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Information on EC 2.3.1.39 - [acyl-carrier-protein] S-malonyltransferase and Organism(s) Escherichia coli and UniProt Accession P0AAI9

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EC Tree
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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Escherichia coli
UNIPROT: P0AAI9
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
fatty acid synthase, malonyl-coa:acp transacylase, malonyl transferase, mtfabd, hpmcat, malonyl-coa:acyl carrier protein transacylase, fabd2, malonyl coa-acyl carrier protein transacylase, malonyl-coa-acyl carrier protein transacylase, mcamt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malonyl-CoA/ACP transacylase
-
malonyl-coenzyme A-holo-acyl-carrier protein transacylase
-
malonyl coenzyme A-acyl carrier protein transacylase
-
-
-
-
malonyl transacylase
-
-
-
-
malonyl transferase
-
-
-
-
malonyl-CoA-acyl carrier protein transacylase
-
-
-
-
malonyl-CoA/holo-ACP transacylase
-
-
malonyl-CoA:acyl carrier protein transacylase
-
-
malonyl-CoA–acyl carrier protein transacylase
-
-
malonyl-coenzyme A (CoA)/holo-ACP transacylase
-
-
malonyltransferase, [acyl-carrier-protein]
-
-
-
-
[acyl carrier protein]malonyltransferase
-
-
-
-
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
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein]
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
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
-
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 + an [acyl-carrier protein]
CoA + a malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
2-butenoyl-CoA + an [acyl-carrier protein]
CoA + 2-butenoyl-[acyl carrier protein]
show the reaction diagram
-
the reaction is catalyzed by mutant enzyme R117A
-
-
?
2-hydroxybutyryl-CoA + an [acyl-carrier protein]
CoA + 2-hydroxybutyryl-[acyl carrier protein]
show the reaction diagram
-
the reaction is catalyzed by mutant enzyme R117A
-
-
?
acetoacetyl-CoA + an [acyl-carrier protein]
CoA + acetoacetyl-[acyl carrier protein]
show the reaction diagram
-
the reaction is catalyzed by the wild type enzyme (very weak activity) and mutant enzyme R117A
-
-
?
acetoacetyl-CoA + an [acyl-carrier protein]
CoA + an acetoacetyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
acetyl-CoA + an [acyl-carrier protein]
CoA + acetyl-[acyl carrier protein]
show the reaction diagram
-
the reaction is catalyzed by mutant enzyme R117A
-
-
?
acetyl-CoA + an [acyl-carrier protein]
CoA + an acetyl-[acyl-carrier protein]
show the reaction diagram
-
activity with mutant enzyme R117A, no activity with wild-type enzyme
-
-
?
butyryl-CoA + an [acyl-carrier protein]
CoA + butyryl-[acyl carrier protein]
show the reaction diagram
-
the reaction is catalyzed by mutant enzyme R117A
-
-
?
isobutyryl-CoA + an [acyl-carrier protein]
CoA + isobutyryl-[acyl carrier protein]
show the reaction diagram
-
the reaction is catalyzed by mutant enzyme R117A
-
-
?
isovaleryl-CoA + an [acyl-carrier protein]
CoA + isovaleryl-[acyl carrier protein]
show the reaction diagram
-
the reaction is catalyzed by mutant enzyme R117A
-
-
?
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 + an [acyl-carrier protein]
CoA + a malonyl-[acyl-carrier protein]
show the reaction diagram
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 + pantetheine
malonyl-pantetheine + CoA
show the reaction diagram
-
-
-
-
?
malonyl-pantetheine + acyl-carrier protein
pantetheine + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
methylmalonyl-CoA + an [acyl-carrier protein]
CoA + methylmalonyl-[acyl carrier protein]
show the reaction diagram
-
the reaction is catalyzed by the wild type enzyme (low activity) and mutant enzyme R117A
-
-
?
methylmalonyl-CoA + an [acyl-carrier protein]
CoA + methylmalonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
propionyl-CoA + an [acyl-carrier protein]
CoA + propionyl-[acyl carrier protein]
show the reaction diagram
-
the reaction is catalyzed by mutant enzyme R117A
-
-
?
