Terpene

Malonyl-CoA O-methyltransferase
Identifiers
EC no.2.1.1.197
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
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NCBIproteins

Malonyl-CoA O-methyltransferase (EC 2.1.1.197, BioC) is an enzyme with systematic name S-adenosyl-L-methionine:malonyl-CoA O-methyltransferase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

S-adenosyl-L-methionine + malonyl-CoA S-adenosyl-L-homocysteine + malonyl-CoA methyl ester

Malonyl-CoA O-methyltransferase is involved in an early step of biotin biosynthesis in Gram-negative bacteria.

References[edit]

  1. ^ Del Campillo-Campbell A, Kayajanian G, Campbell A, Adhya S (December 1967). "Biotin-requiring mutants of Escherichia coli K-12". Journal of Bacteriology. 94 (6): 2065–6. PMC 276941. PMID 4864413.
  2. ^ Rolfe B, Eisenberg MA (August 1968). "Genetic and biochemical analysis of the biotin loci of Escherichia coli K-12". Journal of Bacteriology. 96 (2): 515–24. PMC 252325. PMID 4877129.
  3. ^ Otsuka AJ, Buoncristiani MR, Howard PK, Flamm J, Johnson C, Yamamoto R, Uchida K, Cook C, Ruppert J, Matsuzaki J (December 1988). "The Escherichia coli biotin biosynthetic enzyme sequences predicted from the nucleotide sequence of the bio operon". The Journal of Biological Chemistry. 263 (36): 19577–85. PMID 3058702.
  4. ^ Cleary PP, Campbell A (November 1972). "Deletion and complementation analysis of biotin gene cluster of Escherichia coli". Journal of Bacteriology. 112 (2): 830–9. PMC 251493. PMID 4563978.
  5. ^ Lin S, Hanson RE, Cronan JE (September 2010). "Biotin synthesis begins by hijacking the fatty acid synthetic pathway". Nature Chemical Biology. 6 (9): 682–8. doi:10.1038/nchembio.420. PMC 2925990. PMID 20693992.

External links[edit]

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