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Information on EC 2.1.1.197 - malonyl-[acyl-carrier protein] O-methyltransferase and Organism(s) Escherichia coli and UniProt Accession P12999

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IUBMB Comments
Involved in an early step of biotin biosynthesis in Gram-negative bacteria. This enzyme catalyses the transfer of a methyl group to the omega-carboxyl group of malonyl-[acyl-carrier protein] forming a methyl ester. The methyl ester is recognized by the fatty acid synthetic enzymes, which process it via the fatty acid elongation cycle to give pimelyl-[acyl-carrier-protein] methyl ester . While the enzyme can also accept malonyl-CoA, it has a much higher activity with malonyl-[acyl-carrier protein]
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This record set is specific for:
Escherichia coli
UNIPROT: P12999
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
sam-dependent methyltransferase, s-adenosyl-l-methionine-dependent methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S-adenosyl-L-methionine-dependent methyltransferase
-
-
SAM-dependent methyltransferase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:malonyl-[acyl-carrier protein] O-methyltransferase
Involved in an early step of biotin biosynthesis in Gram-negative bacteria. This enzyme catalyses the transfer of a methyl group to the omega-carboxyl group of malonyl-[acyl-carrier protein] forming a methyl ester. The methyl ester is recognized by the fatty acid synthetic enzymes, which process it via the fatty acid elongation cycle to give pimelyl-[acyl-carrier-protein] methyl ester [5]. While the enzyme can also accept malonyl-CoA, it has a much higher activity with malonyl-[acyl-carrier protein] [6]
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + malonyl-CoA
S-adenosyl-L-homocysteine + malonyl-CoA methyl ester
show the reaction diagram
-
-
the methyl ester moiety is essential for chain elongation
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + malonyl-CoA
S-adenosyl-L-homocysteine + malonyl-CoA methyl ester
show the reaction diagram
-
-
the methyl ester moiety is essential for chain elongation
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.4
calculated
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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the DELTAbioC deletion mutant is only able to grow in biotin supplemented medium. Also supplementation with pimelic acid, and putative intermediates in the pathway, the enoyl, 3-keto and 3-hydroxy derivatives of the monomethyl ester of glutarate and the 3-keto and 3-hydroxy derivatives of the monomethyl ester of pimelate, allow growth of the mutant strain in the absence of biotin, but the 2-keto, 2-hydroxy and 4-keto derivatives, as well as monomethyl esters of C4, C6, C8, C9 and C11 dicarboxylates, do not, overview
metabolism
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the pimeloyl moiety of biotin is synthesized by a modified fatty acid synthetic pathway in which the omega-carboxyl group of a malonyl-thioester is methylated by BioC which allows recognition of this atypical substrate by the fatty acid synthetic enzymes. The malonyl-thioester methyl ester enters fatty acid synthesis as the primer and undergoes two reiterations of the fatty acid elongation cycle to give pimeloyl-acyl carrier protein methyl ester which is hydrolyzed to pimeloyl-ACP and methanol by BioH
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28322
x * 28322, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 28322, calculated
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the biotin operon contains the five biotin operon genes, bioA, B, F, C, and D, and an open reading frame of unknown function. The operon is negatively regulated and divergently transcribed from a control region between the bioA and bioB genes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Otsuka, A.J.; Buoncristiani, M.R.; Howard, P.K.; Flamm, J.; Johnson, C.; Yamamoto, R.; Uchida, K.; Cook, C.; Ruppert, J.; Matsuzaki, J.
The Escherichia coli biotin biosynthetic enzyme sequences predicted from the nucleotide sequence of the bio operon
J. Biol. Chem.
263
19577-19585
1988
Escherichia coli (P12999)
Manually annotated by BRENDA team
Cleary, P.P.; Campbell, A.
Deletion and complementation analysis of biotin gene cluster of Escherichia coli
J. Bacteriol.
112
830-839
1972
Escherichia coli
Manually annotated by BRENDA team
Lin, S.; Hanson, R.E.; Cronan, J.E.
Biotin synthesis begins by hijacking the fatty acid synthetic pathway
Nat. Chem. Biol.
6
682-688
2010
Escherichia coli
Manually annotated by BRENDA team