succinyl-CoA + an [acyl-carrier protein]
CoA + succinyl-[acyl carrier protein]
show the reaction diagram
-
the reaction is catalyzed by mutant enzyme R117A
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
malonyl-CoA + an [acyl-carrier protein]
CoA + a malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
malonyl-CoA + acyl-carrier protein
CoA + malonyl-acyl-carrier protein
show the reaction diagram
malonyl-CoA + an [acyl-carrier protein]
CoA + a malonyl-[acyl-carrier protein]
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
-
competitive to malonyl-CoA
iodoacetamide
iodoacetate
-
-
N-ethylmaleimide
p-chloromercuribenzoate
p-toluenesulfonyl fluoride
-
strong inhibitor
phenylmethanesulfonyl fluoride
sulfhydryl compounds
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
acetoacetyl-CoA
-
mutant enzyme R117A, pH and temperature not specified in the publication
0.2
acetyl-CoA
-
mutant enzyme R117A, pH and temperature not specified in the publication
0.351
acyl-carrier protein
-
reaction with E. coli acyl-carrier-protein
0.011 - 0.04
an [acyl-carrier protein]
0.011 - 0.25
malonyl-CoA
0.33 - 0.58
methylmalonyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.041
acetoacetyl-CoA
-
mutant enzyme R117A, pH and temperature not specified in the publication
0.029
acetyl-CoA
-
mutant enzyme R117A, pH and temperature not specified in the publication
1580
malonyl CoA
-
reaction with E. coli acyl-carrier-protein
0.00047 - 2100
malonyl-CoA
5 - 1000
methylmalonyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0095 - 0.03
malonyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.001
-
mutant enzyme R117A with isovaleryl-CoA as substrate, pH and temperature not specified in the publication
0.0016
0.0037
-
mutant enzyme R117A with isobutyryl-CoA as substrate, pH and temperature not specified in the publication
0.005
-
mutant enzyme R117A with 2-hydroxybutyryl-CoA as substrate, pH and temperature not specified in the publication
0.0054
-
mutant enzyme R117A with 2-butenoyl-CoA as substrate, pH and temperature not specified in the publication
0.011
-
mutant enzyme R117A with butyryl-CoA as substrate, pH and temperature not specified in the publication
0.016
-
mutant enzyme R117A with succinyl-CoA as substrate, pH and temperature not specified in the publication
0.041
-
strain LA2-89
0.052
-
mutant enzyme R117A with propionyl-CoA as substrate, pH and temperature not specified in the publication
1.5
-
strain JM101
1851
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
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
8.1
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
-
about half-maximal activity at pH 5.0, about 80% of maximal activity at pH 10.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
32300
-
from amino acid sequence
35000
35500
-
1 * 35000, SDS-PAGE, alkylated: 1 * 35500, SDS-PAGE, native: 1 * 36500, SDS-PAGE
36500
-
1 * 35000, SDS-PAGE, alkylated: 1 * 35500, SDS-PAGE, native: 1 * 36500, SDS-PAGE
36660
-
carboxymethylated enzyme: sedimentation equilibrium centrifugation
37000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 30000, SDS-PAGE
?
-
x * 35000, SDS-PAGE
monomer
-
1 * 35000, SDS-PAGE, alkylated: 1 * 35500, SDS-PAGE, native: 1 * 36500, SDS-PAGE
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase by protein crystallography
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H91A/S92A
inactive
K61A
-
complete loss of the malonyl transferase activities
Q66A
-
complete loss of the malonyl transferase activities
Q66G
-
complete loss of the malonyl transferase activities
Q66R
-
increase in the malonyl transferase activities
R117A
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
of malonyl-enzyme intermediate
486883
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
t1/2: 15 min
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
60
-
stable for at least 40 min
80
-
20% loss of activity after 20 min
additional information
-
the enzyme is quite stable to heat
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol stabilizes
-
salt concentrations above 0.1 M inactivate
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, several weeks
-
-20°C, 2-4 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
effects of overexpression on the fatty acid composition of the membrane phospholipids of Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vagelos, R.P.
Acyl group transfer (acyl carrier protein)
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
8
155-199
1973
Escherichia coli
-
Manually annotated by BRENDA team
Prescott, D.J.; Vagelos, P.R.
Acyl carrier protein
Adv. Enzymol. Relat. Areas Mol. Biol.
36
269-311
1972
Escherichia coli
Manually annotated by BRENDA team
Williamson, I.P.; Wakil, S.J.
Studies on the mechanism of fatty acid synthesis. XVII. Preparation and general properties of acetyl coenzyme A and malonyl coenzyme A-acyl carrier protein transacylases
J. Biol. Chem.
241
2326-2332
1966
Escherichia coli
Manually annotated by BRENDA team
Alberts, A.W.; Majerus, P.W.; Vagelos, P.R.
Malonyl-CoA acyl carrier protein transacylase
Methods Enzymol.
14
53-56
1969
Escherichia coli
-
Manually annotated by BRENDA team
Joshi, V.C.
Mechanism of malonyl-coenzyme A-acyl carrier protein transacylase
Biochem. J.
128
43P-44P
1972
Escherichia coli
Manually annotated by BRENDA team
Ruch, F.E.; Vagelos, P.R.
The isolation and general properties of Escherichia coli malonyl coenzyme A-acyl carrier protein transacylase
J. Biol. Chem.
248
8086-8094
1973
Escherichia coli
Manually annotated by BRENDA team
Ruch, F.E.; Vagelos, P.R.
