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 |
1.5.3.7 |
Accepted name: |
L-pipecolate oxidase |
Reaction: |
L-pipecolate + O2 = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2 |
Glossary: |
L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate (S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine |
Other name(s): |
pipecolate oxidase; L-pipecolic acid oxidase |
Systematic name: |
L-pipecolate:oxygen 1,6-oxidoreductase |
Comments: |
The product reacts with water to form (S)-2-amino-6-oxohexanoate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81669-65-0 |
References: |
1. |
Baginsky, B.L. and Rodwell, V.W. Metabolism of pipecolic acid in a Pseudomonas species. V. Pipecolate oxidase and dehydrogenase. J. Bacteriol. 94 (1967) 1034–1039. [PMID: 6051341] |
2. |
Kinzel, J.J. and Bhattacharjee, J.K. Lysine biosynthesis in Rhodotorula glutinis: properties of pipecolic acid oxidase. J. Bacteriol. 151 (1982) 1073–1077. [PMID: 6809728] |
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[EC 1.5.3.7 created 1986, modified 2011] |
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EC |
1.5.99.3 |
Accepted name: |
L-pipecolate dehydrogenase |
Reaction: |
L-pipecolate + acceptor = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + reduced acceptor |
Glossary: |
(S)-2-amino-6-oxohexanoate = L-2-aminoadipate 6-semialdehyde = L-allysine L-1-piperideine 6-carboxylate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate = (S)-1,6-didehydropiperidine-2-carboxylate |
Other name(s): |
L-pipecolate:(acceptor) 1,6-oxidoreductase |
Systematic name: |
L-pipecolate:acceptor 1,6-oxidoreductase |
Comments: |
The product reacts with water to form (S)-2-amino-6-oxohexanoate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9076-63-5 |
References: |
1. |
Baginsky, B.L. and Rodwell, V.W. Metabolism of pipecolic acid in a Pseudomonas species. V. Pipecolate oxidase and dehydrogenase. J. Bacteriol. 94 (1967) 1034–1039. [PMID: 6051341] |
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[EC 1.5.99.3 created 1972, modified 1986, modified 2011] |
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EC |
3.5.1.101 |
Accepted name: |
L-proline amide hydrolase |
Reaction: |
(1) (S)-piperidine-2-carboxamide + H2O = (S)-piperidine-2-carboxylate + NH3 (2) L-prolinamide + H2O = L-proline + NH3 |
Glossary: |
L-pipecolate = piperidine-2-carboxylate |
Other name(s): |
S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase; LaaA; L-amino acid amidase |
Systematic name: |
(S)-piperidine-2-carboxamide amidohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Komeda, H., Harada, H., Washika, S., Sakamoto, T., Ueda, M. and Asano, Y. S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase from Pseudomonas azotoformans IAM 1603 is a novel L-amino acid amidase. Eur. J. Biochem. 271 (2004) 1465–1475. [DOI] [PMID: 15066172] |
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[EC 3.5.1.101 created 2009] |
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EC |
4.3.1.28 |
Accepted name: |
L-lysine cyclodeaminase |
Reaction: |
L-lysine = L-pipecolate + NH3 |
Other name(s): |
rapL (gene name); fkbL (gene name); tubZ (gene name); visC (gene name) |
Systematic name: |
L-lysine ammonia-lyase (cyclizing; ammonia-forming) |
Comments: |
Requires bound NAD+. The enzyme produces the non-proteinogenic amino acid L-pipecolate, which is incorporated into multiple secondary metabolite products, including rapamycin, tobulysin, virginiamycin and pristinamycin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Khaw, L.E., Bohm, G.A., Metcalfe, S., Staunton, J. and Leadlay, P.F. Mutational biosynthesis of novel rapamycins by a strain of Streptomyces hygroscopicus NRRL 5491 disrupted in rapL, encoding a putative lysine cyclodeaminase. J. Bacteriol. 180 (1998) 809–814. [PMID: 9473033] |
2. |
Gatto, G.J., Jr., Boyne, M.T., 2nd, Kelleher, N.L. and Walsh, C.T. Biosynthesis of pipecolic acid by RapL, a lysine cyclodeaminase encoded in the rapamycin gene cluster. J. Am. Chem. Soc. 128 (2006) 3838–3847. [DOI] [PMID: 16536560] |
3. |
Tsotsou, G.E. and Barbirato, F. Biochemical characterisation of recombinant Streptomyces pristinaespiralis L-lysine cyclodeaminase. Biochimie 89 (2007) 591–604. [DOI] [PMID: 17291665] |
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[EC 4.3.1.28 created 2012] |
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