Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
ID:1.14.11.57
Description:L-proline trans-4-hydroxylase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.11.57
BRENDA Enzyme Link: BRENDA 1.14.11.57
KEGG Enzyme Link: KEGG1.14.11.57
BioCyc Enzyme Link: BioCyc 1.14.11.57
ExPASy Enzyme Link: ExPASy1.14.11.57
EC2PDB Enzyme Link: EC2PDB 1.14.11.57
ExplorEnz Enzyme Link: ExplorEnz 1.14.11.57
PRIAM enzyme-specific profiles Link: PRIAM 1.14.11.57
IntEnz Enzyme Link: IntEnz 1.14.11.57
MEDLINE Enzyme Link: MEDLINE 1.14.11.57
MSA:

1.14.11.57;

Phylogenetic Tree:

1.14.11.57;

Uniprot:
M-CSA:
RHEA:51508 2-oxoglutarate + L-proline + O2 = CO2 + succinate + trans-4-hydroxy-L-proline
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[*:4]=[C;H0;+0:5](-[OH;+0:6])-[C;H0;+0:7](=[*:8])-[*:9].[O;H0;+0:10]=[O;H0;+0:11]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:10].[*:8]=[C;H0;+0:7](-[*:9])-[OH;+0:11].[*:4]=[C;H0;+0:5]=[O;H0;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification and initial characterization of proline 4-hydroxylase from Streptomyces griseoviridus P8648: a 2-oxoacid, ferrous-dependent dioxygenase involved in etamycin biosynthesis.Lawrence CC, Sobey WJ, Field RA, Baldwin JE, Schofield CJ1996 Jan 18546682
Microbial proline 4-hydroxylase screening and gene cloning.Shibasaki T, Mori H, Chiba S, Ozaki A1999 Sep10473412