Enzyme

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EC Tree
     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.14.117
Description:Aflatoxin B synthase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.14.117
BRENDA Enzyme Link: BRENDA 1.14.14.117
KEGG Enzyme Link: KEGG1.14.14.117
BioCyc Enzyme Link: BioCyc 1.14.14.117
ExPASy Enzyme Link: ExPASy1.14.14.117
EC2PDB Enzyme Link: EC2PDB 1.14.14.117
ExplorEnz Enzyme Link: ExplorEnz 1.14.14.117
PRIAM enzyme-specific profiles Link: PRIAM 1.14.14.117
IntEnz Enzyme Link: IntEnz 1.14.14.117
MEDLINE Enzyme Link: MEDLINE 1.14.14.117
MSA:

1.14.14.117;

Phylogenetic Tree:

1.14.14.117;

Uniprot:
M-CSA:
RHEA:35763 8-O-methyldihydrosterigmatocystin + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = aflatoxin B2 + CO2 + 2 H(+) + H2O + methanol + 2 oxidized [NADPH--hemoprotein reductase]
RULE(radius=1) [*:1]-[C;H0;+0:2]1=[CH;+0:3]-[N;H0;+0:4](-[*:5])-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-1.([*:9]-[N;H0;+0:10]1-[CH;+0:11]=[C;H0;+0:12](-[*:13])-[CH2;+0:14]-[CH;+0:15]=[CH;+0:16]-1.[*:17]-[P;H0;+0:18](=[*:19])(-[*:20])-[OH;+0:21]).[*:22]:[c;H0;+0:23]1:[cH;+0:24]:[cH;+0:25]:[cH;+0:26]:[c;H0;+0:27](-[O;H0;+0:28]-[CH3;+0:29]):[*:30]:1:[c;H0;+0:31](:[*:32])=[O;H0;+0:33].[H+;H0:34].[H+;H0:35].[O;H0;+0:36]=[O;H0;+0:37].[O;H0;+0:38]=[O;H0;+0:39]>>([*:17]-[P;H0;+0:18](=[*:19])(-[*:20])-[OH;+0:36].[*:9]-[n+;H0:10]1:[cH;+0:11]:[c;H0;+0:12](-[*:13]):[cH;+0:14]:[cH;+0:15]:[cH;+0:16]:1).[*:1]-[c;H0;+0:2]1:[cH;+0:3]:[n+;H0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:22]:[c;H0;+0:23](=[O;H0;+0:33]):[*:30]1:[c;H0;+0:31](:[*:32])-[CH2;+0:25]-[CH2;+0:26]-[C;H0;+0:27]-1=[O;H0;+0:28].[CH3;+0:29]-[OH;+0:37].[O;H0;+0:38]=[C;H0;+0:24]=[O;H0;+0:39].[OH2;+0:21]
Reaction
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References

TitleAuthorsDatePubMed ID
Characterization of the critical amino acids of an Aspergillus parasiticus cytochrome P-450 monooxygenase encoded by ordA that is involved in the biosynthesis of aflatoxins B1, G1, B2, and G2.Yu J, Chang PK, Ehrlich KC, Cary JW, Montalbano B, Dyer JM, Bhatnagar D, Cleveland TE1998 Dec9835571
Enzymological evidence for separate pathways for aflatoxin B1 and B2 biosynthesis.Bhatnagar D, Cleveland TE, Kingston DG1991 Apr 301902378

RHEA:35759 8-O-methylsterigmatocystin + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = aflatoxin B1 + CO2 + 2 H(+) + H2O + methanol + 2 oxidized [NADPH--hemoprotein reductase]
RULE(radius=1) [*:1]-[C;H0;+0:2]1=[CH;+0:3]-[N;H0;+0:4](-[*:5])-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-1.([*:9]-[N;H0;+0:10]1-[CH;+0:11]=[C;H0;+0:12](-[*:13])-[CH2;+0:14]-[CH;+0:15]=[CH;+0:16]-1.[*:17]-[P;H0;+0:18](=[*:19])(-[*:20])-[OH;+0:21]).[*:22]:[c;H0;+0:23]1:[cH;+0:24]:[cH;+0:25]:[cH;+0:26]:[c;H0;+0:27](-[O;H0;+0:28]-[CH3;+0:29]):[*:30]:1:[c;H0;+0:31](:[*:32])=[O;H0;+0:33].[H+;H0:34].[H+;H0:35].[O;H0;+0:36]=[O;H0;+0:37].[O;H0;+0:38]=[O;H0;+0:39]>>([*:17]-[P;H0;+0:18](=[*:19])(-[*:20])-[OH;+0:36].[*:9]-[n+;H0:10]1:[cH;+0:11]:[c;H0;+0:12](-[*:13]):[cH;+0:14]:[cH;+0:15]:[cH;+0:16]:1).[*:1]-[c;H0;+0:2]1:[cH;+0:3]:[n+;H0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:22]:[c;H0;+0:23](=[O;H0;+0:33]):[*:30]1:[c;H0;+0:31](:[*:32])-[CH2;+0:25]-[CH2;+0:26]-[C;H0;+0:27]-1=[O;H0;+0:28].[CH3;+0:29]-[OH;+0:37].[O;H0;+0:38]=[C;H0;+0:24]=[O;H0;+0:39].[OH2;+0:21]
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Characterization of the critical amino acids of an Aspergillus parasiticus cytochrome P-450 monooxygenase encoded by ordA that is involved in the biosynthesis of aflatoxins B1, G1, B2, and G2.Yu J, Chang PK, Ehrlich KC, Cary JW, Montalbano B, Dyer JM, Bhatnagar D, Cleveland TE1998 Dec9835571
Enzymological evidence for separate pathways for aflatoxin B1 and B2 biosynthesis.Bhatnagar D, Cleveland TE, Kingston DG1991 Apr 301902378