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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

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UniProtKB Enzyme Link:	UniProtKB 1.14.11.28
BRENDA Enzyme Link:	BRENDA 1.14.11.28
KEGG Enzyme Link:	KEGG1.14.11.28
BioCyc Enzyme Link:	BioCyc 1.14.11.28
ExPASy Enzyme Link:	ExPASy1.14.11.28
EC2PDB Enzyme Link:	EC2PDB 1.14.11.28
ExplorEnz Enzyme Link:	ExplorEnz 1.14.11.28
PRIAM enzyme-specific profiles Link:	PRIAM 1.14.11.28
IntEnz Enzyme Link:	IntEnz 1.14.11.28
MEDLINE Enzyme Link:	MEDLINE 1.14.11.28

RHEA:20265	2-oxoglutarate + L-proline + O2 = cis-3-hydroxy-L-proline + CO2 + succinate
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

Title	Authors	Date	PubMed ID
Purification and cloning of a proline 3-hydroxylase, a novel enzyme which hydroxylates free L-proline to cis-3-hydroxy-L-proline.	Mori H, Shibasaki T, Yano K, Ozaki A	1997 Sep	9294421
Detection of Novel Proline 3-Hydroxylase Activities in Streptomyces and Bacillus spp. by Regio- and Stereospecific Hydroxylation of l-Proline.	Mori H, Shibasaki T, Uozaki Y, Ochiai K, Ozaki A	1996 Jun	16535329
Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases.	Clifton IJ, Hsueh LC, Baldwin JE, Harlos K, Schofield CJ	2001 Dec	11737217