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
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
mechanism, formation of a malonyl-enzyme intermediate
-
malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
isolation and characterization of an enzyme-intermediate; mechanism, formation of a malonyl-enzyme intermediate
-
malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
isolation and characterization of an enzyme-intermediate
-
malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
mechanism, kinetic studies
-
malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
mechanism, kinetic studies
-
malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
putative active site structure and involved catalytic residues
-
malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
catalytic mechanism, [acyl-carrier protein] binding site, residues Phe200 and Met126 are involved
-
malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
the catalytic malonyl transferase activity is intrinsic to an individual acyl carrier protein. An arginine/lysine in loop II and an arginine/glutamine in helix III are the catalytic residues for transferase function. The hydrogen bonding properties of these residues are indespensible for the transferase reaction
-
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-CoAacyl 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
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
the effect of overexpressing four different malonyl transacylases on fatty acid production is evaluated in an Escherichia coli fatty acid overproducing strain ML103(pXZ18). The strain carrying an acyl-ACP TE gene and a fabD gene from Escherichia coli, Streptomyces avermitilis MA-4680, or Streptomyces coelicolor A3 produce more free fatty acid than the control strain, whereas the strain carrying an acyl-ACP TE gene and a fabD gene from Clostridium acetobutylicum ATCC 824 produce similar quantity of free fatty acid as the control strain
malfunction
-
functional replacement of the fabD gene with amber mutation of Escherichia coli temperature-sensitive LA2-89 strain by Eimeria tenella EtMCAT demonstrates that EcFabD and EtMCAT perform the same biochemical function
malfunction
Clostridium acetobutylicum ATCC824, Escherichia coli ML103, Streptomyces avermitilis MA-4680, Streptomyces coelicolor A3
-
the effect of overexpressing four different malonyl transacylases on fatty acid production is evaluated in an Escherichia coli fatty acid overproducing strain ML103(pXZ18). The strain carrying an acyl-ACP TE gene and a fabD gene from Escherichia coli, Streptomyces avermitilis MA-4680, or Streptomyces coelicolor A3 produce more free fatty acid than the control strain, whereas the strain carrying an acyl-ACP TE gene and a fabD gene from Clostridium acetobutylicum ATCC 824 produce similar quantity of free fatty acid as the control strain
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
r
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
both isozymes may not be completely specific for malonyl-CoA as the substrate
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
holo-acyl-carrier-protein from Mycobacterium tuberculosis constitutes the preferred substrate for the enzyme, however the enzyme uses both E. coli holo-acyl-carrier-protein and Mycobacterium tuberculosis holo-acyl-carrier-protein as substrates for transacylation in vivo and in vitro
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
the recombinant enzyme is able to use E. coli acyl-carrier-protein, Streptomyces glaucescens acyl-carrier-protein as well as the tetracenomycin M acyl-carrier-protein component of the tetracenomycin type II polyketide synthase
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
acetyl-CoA cannot replace malonyl-CoA
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
acetyl-CoA cannot replace malonyl-CoA
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
acetyl-CoA cannot replace malonyl-CoA
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
acetyl-CoA cannot replace malonyl-CoA
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
acetyl-CoA cannot replace malonyl-CoA
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
acetyl-CoA cannot replace malonyl-CoA
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
the enzyme is very specific for the malonyl group
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
the enzyme is very specific for the malonyl group
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
characterization of acyl-carrier protein
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
characterization of acyl-carrier protein
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
characterization of acyl-carrier protein
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
via stable covalent malonyl-enzyme intermediate
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
via stable covalent malonyl-enzyme intermediate
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
via stable covalent malonyl-enzyme intermediate
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
via stable covalent malonyl-enzyme intermediate
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
via stable covalent malonyl-enzyme intermediate
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
via stable covalent malonyl-enzyme intermediate
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
via stable covalent malonyl-enzyme intermediate
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
via stable covalent malonyl-enzyme intermediate
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
via stable covalent malonyl-enzyme intermediate
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
via stable covalent malonyl-enzyme intermediate
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
via stable covalent malonyl-enzyme intermediate
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
via stable covalent malonyl-enzyme intermediate
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
participation of a malonyl-enzyme intermediate in the reaction
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
Streptomyces coelicolor actinorhodin polyketide synthase acyl carrier protein can catalyze transfer of malonate to type II Streptomyces coelicolor fatty acid synthase and other polyketide synthase acyl carrier protein in vitro
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
Euglena gracilis Z
-
via stable covalent malonyl-enzyme intermediate
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-acyl-carrier protein
show the reaction diagram
-
-
-
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-acyl-carrier protein
show the reaction diagram
-
initial reaction in de novo fatty acid synthesis, part of non-associated fatty acid synthase system of plants and prokaryotes
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-acyl-carrier protein
show the reaction diagram
-
initial reaction in de novo fatty acid synthesis, part of non-associated fatty acid synthase system of plants and prokaryotes
-
r
malonyl-CoA + acyl-carrier protein
CoA + malonyl-acyl-carrier protein
show the reaction diagram
-
the enzyme is a component of the fatty acid synthetase system
-
?
