Biology:Sterigmatocystin 8-O-methyltransferase
| Sterigmatocystin 7-O-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.1.110 | ||||||||
| CAS number | 116958-29-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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Sterigmatocystin 8-O-methyltransferase (EC 2.1.1.110) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
This is a methylation reaction in which the aflatoxin, sterigmatocystin, is converted to its methyl ether, 8-O-methylsterigmatocystin. The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which becomes S-adenosyl-L-homocysteine (SAH). The enzyme was characterised from Aspergillus parasiticus.[1]
-Aflatoxin_B1_Structural_Formulae_V.1.svg)
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:sterigmatocystin 8-O-methyltransferase. Other names in common use include sterigmatocystin methyltransferase, O-methyltransferase II, sterigmatocystin 7-O-methyltransferase (incorrect), S-adenosyl-L-methionine:sterigmatocystin 7-O-methyltransferase, and (incorrect).[2] It is part of the biosynthetic pathway to aflatoxin B1.[3]
References
- ↑ "Two distinct O-methyltransferases in aflatoxin biosynthesis". Appl. Environ. Microbiol. 55 (9): 2172–7. 1989. doi:10.1128/aem.55.9.2172-2177.1989. PMID 2802602. Bibcode: 1989ApEnM..55.2172Y.
- ↑ Enzyme 2.1.1.110 at KEGG Pathway Database.
- ↑ "Identification of O-methylsterigmatocystin as an aflatoxin B1 and G1 precursor in Aspergillus parasiticus". Appl. Environ. Microbiol. 53 (5): 1028–33. 1987. doi:10.1128/aem.53.5.1028-1033.1987. PMID 3111363. Bibcode: 1987ApEnM..53.1028B.
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