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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 1.14.11.41
BRENDA Enzyme Link:	BRENDA 1.14.11.41
KEGG Enzyme Link:	KEGG1.14.11.41
BioCyc Enzyme Link:	BioCyc 1.14.11.41
ExPASy Enzyme Link:	ExPASy1.14.11.41
EC2PDB Enzyme Link:	EC2PDB 1.14.11.41
ExplorEnz Enzyme Link:	ExplorEnz 1.14.11.41
PRIAM enzyme-specific profiles Link:	PRIAM 1.14.11.41
IntEnz Enzyme Link:	IntEnz 1.14.11.41
MEDLINE Enzyme Link:	MEDLINE 1.14.11.41

RHEA:36607	2-oxoglutarate + L-arginine + O2 = (2S,3S)-hydroxyarginine + 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
Structural basis for the erythro-stereospecificity of the L-arginine oxygenase VioC in viomycin biosynthesis.	Helmetag V, Samel SA, Thomas MG, Marahiel MA, Essen LO	2009 Jul	19490124
Conversion of (2S)-arginine to (2S,3R)-capreomycidine by VioC and VioD from the viomycin biosynthetic pathway of Streptomyces sp. strain ATCC11861.	Ju J, Ozanick SG, Shen B, Thomas MG	2004 Sep 6	15368582
VioC is a non-heme iron, alpha-ketoglutarate-dependent oxygenase that catalyzes the formation of 3S-hydroxy-L-arginine during viomycin biosynthesis.	Yin X, Zabriskie TM	2004 Sep 6	15368580