malonyl-CoA + N-(N-acetyl-beta-alanyl)cysteamine
CoA + N-(N-acetyl-beta-alanyl)-S-malonylcysteamine
show the reaction diagram
-
-
-
-
?
malonyl-CoA + N-acetylcysteamine
CoA + N-acetyl-S-malonylcysteamine
show the reaction diagram
-
-
-
-
?
malonyl-CoA + N-acetylcysteamine
CoA + N-acetyl-S-malonylcysteamine
show the reaction diagram
-
in the presence of high N-acetylcysteamine concentrations the forward reaction can be driven to completion
-
-
?
malonyl-CoA + pantetheine
malonyl-pantetheine + CoA
show the reaction diagram
-
-
-
-
?
malonyl-CoA + pantetheine
malonyl-pantetheine + CoA
show the reaction diagram
-
-
-
-
?
malonyl-CoA + pantetheine
malonyl-pantetheine + CoA
show the reaction diagram
-
reaction catalysed by the malonyl transferase domain of EC 2.3.1.85
-
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
absolutely specific for the substrates, type II [acyl-carrier protein]
-
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
enzyme is involved in both fatty acid and polyketide synthesis pathways
-
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
enzyme provides acyl-ACP thioesters for the biosynthesis of aromatic polyketides, overview, and thus is the primary gatekeeper of substrate specificity in type II polyketide synthase
-
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
key enzyme in fatty acid synthesis
malonyl-[acyl-carrier protein] is the key building block for de novo fatty acid synthesis
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
absolutely specific for the substrates, recombinant type II [acyl-carrier protein] lacking the N-terminal 68 amino acid residues from human, or recombinant ACP-A from Bacillus subtilis
-
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
enzyme is active with a type II [acyl-carrier protein] from a recombinant modular polyketid synthase with inactivated acyl transferase domain, overview
-
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
the active site is rigorously ordered around the acyl-thioester moiety of the acyl-CoA to facilitate rapid and efficient transacylation to an ACP
-
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
transfer to the free thiol group of the phosphopantetheine arm of the [acyl-carrier protein]
-
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
type II [acyl-carrier protein] from Plasmodium falsiparum
-
-
?
malonyl-pantetheine + acyl-carrier protein
pantetheine + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
mercaptoethanol is inactive as a substitute for acyl-carrier-protein
-
-
-
additional information
?
-
-
the enzyme is responsible for charging the tetracenomycin M acyl-carrier-protein with malonate in vivo, a key step in the synthesis of the deca(polyketide) precursor of tetracenomycin C. This implies the existence of a functional connection between fatty acid and polyketide metabolism in this bacterium
-
-
-
additional information
?
-
-
enzyme is part of the malonyl-CoA-dependent type II fatty acid synthase complex in mitochondria
-
-
-
additional information
?
-
-
enzyme is part of the malonyl-CoA-dependent type II fatty acid synthase complex in mitochondria, reaction sequence of the involved enzymes, overview
-
-
-
additional information
?
-
-
development of a continuous fluorometric coupled assay method in microplates by coupling of the enzyme to alpha-ketoglutarate dehydrogenase consuming CoA, overview
-
-
-
additional information
?