Characterization of a malonyl-enzyme intermediate and identification of the malonyl binding site in malonyl coenzyme A-acyl carrier protein transacylase of Escherichia coli
J. Biol. Chem.
248
8095-8106
1973
Escherichia coli
Manually annotated by BRENDA team
Verwoert, I.I.G.S.; Verbree, E.C.; VanDerLinden, K.H.; Nijkamp, H.J.J.; Stuitje, A.R.
Cloning, nucleotide sequence, and expression of the Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl carrier protein transacylase
J. Bacteriol.
174
2851-2857
1992
Escherichia coli
Manually annotated by BRENDA team
Magnuson, K.; Oh, W.; Larson, T.J.; Cronan, J.E.
Cloning and nucleotide sequence of the fabD gene encoding malonyl coenzyme A-acyl carrier protein transacylase of Escherichia coli
FEBS Lett.
299
262-266
1992
Escherichia coli
Manually annotated by BRENDA team
Guerra, D.J.; Ohlrogge, J.B.
Partial purification and characterization of two forms of malonyl-coenzyme A:acyl carrier protein transacylase from soybean leaf tissue
Arch. Biochem. Biophys.
246
274-285
1986
Escherichia coli, Glycine max
Manually annotated by BRENDA team
Szafranska, A.E.; Hitchman, T.S.; Cox, R.J.; Crosby, J.; Simpson, T.J.
Kinetic and mechanistic analysis of the malonyl CoA:ACP transacylase from Streptomyces coelicolor indicates a single catalytically competent serine nucleophile at the active site
Biochemistry
41
1421-1427
2002
Escherichia coli, Streptomyces coelicolor
Manually annotated by BRENDA team
Dreier, J.; Li, Q.; Khosla, C.
Malonyl-CoA:ACP transacylase from Streptomyces coelicolor has two alternative catalytically active nucleophiles
Biochemistry
40
12407-12411
2001
Escherichia coli, Streptomyces coelicolor
Manually annotated by BRENDA team
Taguchi, K.; Aoyagi, Y.; Matsusaki, H.; Fukui, T.; Doi, Y.
Over-expression of 3-ketoacyl-ACP synthase III or malonyl-CoA-ACP transacylase gene induces monomer supply for polyhydroxybutyrate production in Escherichia coli HB101
Biotechnol. Lett.
21
579-584
1999
Escherichia coli, Pseudomonas sp. (Q9WXI0)
-
Manually annotated by BRENDA team
Kutchma, A.J.; Hoang, T.T.; Schweizer, H.P.
Characterization of a Pseudomonas aeruginosa fatty acid biosynthetic gene cluster: purification of acyl carrier protein (ACP) and malonyl-coenzyme A:ACP transacylase (FabD)
J. Bacteriol.
181
5498-5504
1999
Escherichia coli, Pseudomonas aeruginosa
Manually annotated by BRENDA team
Serre, L.; Verbree, E.C.; Dauter, Z.; Stuitje, A.R.; Derewenda, Z.S.
The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-.ANG. resolution
J. Biol. Chem.
270
12961-12964
1995
Escherichia coli
Manually annotated by BRENDA team
Verwoert, II; Verhagen, E.F.; van der Linden, K.H.; Verbree, E.C.; Nijkamp, H.J.; Stuitje, A.R.
Molecular characterization of an Escherichia coli mutant with a temperature-sensitive malonyl coenzyme A-acyl carrier protein transacylase
FEBS Lett.
348
311-316
1994
Escherichia coli
Manually annotated by BRENDA team
Oefner, C.; Schulz, H.; DArcy, A.; Dale, G.E.
Mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase (FabD) by protein crystallography
Acta Crystallogr. Sect. D
D62
613-618
2006
Escherichia coli
Manually annotated by BRENDA team
Misra, A.; Surolia, N.; Surolia, A
Catalysis and mechanism of malonyl transferase activity in type II fatty acid biosynthesis acyl carrier proteins
Mol. Biosyst.
5
651-659
2009
Escherichia coli, Plasmodium falciparum
Manually annotated by BRENDA team
Zhang, X.; Agrawal, A.; San, K.Y.
Improving fatty acid production in Escherichia coli through the overexpression of malonyl coA-acyl carrier protein transacylase
Biotechnol. Prog.
28
60-65
2012
Clostridium acetobutylicum, Escherichia coli, Streptomyces avermitilis, Streptomyces coelicolor, Streptomyces avermitilis MA-4680, Escherichia coli ML103
Manually annotated by BRENDA team
Marcella, A.M.; Barb, A.W.
The R117A variant of the Escherichia coli transacylase FabD synthesizes novel acyl-(acyl carrier proteins)
Appl. Microbiol. Biotechnol.
101
8431-8441
2017
Escherichia coli
Manually annotated by BRENDA team
Marcella, A.M.; Barb, A.W.
Acyl-coenzyme A (holo-acyl carrier protein) transacylase enzymes as templates for engineering
Appl. Microbiol. Biotechnol.
102
6333-6341
2018
Escherichia coli (P0AAI9)
Manually annotated by BRENDA team