EC number:1.14.11.35

Enzyme

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EC Tree
     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:1.14.11.35
Description:1-deoxypentalenic acid 11-beta-hydroxylase.
Cath: 2.60.120.620;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.11.35
BRENDA Enzyme Link: BRENDA 1.14.11.35
KEGG Enzyme Link: KEGG1.14.11.35
BioCyc Enzyme Link: BioCyc 1.14.11.35
ExPASy Enzyme Link: ExPASy1.14.11.35
EC2PDB Enzyme Link: EC2PDB 1.14.11.35
ExplorEnz Enzyme Link: ExplorEnz 1.14.11.35
PRIAM enzyme-specific profiles Link: PRIAM 1.14.11.35
IntEnz Enzyme Link: IntEnz 1.14.11.35
MEDLINE Enzyme Link: MEDLINE 1.14.11.35

EC number:1.14.11.35

MSA:

1.14.11.35;
Phylogenetic Tree:

1.14.11.35;
Uniprot:
M-CSA:
RHEA:34619 1-deoxypentalenate + 2-oxoglutarate + O2 = 1-deoxy-11beta-hydroxypentalenate + 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

References

TitleAuthorsDatePubMed ID
Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis.You Z, Omura S, Ikeda H, Cane DE, Jogl G2007 Dec 1417942405
Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlH, a non-heme iron dioxygenase of Streptomyces avermitilis.You Z, Omura S, Ikeda H, Cane DE2006 May 2416704250