Uroporphyrinogen-III C-methyltransferase

Last updated
Uroporphyrinogen-III C-methyltransferase
Identifiers
EC no. 2.1.1.107
CAS no. 125752-76-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

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 overall chemical reaction

Contents

+ 2 SAM
 
 
 
 
Uroporphyrinogen-III C-methyltransferase
 
 
 
+ 2 SAH
 

The enzyme catalyses two methylation reactions. The first reaction converts uroporphyrinogen III into precorrin-1 and the second forms dihydrosirohydrochlorin (precorrin-2). In both cases the methyl group comes from the cofactor, S-adenosyl methionine (SAM), which loses its methyl group and becomes S-adenosyl-L-homocysteine (SAH). [4] These reactions are part of the biosynthetic pathway to cobalamin (vitamin B12) in both anaerobic and aerobic bacteria. [5]

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.
  4. Enzyme 2.1.1.107 at KEGG Pathway Database.
  5. Battersby, Alan R. (2000). "Tetrapyrroles: The pigments of life". Natural Product Reports. 17 (6): 507–526. doi:10.1039/b002635m. PMID   11152419.