-
-
the beta-ketoacyl ACP synthase also catalyzes the reaction with low activity, overview, no activity with a recombinant type II [acyl-carrier protein] from Plasmodium falsiparum containing an N-terminal apicoplast transit peptide
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
malonyl-CoA + acyl-carrier protein
CoA + malonyl-acyl-carrier protein
show the reaction diagram
-
initial reaction in de novo fatty acid synthesis, part of non-associated fatty acid synthase system of plants and prokaryotes
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-acyl-carrier protein
show the reaction diagram
-
initial reaction in de novo fatty acid synthesis, part of non-associated fatty acid synthase system of plants and prokaryotes
-
r
malonyl-CoA + acyl-carrier protein
CoA + malonyl-acyl-carrier protein
show the reaction diagram
-
the enzyme is a component of the fatty acid synthetase system
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
absolutely specific for the substrates, type II [acyl-carrier protein]
-
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
enzyme is involved in both fatty acid and polyketide synthesis pathways
-
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
enzyme provides acyl-ACP thioesters for the biosynthesis of aromatic polyketides, overview, and thus is the primary gatekeeper of substrate specificity in type II polyketide synthase
-
-
?
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
-
key enzyme in fatty acid synthesis
malonyl-[acyl-carrier protein] is the key building block for de novo fatty acid synthesis
-
?
additional information
?
-
-
the enzyme is responsible for charging the tetracenomycin M acyl-carrier-protein with malonate in vivo, a key step in the synthesis of the deca(polyketide) precursor of tetracenomycin C. This implies the existence of a functional connection between fatty acid and polyketide metabolism in this bacterium
-
-
-
additional information
?
-
-
enzyme is part of the malonyl-CoA-dependent type II fatty acid synthase complex in mitochondria
-
-
-
additional information
?
-
-
enzyme is part of the malonyl-CoA-dependent type II fatty acid synthase complex in mitochondria, reaction sequence of the involved enzymes, overview
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetoacetyl-CoA
-
inhibition of both isozymes at 0.02 mM and at 0.1 mM
acetyl-CoA
-
competitive to malonyl-CoA
CaCl2
-
1 mM, 17% inhibition
CoA
-
not inhibitory
corytuberine
-
-
-
diethyldicarbonate
-
inhibits MCT1 but not MCT2 at 1 mM
EDTA
-
63% inhibition at 1 mM, complete inhibition at 10 mM
iodoacetamide
-
-
iodoacetamide
-
59% inhibition at 0.1 mM
iodoacetamide
-
malonyl-CoA protects; pH-dependent
iodoacetate
-
-
Isoniazid
-
acts synergistically with trifluoroperazine
malonyl-CoA
-
inhibition of MCT1 at 0.01 mM and inhibition of both isozymes at 0.02 mM and 0.04 mM; inhibits both MCT1 and MCT2
methylmalonyl-CoA
-
inhibition of MCT1 at 0.1 mM
MgCl2
-
1 mM, 34% inhibition
N-ethylmaleimide
-
79% inhibition at 0.1 mM
N-ethylmaleimide
-
malonyl-CoA protects; pH-dependent inhibition of purified enzyme
N-ethylmaleimide
-
-
N-ethylmaleimide
-
1 mM, isozyme MCT2: 40% loss of activity of isozyme MCT2, no effect on isozyme MCT1, both, MCT1 and MCT2, are inactivated at 10 mM
NiSO4
-
1 mM, 12% inhibition
p-chloromercuribenzoate
-
pH-independent
p-chloromercuribenzoate
-
strong
p-toluenesulfonyl fluoride
-
strong inhibitor
phenylmethanesulfonyl fluoride
-
malonyl-CoA protects
phenylmethanesulfonyl fluoride
-
not inhibitory
phenylmethanesulfonyl fluoride
-
-
phenylmethanesulfonyl fluoride
-
-
propionyl-CoA
-
inhibition of both isozymes at 0.1 mM
reduced CoA
-
inhibition of both isozymes at 0.1 mM
succinyl-CoA
-
inhibition of MCT2 at 0.02 mM and inhibition of both isozymes at 0.1 mM
sulfhydryl compounds
-
-
sulfhydryl compounds
-
purified enzyme
trifluoroperazine
-
acts as calmodulin-antagonist in animals, inhibits mycobacterial lipid synthesis, acts synergistically with isoniazid
MnCl2
-
1 mM, 7% inhibition
additional information
-
arsenite
-
additional information
-
inhibition of the enzyme by thiol-alkylating reagents
-
additional information
-
-
-
additional information
-
no inhibition by sulfhydryl inhibitors
-
additional information
-
