The Enzyme Database

Your query returned 6 entries.    printer_iconPrintable version



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+
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]
[EC 1.5.1.1 created 1961, modified 2015]
 
 
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, 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]
 
 
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]
[EC 1.5.1.49 created 2015]
 
 
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]
[EC 1.5.99.13 created 2010, modified 2011]
 
 
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
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]
[EC 4.2.1.77 created 1984]
 
 
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
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]
[EC 4.2.1.171 created 2017]
 
 


Data © 2001–2020 IUBMB
Web site © 2005–2020 Andrew McDonald