EC number:1.5.1.2

Enzyme

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     1. Oxidoreductases
        1.5 Acting on the CH-NH group of donors
            1.5.1 With NAD+ or NADP+ as acceptor
ID:1.5.1.2
Description:Pyrroline-5-carboxylate reductase.
Alternative Name: P5CR.
Prosite: PDOC00451;
PDB:
PDBScop
5UAX
5UAW
5UAV
5UAU
5UAT
 » show all
Cath: 1.10.3730.10; 3.40.50.720;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.5.1.2
BRENDA Enzyme Link: BRENDA 1.5.1.2
KEGG Enzyme Link: KEGG1.5.1.2
BioCyc Enzyme Link: BioCyc 1.5.1.2
ExPASy Enzyme Link: ExPASy1.5.1.2
EC2PDB Enzyme Link: EC2PDB 1.5.1.2
ExplorEnz Enzyme Link: ExplorEnz 1.5.1.2
PRIAM enzyme-specific profiles Link: PRIAM 1.5.1.2
IntEnz Enzyme Link: IntEnz 1.5.1.2
MEDLINE Enzyme Link: MEDLINE 1.5.1.2

EC number:1.5.1.2

MSA:

1.5.1.2;
Phylogenetic Tree:

1.5.1.2;
Uniprot:
M-CSA:
RHEA:14109 L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADPH
RULE(radius=1) [*:1]-[NH;+0:2]-[CH2;+0:3]-[*:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1.[*:1]-[N;H0;+0:2]=[CH;+0:3]-[*:4]
Reaction
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References

TitleAuthorsDatePubMed ID
Pyrroline-5-carboxylate reductase in human erythrocytes.Yeh GC, Harris SC, Phang JM1981 Apr6894153
Escherichia coli delta 1-pyrroline-5-carboxylate reductase: gene sequence, protein overproduction and purification.Deutch AH, Smith CJ, Rushlow KE, Kretschmer PJ1982 Dec 116296787
Purified human erythrocyte pyrroline-5-carboxylate reductase. Preferential oxidation of NADPH.Merrill MJ, Yeh GC, Phang JM1989 Jun 52722838
Functional specialization in proline biosynthesis of melanoma.De Ingeniis J, Ratnikov B, Richardson AD, Scott DA, Aza-Blanc P, De SK, Kazanov M, Pellecchia M, Ronai Z, Osterman AL, Smith JW201223024808
Complementation of an Escherichia coli proC mutation by a gene cloned from Treponema pallidum.Gherardini FC, Hobbs MM, Stamm LV, Bassford PJ Jr1990 Jun2188947
Crystal structure of human pyrroline-5-carboxylate reductase.Meng Z, Lou Z, Liu Z, Li M, Zhao X, Bartlam M, Rao Z2006 Jun 2316730026
Partial purification and some properties of delta1-pyrroline-5-carboxylate reductase from Escherichia coli.Rossi JJ, Vender J, Berg CM, Coleman WH1977 Jan12133
RHEA:14105 L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
RULE(radius=1) [*:1]-[NH;+0:2]-[CH2;+0:3]-[*:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1.[*:1]-[N;H0;+0:2]=[CH;+0:3]-[*:4]
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Pyrroline-5-carboxylate reductase in human erythrocytes.Yeh GC, Harris SC, Phang JM1981 Apr6894153
Escherichia coli delta 1-pyrroline-5-carboxylate reductase: gene sequence, protein overproduction and purification.Deutch AH, Smith CJ, Rushlow KE, Kretschmer PJ1982 Dec 116296787
Purified human erythrocyte pyrroline-5-carboxylate reductase. Preferential oxidation of NADPH.Merrill MJ, Yeh GC, Phang JM1989 Jun 52722838
Functional specialization in proline biosynthesis of melanoma.De Ingeniis J, Ratnikov B, Richardson AD, Scott DA, Aza-Blanc P, De SK, Kazanov M, Pellecchia M, Ronai Z, Osterman AL, Smith JW201223024808
Complementation of an Escherichia coli proC mutation by a gene cloned from Treponema pallidum.Gherardini FC, Hobbs MM, Stamm LV, Bassford PJ Jr1990 Jun2188947
Crystal structure of human pyrroline-5-carboxylate reductase.Meng Z, Lou Z, Liu Z, Li M, Zhao X, Bartlam M, Rao Z2006 Jun 2316730026
Partial purification and some properties of delta1-pyrroline-5-carboxylate reductase from Escherichia coli.Rossi JJ, Vender J, Berg CM, Coleman WH1977 Jan12133