apparently homogeneous enzyme not inhibited by sulfhydryl agents, N-ethylmaleimide and iodoacetamide, highly purified enzyme stimulated by dithiothreitol
-
additional information
-
inhibition of malonyl-enzyme intermediate formation by p-chloromercuribenzoate, reversible by 2-mercaptoethanol, prevented by preincubation with malonyl-CoA; inhibition of malonyl-enzyme intermediate formation by phenylmethanesulfonyl fluoride, malonyl-CoA protects; pH-dependent inhibition of malonyl-enzyme intermediate formation by N-ethylmaleimide
-
additional information
-
pH-dependent inhibition of malonyl-enzyme intermediate formation by N-ethylmaleimide
-
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
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.042
-
acyl-carrier protein
-
-
0.073
-
acyl-carrier protein
-
hexahistidine-tagged fusion protein, reaction with Streptomyces coelicolor acyl-carrier-protein
0.351
-
acyl-carrier protein
-
reaction with E. coli acyl-carrier-protein
0.4
-
acyl-carrier protein
-
sequential mechanism
0.6
-
acyl-carrier protein
-
ping-pong mechanism
0.776
-
acyl-carrier protein
-
reaction with E. coli acyl-carrier-protein
1.3
-
acyl-carrier protein
-
ping-pong mechanism
0.0141
-
holo-acyl-carrier protein
-
holo-acyl-carrier protein from Mycobacterium tuberculosis
0.0094
-
malonyl CoA
-
-
0.015
-
malonyl CoA
-
-
0.0013
-
malonyl-CoA
-
R606K mutant
0.0019
-
malonyl-CoA
-
wild-type
0.00326
-
malonyl-CoA
-
-
0.011
-
malonyl-CoA
-
wild-type and mutant
0.0126
-
malonyl-CoA
-
recombinant enzyme
0.015
-
malonyl-CoA
-
pH 6.8, recombinant mutant M137L
0.0162
-
malonyl-CoA
-
R606A mutant
0.0167
-
malonyl-CoA
-
wild-type enzyme, Vmax (RFU/min): 123
0.0175
-
malonyl-CoA
-
mutant N155A, Vmax (RFU/min): 63.06
0.019
-
malonyl-CoA
-
pH 6.8, 28C, recombinant enzyme
0.019
-
malonyl-CoA
-
pH 6.8, recombinant wild-type enzyme
0.0191
-
malonyl-CoA
-
mutant H90A, Vmax (RFU/min): 39.65
0.02
-
malonyl-CoA
-
acyl carrier protein mutant E20A, pH 7.5, 25C
0.0208
-
malonyl-CoA
-
wild-type enzyme
0.0228
-
malonyl-CoA
-
pH 6.8, 28C
0.023
-
malonyl-CoA
-
pH 6.8, recombinant mutant M126I
0.0239
-
malonyl-CoA
-
S97A mutant
0.032
-
malonyl-CoA
-
pH 6.8, recombinant mutant V98Q
0.033
-
malonyl-CoA
-
acyl carrier protein mutant Q67R, pH 7.5, 25C
0.034
-
malonyl-CoA
-
pH 6.8, recombinant mutant A197D
0.034
-
malonyl-CoA
-
acyl carrier protein mutant T65A, pH 7.5, 25C
0.049
-
malonyl-CoA
-
acyl carrier protein mutant Q66R, pH 7.5, 25C; wild-type acyl carrier protein, pH 7.5, 25C
0.05
-
malonyl-CoA
-
pH 6.8, recombinant mutant F200S
0.06
-
malonyl-CoA
-
hexahistidine-tagged fusion protein, reaction with Streptomyces coelicolor acyl-carrier-protein
0.06
-
malonyl-CoA
-
pH 6.8, recombinant mutants G198Y and G198A
0.083
-
malonyl-CoA
-
pH 6.8, recombinant mutant F200A
0.095
-
malonyl-CoA
-
pH 6.8, recombinant mutant F200Y
0.15
-
malonyl-CoA
-
pH 6.8, recombinant mutant R122A
0.2
-
malonyl-CoA
-
pH 6.8, recombinant mutant Q9A
0.25
-
malonyl-CoA
-
reaction with E. coli acyl-carrier-protein
0.3
-
malonyl-CoA
-
sequential mechanism
0.327
-
malonyl-CoA
-
hexahistidine-tagged fusion protein, reaction with E. coli acyl-carrier-protein
0.4
-
malonyl-CoA
-
ping-pong mechanism
0.4
-
malonyl-CoA
-
pH 6.8, recombinant mutant T57V
0.5
-
malonyl-CoA
-
sequential mechanism
0.7
-
malonyl-CoA
-
pH 6.8, recombinant mutant R122K
0.00134
-
pantetheine
-
-
0.075
-
[acyl-carrier protein]
-
pH 6.8, recombinant mutant F200Y
0.1
-
[acyl-carrier protein]
-
pH 6.8, recombinant mutants M137L and F200S
0.12
-
[acyl-carrier protein]
-
pH 6.8, recombinant wild-type enzyme and mutant V98Q
0.13
-
[acyl-carrier protein]
-
pH 6.8, recombinant mutants A197D and G198Y
0.15
-
[acyl-carrier protein]
-
pH 6.8, recombinant mutants M126I and G198A
0.24
-
[acyl-carrier protein]
-
pH 6.8, recombinant mutant F200A
0.57
-
[acyl-carrier protein]
-
pH 6.8, recombinant mutant T57V
0.92
-
[acyl-carrier protein]
-
pH 6.8, recombinant mutant Q9A
1.1
-
[acyl-carrier protein]
-
pH 6.8, recombinant mutant R122A
3.5
-
[acyl-carrier protein]
-
pH 6.8, recombinant mutant R122K
1.4
-
malonyl-CoA
-
ping-pong mechanism
additional information
-
additional information
-
the Km for N-acetylcysteamine is significantly higher than for an acyl-carrier-protein
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.01
-
malonyl CoA
-
R606A mutant
0.12
-
malonyl CoA
-
R606K mutant
1.2
