Information on EC 2.3.1.39 - [acyl-carrier-protein] S-malonyltransferase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC2.3.1.39
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
2.3.1.39
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RECOMMENDED NAME
GeneOntology No.
[acyl-carrier-protein] S-malonyltransferase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
fatty acid biosynthesis (plant mitochondria)
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fatty acid biosynthesis initiation I
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mupirocin biosynthesis
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octanoyl-[acyl-carrier protein] biosynthesis (mitochondria, yeast)
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lipid metabolism
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Fatty acid biosynthesis
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Metabolic 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 4.1.1.89 (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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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
additional information
?
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enzyme is part of the malonyl-CoA-dependent type II fatty acid synthase complex in mitochondria
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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absolutely specific for the substrates, type II [acyl-carrier protein]
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?
additional information
?
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enzyme is part of the malonyl-CoA-dependent type II fatty acid synthase complex in mitochondria
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
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recombinant enzyme with recombinant ACP-A from Bacillus subtilis
0.14
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recombinant enzyme with recombinant human mitochondrial [acyl-carrier protein] lacking the first 68 amino acid residues
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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enzyme is part of the malonyl-CoA-dependent type II fatty acid synthase complex in mitochondria, and contains a mitochondrial targeting sequence
Manually annotated by BRENDA team
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant truncated enzyme forms from Sf9 insect cells
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic tree, expression as GFP-fusion protein containing the mitochondrial targeting sequence in mitochondria of HeLa cells, expression of truncated enzyme forms lacking the first 21 or 59 amino acid residues, respectively, in Escherichia coli strain BL21(DE3) as soluble enzymes, or in Spodoptera frugiperda Sf9 cells via baculovirus infection system
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