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Information on EC 2.3.1.39 - [acyl-carrier-protein] S-malonyltransferase and Organism(s) Staphylococcus aureus and UniProt Accession Q99UN8

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IUBMB Comments
This enzyme, along with EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. This enzyme also provides the malonyl groups for polyketide biosynthesis . The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis. In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7, holo-[acyl-carrier-protein] synthase) is the preferred substrate . This enzyme also forms part of the multienzyme complexes EC 4.1.1.88, biotin-independent malonate decarboxylase and EC 7.2.4.4, biotin-dependent malonate decarboxylase. Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase . In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot whereas the enzyme from Pseudomonas putida can use both as substrates . The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA prosthetic group.
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Staphylococcus aureus
UNIPROT: Q99UN8
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The taxonomic range for the selected organisms is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
fatty acid synthase, malonyl-coa:acp transacylase, malonyl transferase, mtfabd, hpmcat, fabd2, malonyl-coa:acyl carrier protein transacylase, malonyl coa-acyl carrier protein transacylase, malonyl-coa-acyl carrier protein transacylase, mcamt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malonyl-CoA-acyl carrier protein transacylase
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malonyl coenzyme A-acyl carrier protein transacylase
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malonyl transacylase
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malonyl transferase
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malonyl-CoA-acyl carrier protein transacylase
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malonyltransferase, [acyl-carrier-protein]
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[acyl carrier protein]malonyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:[acyl-carrier protein] S-malonyltransferase
This enzyme, along with EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. This enzyme also provides the malonyl groups for polyketide biosynthesis [7]. The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis. In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7, holo-[acyl-carrier-protein] synthase) is the preferred substrate [5]. This enzyme also forms part of the multienzyme complexes EC 4.1.1.88, biotin-independent malonate decarboxylase and EC 7.2.4.4, biotin-dependent malonate decarboxylase. Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase [12]. In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot [10] whereas the enzyme from Pseudomonas putida can use both as substrates [11]. The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA prosthetic group.
CAS REGISTRY NUMBER
COMMENTARY hide
37257-17-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
alpha-ketoglutarate dehydrogenase (KDH)-coupled assay system is used: KDH-dependent consumption of coenzyme A (CoA) generated by MCAT is accompanied by a reduction of nicotinamide adenine dinucleotide (NAD+) to NADH
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of MCAT from Staphylococcus aureus and Streptococcus pneumoniae are determined at 1.46 and 2.1 A resolution, respectively. In the SaMCAT structure, the N-terminal expression peptide of a neighboring molecule running in the opposite direction of malonyl-CoA makes extensive interactions with the highly conserved Gly-Gln-Gly-Ser-Gln stretch, suggesting a new design platform
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hong, S.K.; Kim, K.H.; Kim, E.E.
Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of MCAT from Staphylococcus aureus
Acta Crystallogr. Sect. F
66
20-22
2010
Staphylococcus aureus (Q99UN8), Staphylococcus aureus
Manually annotated by BRENDA team
Hong, S.K.; Kim, K.H.; Park, J.K.; Jeong, K.W.; Kim, Y.; Kim, E.E.
New design platform for malonyl-CoA-acyl carrier protein transacylase
FEBS Lett.
584
1240-1244
2010
Streptococcus pneumoniae, Staphylococcus aureus (Q99UN8), Staphylococcus aureus
Manually annotated by BRENDA team