EC number:1.13.99.1

Enzyme

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     1. Oxidoreductases
        1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
            1.13.99 Miscellaneous
ID:1.13.99.1
Description:Inositol oxygenase.
Alternative Name: Myo-inositol oxygenase.
MOO.
Meso-inositol oxygenase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.13.99.1
BRENDA Enzyme Link: BRENDA 1.13.99.1
KEGG Enzyme Link: KEGG1.13.99.1
BioCyc Enzyme Link: BioCyc 1.13.99.1
ExPASy Enzyme Link: ExPASy1.13.99.1
EC2PDB Enzyme Link: EC2PDB 1.13.99.1
ExplorEnz Enzyme Link: ExplorEnz 1.13.99.1
PRIAM enzyme-specific profiles Link: PRIAM 1.13.99.1
IntEnz Enzyme Link: IntEnz 1.13.99.1
MEDLINE Enzyme Link: MEDLINE 1.13.99.1

EC number:1.13.99.1

MSA:

1.13.99.1;
Phylogenetic Tree:

1.13.99.1;
Uniprot:
M-CSA:
RHEA:23696 myo-inositol + O2 = D-glucuronate + H(+) + H2O
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3]-[OH;+0:4])-[CH;+0:5](-[*:6])-[*:7].[O;H0;+0:8]=[O;H0;+0:9]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:8])-[*:3]-[O;H0;+0:4]-[CH;+0:5](-[*:6])-[*:7].[OH2;+0:9]
Reaction
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References

TitleAuthorsDatePubMed ID
An oxygen-18 tracer investigation of the mechanism of myo-inositol oxygenase.Moskala R, Reddy CC, Minard RD, Hamilton GA1981 Mar 167236254
Structural and biophysical characterization of human myo-inositol oxygenase.Thorsell AG, Persson C, Voevodskaya N, Busam RD, Hammarström M, Gräslund S, Gräslund A, Hallberg BM2008 May 3018364358
Crystal structure of a substrate complex of myo-inositol oxygenase, a di-iron oxygenase with a key role in inositol metabolism.Brown PM, Caradoc-Davies TT, Dickson JM, Cooper GJ, Loomes KM, Baker EN2006 Oct 1017012379