Precorrin-3B C17-methyltransferase
{{infobox enzyme
| Name = precorrin-3B C17-methyltransferase
| EC_number = 2.1.1.131
| CAS_number = 152787-64-9
| GO_code = 0030789
| image =
| width =
| caption =
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In enzymology, precorrin-3B C17-methyltransferase ({{EC number|2.1.1.131}}) is an enzyme that catalyzes the chemical reaction
:S-adenosyl-L-methionine + precorrin-3B S-adenosyl-L-homocysteine + precorrin-4
The two substrates of this enzyme are S-adenosyl methionine and precorrin 3B, and its two products are S-adenosylhomocysteine and precorrin 4.
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:precorrin-3B C17-methyltransferase. Other names in common use include precorrin-3 methyltransferase, and CobJ. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria and during this step the macrocycle ring-contracts so that the corrin core of the vitamin is formed.
See also
References
{{reflist|1}}
- {{cite journal | vauthors = Scott AI, Roessner CA, Stolowich NJ, Spencer JB, Min C, Ozaki SI | date = 1993 | title = Biosynthesis of vitamin B12. Discovery of the enzymes for oxidative ring contraction and insertion of the fourth methyl group | journal = FEBS Lett. | volume = 331 | pages = 105–8 | pmid = 8405386 | doi = 10.1016/0014-5793(93)80306-F | issue = 1–2 | doi-access = free }}
- {{cite journal | vauthors = Debussche L, Thibaut D, Cameron B, Crouzet J, Blanche F | date = 1993 | title = Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas denitrificans | journal = J. Bacteriol. | volume = 175 | pages = 7430–40 | pmid = 8226690 | issue = 22 | pmc = 206888 }}
{{One carbon transferases}}
{{Enzymes}}
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Category:Enzymes of unknown structure
{{2.1-enzyme-stub}}