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 hide
2.3.1.39
-
RECOMMENDED NAME
GeneOntology No.
[acyl-carrier-protein] S-malonyltransferase
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
BRENDA Link
KEGG Link
MetaCyc Link
Fatty acid biosynthesis
-
-
fatty acid biosynthesis (plant mitochondria)
-
-
fatty acid biosynthesis initiation I
-
-
lipid metabolism
-
-
Metabolic pathways
-
-
octanoyl-[acyl-carrier protein] 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.
CAS REGISTRY NUMBER
COMMENTARY hide
37257-17-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
rape
-
-
Manually annotated by BRENDA team
safflower
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Lythraceae
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene fabD
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Z
-
-
Manually annotated by BRENDA team
Z
-
-
Manually annotated by BRENDA team
soy bean, strain AMSOY71
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain BCG, ATCC 35734
-
-
Manually annotated by BRENDA team
avocado
-
-
Manually annotated by BRENDA team
pea
-
-
Manually annotated by BRENDA team
61-3
SwissProt
Manually annotated by BRENDA team
61-3
SwissProt
Manually annotated by BRENDA team
malonyl transferase domain of EC 2.3.1.85
-
-
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
produces tetracenomicin C
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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
malonyl-CoA + acyl-carrier protein
CoA + 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-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
malonyl-pantetheine + acyl-carrier protein
pantetheine + malonyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
malonyl-CoA + [acyl-carrier protein]
CoA + malonyl-[acyl-carrier protein]
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
corytuberine
-
-
diethyldicarbonate
-
inhibits MCT1 but not MCT2 at 1 mM
EDTA
-
63% inhibition at 1 mM, complete inhibition at 10 mM
iodoacetamide
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
MnCl2
-
1 mM, 7% inhibition
N-ethylmaleimide
NiSO4
-
1 mM, 12% inhibition
p-chloromercuribenzoate
p-toluenesulfonyl fluoride
-
strong inhibitor
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
trifluoroperazine
-
acts as calmodulin-antagonist in animals, inhibits mycobacterial lipid synthesis, acts synergistically with isoniazid
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.042 - 1.3
acyl-carrier protein
0.0141
holo-acyl-carrier protein
-
holo-acyl-carrier protein from Mycobacterium tuberculosis
0.0094 - 0.015
malonyl CoA
0.0013 - 1.4
malonyl-CoA
0.00134
pantetheine
-
-
0.075 - 3.5
[acyl-carrier protein]
additional information
additional information
-
the Km for N-acetylcysteamine is significantly higher than for an acyl-carrier-protein
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 1580
malonyl CoA
0.00027 - 100
malonyl-CoA
0.000933 - 0.00683
N-acetylcysteamine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0092 - 0.033
malonyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009 - 0.03
CoA
additional information
additional information
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01647
corytuberine
Eimeria tenella
-
pH 6.8, 28C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
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
7.2
-
assay at
7.5 - 8.5
-
-
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
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
mesocarp
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
from the mesocarp
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / 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)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
COMMENTARY hide
LITERATURE
?
-
x * 35000, SDS-PAGE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
of malonyl-enzyme intermediate
486883
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
60
-
stable for at least 40 min
100
-
t1/2: 15 min
additional information
-
the enzyme is quite stable to heat
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol stabilizes
EDTA stabilizes
-
enzyme labile during chromatography
-
freezing leads to 20% loss of isozyme MCT1-activity
-
glycerol, 15% v/v, stabilizes
-
glycerol, 20% v/v, stabilizes isozyme MCT1
-
salt concentrations above 0.1 M inactivate
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, several weeks
-
-20C, 2-4 months
-
-20C, frozen in liquid nitrogen, several months
-20C, potassium-phosphate buffer, pH: 7.0, 1 mM dithiothreitol, 0.5 mM EDTA, 15% v/v glycerol
-
-80C, stable in the presence of glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation and column chromatography on DEAE-cellulose
-
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
-
Ni2+-chelate chromatography
-
of 2 isozymes MCT1 and MCT2, using salt fractionation, ion-exchange chromatography, and chromatofocusing
-
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 hexahistidine-tagged fusion protein, using Ni(II) affinity chromatography, column chromatography on Q-Sepharose, phenyl Superose and Mono-Q
-
of the mutants R606A und R606K
-
purification of the enzyme as a hexahistidine fusion protein
-
recombinant enzyme from Escherichia coli by amylose affinity chromatography and gel filtration
-
recombinant enzyme from strain M15
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography to homogeneity
-
recombinant truncated enzyme forms from Sf9 insect cells
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
using Ni-NTA chromatography, ion-exchange chromatography and gel filtration
-
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
a hexa-histidine-tagged enzyme overexpressed in Escherichia coli
-
cloning and nucleotide sequence analysis of the enzyme gene, overexpression of fabD89 gene in Escherichia coli
-
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
cloning and sequencing of the enzyme gene, expressed in Escherichia coli BL21
-
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
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
-
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
-
expressed as a His-tagged fusion protein
-
expressed as a His-tagged fusion protein in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli as a hexahistidine-tagged fusion protein
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expression in Escherichia coli
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 in Escherichia coli strain BL21(DE3)
-
expression in Saccharomyces cerevisiae mutant lacking the corresponding mitochondrial malonyl-CoA transerase Mctp1
-
expression of five mutants in Escherichia coli
-
expression of mutant proteins R606A and R606K in Escherichia coli
-
expression of the enzyme gene in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
fabd2 is inserted into a bacterial expression vector pET28a resulting in a 6' histidine-tag fabd2 fusion gene construction
-
from K-12 strain MC4100, overexpression in strain M15
-
gene fabD, expression of His-tagged enzyme in Escherichia coli strain BL21
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
H90A
-
Km only slightly increased compared to wild-type but Vmax strongly decreased compared to wild-type
H90A/N155A
-
lowest enzymatic activity
N155A
-
Km only slightly increased compared to wild-type but Vmax strongly decreased compared to wild-type
H90A
-
Km only slightly increased compared to wild-type but Vmax strongly decreased compared to wild-type
-
H90A/N155A
-
lowest enzymatic activity
-
N155A
-
Km only slightly increased compared to wild-type but Vmax strongly decreased compared to wild-type
-
E20A
-
mutant retains activity
K62A
-
complete loss of the malonyl transferase activities
Q67A
-
complete loss of the malonyl transferase activities
Q67G
-
complete loss of the malonyl transferase activities
Q67R
-
increase in the malonyl transferase activities
T65A
-
mutant retains activity
F198S
-
mutant shows a reduction in activity
H199A
-
mutant shows a drastic reduction in activity
L89A
-
mutant shows almost the same activity as wild-type
N158A
-
mutant shows almost the same activity as wild-type
R115A
-
mutant shows a reduction in activity
A197D
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
F200A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
F200S
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
F200Y
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
G198A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
G198Y
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
M126I
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
M137L
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
Q9A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
R122A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
R122K
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
T57V
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
V98Q
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
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
-
of the mutant proteins R606A and R606K
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
the enzyme is active as part of a recombinant engineered modular enzyme complex system for modified and designed polyketid synthesis, overview
diagnostics
-
coupled enzyme assay can be used in development and optimization of small-molecule inhibitors for antibacterial therapy
medicine
-
enzyme is a potential target for antimycobacterial compounds
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