Information on EC 2.1.1.197 - malonyl-[acyl-carrier protein] O-methyltransferase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
2.1.1.197
-
RECOMMENDED NAME
GeneOntology No.
malonyl-[acyl-carrier protein] O-methyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + malonyl-[acyl-carrier protein] = S-adenosyl-L-homocysteine + malonyl-[acyl-carrier protein] methyl ester
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
8-amino-7-oxononanoate biosynthesis I
-
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Biotin metabolism
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Metabolic pathways
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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]
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
BioC
-
gene name
S-adenosyl-L-methionine-dependent methyltransferase
-
-
SAM-dependent methyltransferase
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Bacillus cereus ATCC10987
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UniProt
Manually annotated by BRENDA team
; gene bioC
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
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
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deletion and complementation analysis of the biotin gene cluster. Mutants in BioC are blocked early in the biosynthetic pathway and complement mutants in bioA, bioB, and bioD
physiological function
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in biotin synthesis, the pimeloyl moiety 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. Supplementation of biotin-free medium with any of malonic, glutaric and pimelic acid monomethyl ester allows for acyl-ACP-synthetase-dependent growth of the bioC deletion strain; the role of BioC is to convert the free carboxyl group of a malonylthioester to its methyl ester by transfer of a methyl group from SAM. Methylation both cancels the charge of the carboxyl group and provides a methyl carbon to mimic the methyl ends of normal fatty acyl chains
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
?
S-adenosyl-L-methionine + malonyl-CoA
S-adenosyl-L-homocysteine + malonyl-CoA methyl ester
show the reaction diagram
-
-
?
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
?
S-adenosyl-L-methionine + malonyl-CoA
S-adenosyl-L-homocysteine + malonyl-CoA methyl ester
show the reaction diagram
Bacillus cereus ATCC10987
-
-
?
S-adenosyl-L-methionine + malonyl-[acyl-carrier protein]
S-adenosyl-L-homocysteine + malonyl-[acyl-carrier protein] methyl ester
show the reaction diagram
acyl-carrier protein from Escherichia coli
-
?
S-adenosyl-L-methionine + malonyl-[acyl-carrier protein]
S-adenosyl-L-homocysteine + malonyl-[acyl-carrier protein] methyl ester
show the reaction diagram
Bacillus cereus ATCC10987
acyl-carrier protein from Escherichia coli
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?
additional information
?
-
Bacillus cereus, Bacillus cereus ATCC10987
holo-[acyl-carrier protein], acetyl-[acyl-carrier protein], succinyl-[acyl-carrier protein], and glutaryl-[acyl-carrier protein] are no substrates
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
?
S-adenosyl-L-methionine + malonyl-[acyl-carrier protein]
S-adenosyl-L-homocysteine + malonyl-[acyl-carrier protein] methyl ester
show the reaction diagram
Bacillus cereus, Bacillus cereus ATCC10987
Q731I1
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
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-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
addition of metal ions neither enhances nor reduces the activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-homocysteine
product inhibition
sinefungin
0.1 micromol, 60% reduction of activity
additional information
not inhibitory: 5'-deoxyadenosine, methylthioadenosine, adenosine, L-homocysteine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00108
malonyl-[acyl-carrier protein]
pH 7, 37C
0.0019
S-adenosyl-L-methionine
pH 7, 37C, cosubstrate malonyl-[acyl-carrier protein]
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
225
malonyl-[acyl-carrier protein]
Bacillus cereus
Q731I1
pH 7, 37C
173
S-adenosyl-L-methionine
Bacillus cereus
Q731I1
pH 7, 37C, cosubstrate malonyl-[acyl-carrier protein]
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
91050
malonyl-[acyl-carrier protein]
Bacillus cereus
Q731I1
pH 7, 37C
811
20830
S-adenosyl-L-methionine
Bacillus cereus
Q731I1
pH 7, 37C, cosubstrate malonyl-[acyl-carrier protein]
24
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.5
less than 50% of maximal activity above and below
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.4
calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 28322, calculated
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
functional expression in Escherichia coli
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
deletion and complementation analysis of the biotin gene cluster. Mutants in BioC are blocked early in the biosynthetic pathway and complement mutants in bioA, bioB, and bioD
additional information
-
construction of the DELTAbioC deletion mutant, that is only able to grow in biotin and derivative supplemented medium. Escherichia coli strain ER90 DELTAbioF bioC bioD carries an insertion-deletion mutation within bioF that also inactivates the downstream genes, bioC and bioD, by transcriptional polarity
additional information
-
complementational analysis of biotin-requiring mutants. Biotin biosynthesis is controlled by a closely linked cluster of at least four genes mediating different steps in the process
additional information
complementation of Escherichia coli mutant lacking the biotin operon by Erwinia herbicola biotin operon