase in the enolase superfamily. J. Am. Chem. Soc. 137 (2015) 1388–1391. [DOI] [PMID: 25608448] |
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[EC 4.2.1.171 created 2017] |
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