Precorrin-8X methylmutase
{{infobox enzyme
| Name = precorrin-8X methylmutase
| EC_number = 5.4.99.61
| CAS_number =
| GO_code = 0016993
| image = 1i1h.png
| width =
| caption = Crystal structure of precorrin-8x methyl mutase with bound hydrogenobyrinate. PDB {{PDBe|1i1h}}{{Cite journal
| last1 = Shipman | first1 = L. W.
| last2 = Li | first2 = D.
| last3 = Roessner | first3 = C. A.
| last4 = Scott | first4 = A. I.
| last5 = Sacchettini | first5 = J. C.
| title = Crystal structure of precorrin-8x methyl mutase
| journal = Structure
| volume = 9
| issue = 7
| pages = 587–596
| year = 2001
| pmid = 11470433 | doi=10.1016/s0969-2126(01)00618-9
| doi-access = free
}}
}}
In enzymology, a precorrin-8X methylmutase ({{EC number|5.4.99.61}}) is an enzyme that catalyzes the chemical reaction
:precorrin-8X hydrogenobyrinate
Hence, this enzyme has one substrate, precorrin 8X, and one product, hydrogenobyrinate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is precorrin-8X 11,12-methylmutase. Other names in common use include precorrin isomerase, hydrogenobyrinic acid-binding protein and CobH. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in aerobic bacteria.
See also
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1F2V}}, {{PDB link|1I1H}}, {{PDB link|1OU0}}, {{PDB link|1V9C}}, {{PDB link|2AFR}}, and {{PDB link|2AFV}}.
References
{{reflist|1}}
- {{cite journal | author = Blanche F | date = 1992 | title = The final step in the biosynthesis of hydrogenobyrinic acid is catalyzed by the cobH gene product with precorrin-8x as the substrate | journal = J. Bacteriol. | volume = 174 | pages = 1043–9 | pmid = 1732194 | last2 = Couder | first2 = M | last3 = Famechon | first3 = A | last4 = Debussche | first4 = L | last5 = Cameron | first5 = B | last6 = Crouzet | first6 = J | last7 = Blanche | first7 = F | issue = 3 | doi = 10.1128/JB.174.3.1043-1049.1992 | pmc = 206186 }}
- {{cite journal | vauthors = Roth JR, Lawrence JG, Rubenfield M, Kieffer-Higgins S, Church GM | date = 1993 | title = Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium | journal = J. Bacteriol. | volume = 175 | pages = 3303–16 | pmid = 8501034 | issue = 11 | pmc = 204727 | doi=10.1128/jb.175.11.3303-3316.1993}}
- {{cite journal | vauthors = Stolowich NJ, Iida K, Scott AI | date = 1992 | title = Expression of 9 Salmonella typhimurium enzymes for cobinamide synthesis. Identification of the 11-methyl and 20-methyl transferases of corrin biosynthesis | journal = FEBS Lett. | volume = 301 | pages = 73–8 | pmid = 1451790 | doi = 10.1016/0014-5793(92)80213-Z | issue = 1 | s2cid = 20198692 | doi-access = free | bibcode = 1992FEBSL.301...73R }}
- {{cite journal | vauthors = Thibaut D, Debussche L | date = 1990 | title = Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans fragment carrying eight genes involved in transformation of precorrin-2 to cobyrinic acid | journal = J. Bacteriol. | volume = 172 | pages = 5980–90 | pmid = 2211521 | issue = 10 | doi = 10.1128/JB.172.10.5980-5990.1990 | pmc = 526920 }}
{{Mutases}}
{{Enzymes}}
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Category:Enzymes of known structure
{{isomerase-stub}}