-
malonyl CoA
-
wild-type
420
-
malonyl CoA
-
hexahistidine-tagged fusion protein, reaction with E. coli acyl-carrier-protein
450
-
malonyl CoA
-
hexahistidine-tagged fusion protein, reaction with Streptomyces coelicolor acyl-carrier-protein
1580
-
malonyl CoA
-
reaction with E. coli acyl-carrier-protein
0.00027
-
malonyl-CoA
-
acyl carrier protein mutant E20A, pH 7.5, 25C
0.00032
-
malonyl-CoA
-
acyl carrier protein mutant T65A, pH 7.5, 25C
0.00047
-
malonyl-CoA
-
wild-type acyl carrier protein, pH 7.5, 25C
0.0011
-
malonyl-CoA
-
acyl carrier protein mutant Q67R, pH 7.5, 25C
0.0015
-
malonyl-CoA
-
acyl carrier protein mutant Q66R, pH 7.5, 25C
0.15
-
malonyl-CoA
-
pH 6.8, recombinant mutant F200S
0.3
-
malonyl-CoA
-
pH 6.8, recombinant mutant M137L
0.35
-
malonyl-CoA
-
pH 6.8, recombinant mutant R122A
0.4
-
malonyl-CoA
-
pH 6.8, recombinant mutants G198Y
0.7
-
malonyl-CoA
-
pH 6.8, recombinant mutant Q9A
0.94
-
malonyl-CoA
-
pH 6.8, recombinant mutant F200A
3
6
malonyl-CoA
-
pH 6.8, recombinant mutant F200Y
3
-
malonyl-CoA
-
pH 6.8, recombinant mutant M126I
11
-
malonyl-CoA
-
pH 6.8, recombinant mutant R122K
12
-
malonyl-CoA
-
pH 6.8, recombinant mutants G198A
25
-
malonyl-CoA
-
pH 6.8, recombinant mutant T57V
70
-
malonyl-CoA
-
pH 6.8, recombinant mutant A197D
95
-
malonyl-CoA
-
pH 6.8, recombinant mutant V98Q
100
-
malonyl-CoA
-
pH 6.8, recombinant wild-type enzyme
0.000933
-
N-acetylcysteamine
-
S97A mutant
0.00683
-
N-acetylcysteamine
-
N-acetylcysteamine as acceptor thiol, wild-type enzyme
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0092
-
malonyl-CoA
-
acyl carrier protein mutant T65A, pH 7.5, 25C
12844
0.0095
-
malonyl-CoA
-
wild-type acyl carrier protein, pH 7.5, 25C
12844
0.013
-
malonyl-CoA
-
acyl carrier protein mutant E20A, pH 7.5, 25C
12844
0.03
-
malonyl-CoA
-
acyl carrier protein mutant Q66R, pH 7.5, 25C
12844
0.033
-
malonyl-CoA
-
acyl carrier protein mutant Q67R, pH 7.5, 25C
12844
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.009
-
CoA
-
with respect to acyl carrier protein
0.015
-
CoA
-
with respect to malonyl-CoA
0.023
-
CoA
-
with respect to malonyl-CoA
0.03
-
CoA
-
with respect to acyl carrier protein
additional information
-
additional information
-
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.01647
-
corytuberine
-
pH 6.8, 28C
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.015
-
-
R606A mutant
0.041
-
-
strain LA2-89
0.0683
-
-
purified enzyme
0.1
-
-
recombinant enzyme with recombinant ACP-A from Bacillus subtilis
0.14
-
-
recombinant enzyme with recombinant human mitochondrial [acyl-carrier protein] lacking the first 68 amino acid residues
0.154
-
-
R606K mutant
0.1541
-
-
purified enzyme
0.32
-
-
isozyme MCT1
1
-
-
isozyme MCT2
1.5
-
-
strain JM101
1.61
-
-
wild-type
780
-
-
hexahistidine-tagged fusion protein, at pH 6.5 and 30C
1851
-
-
purified enzyme
additional information
-
-
in LA2-89 and JM101 transformants
additional information
-
-
-
additional information
-
-
hexahistidine-tagged fusion protein
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7.5
-
for the malonyl-enzyme intermediate formation. The enzyme accepts malonyl groups from either malonyl-CoA or malonyl-acyl-carrier-protein to form the enzyme-intermediate, the malonyl group of the intermediate can be transferred to both CoA and acyl-carrier-protein
6.5
-
-
assay at
6.8
-
-
assay at
6.8
-
-
assay at
6.8
-
-
assay at
6.8
-
-
assay at
7.2
-
-
assay at
7.3
-
-
assay at
7.5
8.5
-
-
8
-
-
higher activity in Tris buffer than in potassium phosphate buffer
8.1
-
-
assay at
8.5
-
-
higher activity in Tris buffer than in potassium phosphate buffer
8.5
-
-
-
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
assay at
20
-
-
assay at
25
-
-
assay at
28
-
-
assay at
28
-
-
assay at
30
-
-
assay at
30
-
-
assay at
37
-
-
assay at
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
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
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
-
from the mesocarp
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)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
26000
-
-
MALDI-TOF
27000
-
-
polypeptide encoded by the fabD89 allele, Western immunoblot analysis with antiserum raised against wild-type E. coli enzyme
27000
-
-
