Information on EC 2.3.1.39 - [acyl-carrier-protein] S-malonyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
2.3.1.39
-
RECOMMENDED NAME
GeneOntology No.
[acyl-carrier-protein] S-malonyltransferase
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Fatty acid biosynthesis
-
fatty acid biosynthesis (plant mitochondria)
-
fatty acid biosynthesis initiation I
-
Metabolic pathways
-
octanoyl-ACP biosynthesis (mitochondria, yeast)
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
EtMCAT
-
-
FabD
Clostridium acetobutylicum ATCC824
-
-
-
FabD
-
gene name
FabD
Escherichia coli ML103
-
-
-
FabD
Streptomyces avermitilis MA-4680
-
-
-
FabD
Streptomyces coelicolor A3
-
-
-
FabD
-
gene name
HpMCAT
Q56S05
-
malonyl CoA-acyl carrier protein transacylase
Q56S05
-
malonyl CoA-acyl carrier protein transacylase
P63458
-
malonyl CoA-acyl carrier protein transacylase
-
-
malonyl coenzyme A-acyl carrier protein transacylase
-
-
-
-
malonyl coenzyme A:acyl carrier protein transacylase
-
-
malonyl transacylase
-
-
-
-
malonyl transferase
-
-
-
-
malonyl-CoA acyl carrier protein transacylase
P63458
-
malonyl-CoA-acyl carrier protein transacylase
-
-
-
-
malonyl-CoA-acyl carrier protein transacylase
Q99UN8
-
malonyl-CoA-acyl carrier protein transacylase
-
-
malonyl-CoA:ACP transacylase
-
-
malonyl-CoA:AcpM transacylase
-
-
malonyl-CoA:acyl carrier protein transacylase
-
-
malonyl-CoA:acyl carrier protein transacylase
Clostridium acetobutylicum ATCC824
-
-
-
malonyl-CoA:acyl carrier protein transacylase
-
-
malonyl-CoA:acyl carrier protein transacylase
-
-
malonyl-CoA:acyl carrier protein transacylase
-
-
malonyl-CoA:acyl carrier protein transacylase
Escherichia coli ML103
-
-
-
malonyl-CoA:acyl carrier protein transacylase
-
-
malonyl-CoA:acyl carrier protein transacylase
Streptomyces avermitilis MA-4680
-
-
-
malonyl-CoA:acyl carrier protein transacylase
-
-
malonyl-CoA:acyl carrier protein transacylase
Streptomyces coelicolor A3
-
-
-
malonyl-CoA–acyl carrier protein transacylase
-
-
malonyl-coenzyme A:ACP transacylase
-
-
malonyltransferase, [acyl-carrier-protein]
-
-
-
-
MCT
Clostridium acetobutylicum ATCC824
-
-
-
MCT
Escherichia coli ML103
-
-
-
MCT
Streptomyces avermitilis MA-4680
-
-
-
SaMCAT
Q99UN8
-
[acyl carrier protein]malonyltransferase
-
-
-
-
MCT
Streptomyces coelicolor A3
-
-
-
additional information
-
in vertebrates, yeast and mycobacteria malonyl transferase activity is a domain of the multifunctional polypeptide chains of fatty acid synthase EC 2.3.1.85 and EC 2.3.1.86
additional information
-
in vertebrates, yeast and mycobacteria malonyl transferase activity is a domain of the multifunctional polypeptide chains of fatty acid synthase EC 2.3.1.85 and EC 2.3.1.86
CAS REGISTRY NUMBER
COMMENTARY
37257-17-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Clostridium acetobutylicum ATCC824
-
-
-
Manually annotated by BRENDA team
Lythraceae
-
-
Manually annotated by BRENDA team
Escherichia coli ML103
-
-
-
Manually annotated by BRENDA team
Euglena gracilis Z
Z
-
-
Manually annotated by BRENDA team
soy bean, strain AMSOY71
-
-
Manually annotated by BRENDA team
strain BCG, ATCC 35734
-
-
Manually annotated by BRENDA team
avocado
-
-
Manually annotated by BRENDA team
61-3
Q9WXI0
SwissProt
Manually annotated by BRENDA team
61-3
Q9WXI0
SwissProt
Manually annotated by BRENDA team
malonyl transferase domain of EC 2.3.1.85
-
-
Manually annotated by BRENDA team
Streptomyces avermitilis MA-4680
-
-
-
Manually annotated by BRENDA team
Streptomyces coelicolor A3
-
-
-
Manually annotated by BRENDA team
produces tetracenomicin C
-
-
Manually annotated by BRENDA team
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
activation
dithiothreitol
-
stimulates
malonate
-
at 0.1 mM, MCT1 is doubled in activity and MCT2 is 30-40% than control
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.01647
-
corytuberine
-
pH 6.8, 28°C
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
10
-
about half-maximal activity at pH 5.0, about 80% of maximal activity at pH 10.0
6.2
9.8
-
about half-maximal activity at pH 6.2, about 65% of maximal activity at pH 9.8
7.5
8.5
-
maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
isozymes 1 and 2
Manually annotated by BRENDA team
-
isozyme 1 is predominant
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bartonella henselae (strain ATCC 49882 / Houston 1)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A)
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
Xanthomonas oryzae pv. oryzae (strain MAFF 311018)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
computer analysis predicts that EtMCAT protein contains a 20 aa N-terminal signal peptide plus 37 aa transit peptide for targeting and translocating into the apicoplast
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
of malonyl-enzyme intermediate