Uroporphyrinogen-III C-methyltransferase

Uroporphyrinogen-III C-methyltransferase (EC 2.1.1.107), uroporphyrinogen methyltransferase, uroporphyrinogen-III methyltransferase, adenosylmethionine-uroporphyrinogen III methyltransferase, S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase, uroporphyrinogen-III methylase, SirA, CysG, CobA, uroporphyrin-III C-methyltransferase, S-adenosyl-L-methionine:uroporphyrin-III C-methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:uroporphyrinogen-III C-methyltransferase.[1][2][3] This enzyme catalyses the following chemical reaction

2 S-adenosyl-L-methionine + uroporphyrinogen III 2 S-adenosyl-L-homocysteine + precorrin-2 (overall reaction)
(1a) S-adenosyl-L-methionine + uroporphyrinogen III S-adenosyl-L-homocysteine + precorrin-1
(1b) S-adenosyl-L-methionine + precorrin-1 S-adenosyl-L-homocysteine + precorrin-2
uroporphyrinogen III substrate of the enzyme
precorrin-2 product of the enzyme
Uroporphyrinogen-III C-methyltransferase
Identifiers
EC number2.1.1.107
CAS number125752-76-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Uroporphyrinogen-III C-methyltransferase catalyses two methylation reactions. The first reaction converts uroporphyrinogen III into precorrin-1. The second converts precorrin-1 into precorrin-2. These reactions are part of the biosynthetic pathway to cobalamin (vitamin B12) in both anaerobic and aerobic bacteria.

See also

References
  1. Warren MJ, Gonzalez MD, Williams HJ, Stolowich NJ, Scott AI (1990). "Uroporphyrinogen-III methylase catalyzes the enzymatic-synthesis of sirohydrochlorin-II and sirohydrochlorin-IV by a clockwise mechanism". J. Am. Chem. Soc. 112: 5343–5345. doi:10.1021/ja00169a048.
  2. Warren MJ, Roessner CA, Santander PJ, Scott AI (February 1990). "The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase". The Biochemical Journal. 265 (3): 725–9. doi:10.1042/bj2650725. PMC 1133693. PMID 2407234.
  3. Schubert HL, Raux E, Brindley AA, Leech HK, Wilson KS, Hill CP, Warren MJ (May 2002). "The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase". The EMBO Journal. 21 (9): 2068–75. doi:10.1093/emboj/21.9.2068. PMC 125995. PMID 11980703.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.