polypeptide encoded by the fabD89 allele which contains an amber mutation at codon position 257, enzymatically inactive
30700
-
-
calculated from amino acid sequence, consistent with the observed molecular mass of approximately 33000 Da for the enzyme containing the 6-His N-terminal extension
31000
-
-
HPLC gel filtration
32300
-
-
from amino acid sequence
34110
-
-
electrospray mass spectrometry, hexahistidine-tagged fusion protein
36000
-
-
HPLC gel filtration
36660
-
-
carboxymethylated enzyme: sedimentation equilibrium centrifugation
37000
-
-
gel filtration
38800
-
-
calculated from cDNA
40500
-
-
gel filtration, elution from Sephadex G-100
42000
-
-
mutant proteins R606A and R606K, Western analysis
43000
-
-
HPLC-gel permeation chromatography, 2 isozymic forms HPLC analysis
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 35000, SDS-PAGE
monomer
-
1 * 35000, SDS-PAGE, alkylated: 1 * 35500, SDS-PAGE, native: 1 * 36500, SDS-PAGE
monomer
-
malonyl transferase domain of EC 2.3.1.85, gel filtration
monomer
-
crystal structure
additional information
-
vertebrates, yeast and Mycobacteria fatty acid synthetases contain all individual activities on one or two multifunctional polypeptide chains, plant, Escherichia coli and other prokaryotic fatty acid synthases are non-associated systems of individual enzymes
additional information
-
acyl carrier protein of fatty acid synthase interacts with malonyl-CoA-ACP-transacylase through the negatively charged helix II of acyl carrier protein. The affinity of polyketide synthase acyl carrier protein for malonyl-CoA-ACP-transacylase is lower than the affinity of the fatty acid synthase acyl carrier protein, and polyketide synthase acyl carrier protein may bind to malonyl-CoA-ACP-transacylase in a different manner
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase by protein crystallography
-
crystal structure of HpMCAT at 2.5 A resolution is shown. HpMCAT has a compact folding composed of a large subdomain with a similar core as in alpha/beta hydrolases, and a similar ferredoxin-like small subdomain as in acylphosphatases
-, Q56S05
crystal structure of MCAT is determined to 2.3 A
-
crystal structure of Mycobacterium tuberculosis MCAT (mtFabD) is determined to 3.0 A resolution by multi-wavelength anomalous dispersion. Phasing is facilitated by Ni2+ ions bound to the 20-residue N-terminal affinity tag, which packed between the two independent copies of mtFabD
-
1.2 A resolution
-
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
-
crystal structures of MCAT from Staphylococcus aureus and Streptococcus pneumoniae are determined at 1.46 and 2.1 A resolution, respectively
-
recombinant purified enzyme, 3 mg/ml protein in 10 mM Tris-HCl, pH 7.4, 1 mM 2-mercaptoethanol, hanging drop vapoir diffusion method, 3 days, room temperature, soaking of crystals in 30% PEG 4000, 100 mM sodium acetate, pH 4.8, 200 mM ammonium acetate, and 20% glycerol for cryoprotection, X-ray diffraction structure determination and analysis at 2.0 A resolution, macromolecular docking simulation with K47A/K190A/R287A/K293A mutant actinorhodin ACP structure, overview
-
the crystal structure of malonyl CoA-acyl carrier protein transacylase (XoMCAT) is determined at 2.3 A resolution in complex with N-cyclohexyl-2-aminoethansulfonic acid
-
to 1.9 A resolution, space group P212121
Q5H4I7, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
of malonyl-enzyme intermediate
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42
-
-
strain LA2-89 carrying the fabD89 allele which contains an amber mutation at codon position 257: the enzyme activity is almost completely inactivated by pre-incubation of the extract at this temperature
50
-
-
1 h stable
50
-
-
isozyme MCT1: 50% loss of activity after 5 min and 60% loss of activity after 10 min, isozyme MCT2: 30% increase of activity after 10 min
60
-
-
stable for at least 40 min
80
-
-
20% loss of activity after 20 min
80
-
-
inactivation after 20 min
100
-
-
t1/2: 15 min
additional information
-
-
the enzyme is quite stable to heat
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dithiothreitol stabilizes
-
salt concentrations above 0.1 M inactivate
-
freezing leads to 20% loss of isozyme MCT1-activity
-
glycerol, 20% v/v, stabilizes isozyme MCT1
-
dithiothreitol stabilizes
-
EDTA stabilizes
-
glycerol, 15% v/v, stabilizes
