EC number:1.14.19.69

Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.19 With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
ID:1.14.19.69
Description:Biflaviolin synthase.
Alternative Name: CYP158A2.
Prosite: PDOC00081;
PDB:
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3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.19.69
BRENDA Enzyme Link: BRENDA 1.14.19.69
KEGG Enzyme Link: KEGG1.14.19.69
BioCyc Enzyme Link: BioCyc 1.14.19.69
ExPASy Enzyme Link: ExPASy1.14.19.69
EC2PDB Enzyme Link: EC2PDB 1.14.19.69
ExplorEnz Enzyme Link: ExplorEnz 1.14.19.69
PRIAM enzyme-specific profiles Link: PRIAM 1.14.19.69
IntEnz Enzyme Link: IntEnz 1.14.19.69
MEDLINE Enzyme Link: MEDLINE 1.14.19.69

EC number:1.14.19.69

MSA:

1.14.19.69;
Phylogenetic Tree:

1.14.19.69;
Uniprot:
M-CSA:
RHEA:26035 2 flaviolin + H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 3,8'-biflaviolin + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
RULE(radius=1) [*:1]-[CH;+0:2]=[*:3].[*:4]-[N;H0;+0:5]1-[CH;+0:6]=[C;H0;+0:7](-[*:8])-[CH2;+0:9]-[CH;+0:10]=[CH;+0:11]-1.[*:12]:[cH;+0:13]:[*:14].[O;H0;+0:15]=[O;H0;+0:16]>>[*:1]-[C;H0;+0:2](=[*:3])-[c;H0;+0:13](:[*:12]):[*:14].[*:4]-[n+;H0:5]1:[cH;+0:6]:[c;H0;+0:7](-[*:8]):[cH;+0:9]:[cH;+0:10]:[cH;+0:11]:1.[OH2;+0:15].[OH2;+0:16]
Reaction
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References

TitleAuthorsDatePubMed ID
Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2.Zhao B, Lamb DC, Lei L, Kelly SL, Yuan H, Hachey DL, Waterman MR2007 Jul 3117614370
Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer.Zhao B, Guengerich FP, Voehler M, Waterman MR2005 Dec 2316239228
Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2.Zhao B, Guengerich FP, Bellamine A, Lamb DC, Izumikawa M, Lei L, Podust LM, Sundaramoorthy M, Kalaitzis JA, Reddy LM, Kelly SL, Moore BS, Stec D, Voehler M, Falck JR, Shimada T, Waterman MR2005 Mar 2515659395
RHEA:26031 2 flaviolin + H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 3,3'-biflaviolin + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
RULE(radius=1) [*:1]-[CH;+0:2]=[*:3].[*:4]-[CH;+0:5]=[*:6].[*:7]-[N;H0;+0:8]1-[CH;+0:9]=[C;H0;+0:10](-[*:11])-[CH2;+0:12]-[CH;+0:13]=[CH;+0:14]-1.[O;H0;+0:15]=[O;H0;+0:16]>>[*:1]-[C;H0;+0:2](=[*:3])-[C;H0;+0:5](-[*:4])=[*:6].[*:7]-[n+;H0:8]1:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:[cH;+0:13]:[cH;+0:14]:1.[OH2;+0:15].[OH2;+0:16]
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2.Zhao B, Lamb DC, Lei L, Kelly SL, Yuan H, Hachey DL, Waterman MR2007 Jul 3117614370
Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer.Zhao B, Guengerich FP, Voehler M, Waterman MR2005 Dec 2316239228
Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2.Zhao B, Guengerich FP, Bellamine A, Lamb DC, Izumikawa M, Lei L, Podust LM, Sundaramoorthy M, Kalaitzis JA, Reddy LM, Kelly SL, Moore BS, Stec D, Voehler M, Falck JR, Shimada T, Waterman MR2005 Mar 2515659395