From Wikipedia, the free encyclopedia
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
⇌
{\displaystyle \rightleftharpoons }
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
^ 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 .
^ 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 .
^ 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 .
^ 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 .
^ 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
Activity Regulation Classification Kinetics Types