-
enzyme labile during chromatography
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, frozen in liquid nitrogen, several months
-
-10C, several weeks
-
-20C, 2-4 months
-
-80C, stable in the presence of glycerol
-
-20C, potassium-phosphate buffer, pH: 7.0, 1 mM dithiothreitol, 0.5 mM EDTA, 15% v/v glycerol
-
-20C, frozen in liquid nitrogen, several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate fractionation and DEAE-cellulose
-
chromatography on DEAE-cellulose, Sephadex G-100, Sephadex G-75, DEAE-Sephadex, and preparative polyacrylamide gel electrophoresis
-
DEAE-cellulose and DEAE-Sephadex chromatography
-
using streptomycin sulfate, column chromatography on DEAE-cellulose, ammonium sulfate fractionation, chromatography on Sephadex G-100 I column, DEAE-Sephadex column and Sephadex G-100 II column
-
recombinant enzyme from strain M15
-
of 2 isozymes MCT1 and MCT2, using salt fractionation, ion-exchange chromatography, and chromatofocusing
-
recombinant truncated enzyme forms from Sf9 insect cells
-
Ni2+-chelate chromatography
-
using Ni-NTA chromatography, ion-exchange chromatography and gel filtration
-
ammonium sulfate fractionation and column chromatography on DEAE-cellulose
-
recombinant enzyme from Escherichia coli by amylose affinity chromatography and gel filtration
-
purification of the enzyme as a hexahistidine fusion protein
-
of cytosolic recombinant transacylase, resulting from the expression of DNA corresponding to residues 488-809 of EC 2.3.1.85 in Sf9 cells, purified with column chromatography on DE-53 anion exchanger, high-performance liquid chromatography on an Ultraspherogel SEC3000 and gel filtration
-
of the mutants R606A und R606K
-
ammonium sulfate fractionation and DEAE-cellulose
-
of the hexahistidine-tagged fusion protein, using Ni(II) affinity chromatography, column chromatography on Q-Sepharose, phenyl Superose and Mono-Q
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography to homogeneity
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
cloning and nucleotide sequence analysis of the enzyme gene, overexpression of fabD89 gene in Escherichia coli
-
cloning, nucleotide sequence and expression of the fabD-gene in an appropriate Escherichia coli expression vector
-
cloning, nucleotide sequence and expression of the fabD-gene in an appropriate Escherichia coli expression vector; effects of overexpression on the fatty acid composition of the membrane phospholipids of Escherichia coli
-
from K-12 strain MC4100, overexpression in strain M15
-
expressed as a His-tagged fusion protein in Escherichia coli
-, Q56S05
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
-
a hexa-histidine-tagged enzyme overexpressed in Escherichia coli
-
expressed as a His-tagged fusion protein
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expression in Saccharomyces cerevisiae mutant lacking the corresponding mitochondrial malonyl-CoA transerase Mctp1
-
fabd2 is inserted into a bacterial expression vector pET28a resulting in a 6' histidine-tag fabd2 fusion gene construction
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
-
cloning and sequencing of the enzyme gene, expressed in Escherichia coli BL21
-
cloning and sequencing of the enzyme gene using equivalent gene of Escherichia coli HB101 as a probe. The overexpression of the enzyme gene induces monomer supply for polyhydroxybutyrate production in Escherichia coli HB101
Q9WXI0
expression in Escherichia coli of cDNAs of various lengths encoding the second domain of EC 2.3.1.85. Expression of a shortened transacylase, consisting of EC 2.3.1.85 residues 488-809 in Spodoptera frugiperda
-
expression of mutant proteins R606A and R606K in Escherichia coli
-
expressed in Escherichia coli
-
expression in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli as a hexahistidine-tagged fusion protein
-
expression in Escherichia coli strain BL21(DE3)
-
expression of five mutants in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene fabD, expression of His-tagged enzyme in Escherichia coli strain BL21
-
expression of the enzyme gene in Escherichia coli
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expressed in Escherichia coli
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expression in Escherichia coli
Q5H4I7, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K61A
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complete loss of the malonyl transferase activities
Q66A
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complete loss of the malonyl transferase activities
Q66G
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complete loss of the malonyl transferase activities
H90A
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Km only slightly increased compared to wild-type but Vmax strongly decreased compared to wild-type
N155A
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Km only slightly increased compared to wild-type but Vmax strongly decreased compared to wild-type
E20A
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mutant retains activity
K62A
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complete loss of the malonyl transferase activities
Q67A
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complete loss of the malonyl transferase activities
Q67G
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complete loss of the malonyl transferase activities
Q67R
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increase in the malonyl transferase activities
T65A
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mutant retains activity
F198S
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mutant shows a reduction in activity
H199A
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mutant shows a drastic reduction in activity
L89A
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mutant shows almost the same activity as wild-type
N158A
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mutant shows almost the same activity as wild-type
R115A
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mutant shows a reduction in activity
A197D
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
F200A
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
F200S
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
F200Y
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
G198A
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
G198Y
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
M126I
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
M137L
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
Q9A
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
R122A
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
R122K
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
T57V
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
V98Q
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site-directed mutagenesis, reduced activity compared to the wild-type enzyme
Q66R
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increase in the malonyl transferase activities
additional information
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enzyme overexpression in strain BCG confers resistance to trifluoroperazine, but not to isoniazid
H90A/N155A
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lowest enzymatic activity
additional information
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expression in Saccharomyces cerevisiae mutant lacking the corresponding mitochondrial malonyl-CoA transerase Mctp1 allows the mutant to recover its ability to respire on glycerol and synthesize lipoic acid
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
malonyl transferase domain of EC 2.3.1.85: refolding in vitro of the recombinant protein expressed in E. coli. A shortened transacylase, consisting of EC 2.3.1.85 residues 488-409 can be repeatedly denatured and renatured in vitro with reproducible high recovery and no loss in specific activity
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of the mutant proteins R606A and R606K
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
diagnostics
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coupled enzyme assay can be used in development and optimization of small-molecule inhibitors for antibacterial therapy
medicine
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enzyme is a potential target for antimycobacterial compounds
biotechnology
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the enzyme is active as part of a recombinant engineered modular enzyme complex system for modified and designed polyketid synthesis, overview