Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.3.1.293 - meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase I and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WQD9

for references in articles please use BRENDA:EC2.3.1.293
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme is part of the fatty acid synthase (FAS) II system of mycobacteria, which extends modified products of the FAS I system, eventually forming meromycolic acids that are incorporated into mycolic acids. Meromycolic acids consist of a long chain, typically 50-60 carbons, which is functionalized by different groups.Two 3-oxoacyl-(acyl carrier protein) synthases function within the FAS II system, encoded by the kasA and kasB genes. The two enzymes share some sequence identity but function independently on separate sets of substrates. KasA differs from KasB [EC 2.3.1.294, meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase II], by preferring shorter (C-22 to C-36) and more saturated (only one double bond) substrates.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WQD9
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Mycobacteriaceae
Reaction Schemes
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein]
+
=
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein]
+
+
Synonyms
beta-ketoacyl-acyl carrier protein synthase, beta-ketoacyl acp synthase, rv2245, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-ketoacyl ACP synthase I
-
beta-ketoacyl ACP synthase
-
-
beta-ketoacyl acyl carrier protein synthase
-
-
beta-ketoacyl-ACP synthase
-
-
beta-ketoacyl-AcpM synthase
-
-
beta-ketoacyl-AcpM synthase A
-
-
beta-ketoacyl-acyl carrier protein synthase
-
-
beta-ketoacyl-acyl carrier protein synthase KasA
-
-
-
-
beta-ketoacyl-acyl-carrier protein synthase
-
-
beta-ketoacylacyl synthase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ultra-long-chain mono-unsaturated fattyl acyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating)
The enzyme is part of the fatty acid synthase (FAS) II system of mycobacteria, which extends modified products of the FAS I system, eventually forming meromycolic acids that are incorporated into mycolic acids. Meromycolic acids consist of a long chain, typically 50-60 carbons, which is functionalized by different groups.Two 3-oxoacyl-(acyl carrier protein) synthases function within the FAS II system, encoded by the kasA and kasB genes. The two enzymes share some sequence identity but function independently on separate sets of substrates. KasA differs from KasB [EC 2.3.1.294, meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase II], by preferring shorter (C-22 to C-36) and more saturated (only one double bond) substrates.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
show the reaction diagram
-
-
-
?
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
show the reaction diagram
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein AcpM]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein AcpM]
show the reaction diagram
-
-
-
-
?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + palmitoyl-[acyl-carrier protein AcpM]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein AcpM]
show the reaction diagram
-
-
-
-
?
C12:0-[acyl-carrier protein from Escherichia coli] + malonyl-[acyl-carrier protein from Escherichia coli]
?
show the reaction diagram
-
-
-
-
?
C20:0-[acyl-carrier protein from Escherichia coli] + malonyl-[acyl-carrier protein from Escherichia coli]
?
show the reaction diagram
-
best substrate
-
-
?
C4:0-[acyl-carrier protein from Escherichia coli] + malonyl-[acyl-carrier protein from Escherichia coli]
?
show the reaction diagram
-
very low activity
-
-
?
myristoyl-[acyl-carrier protein] + biotinylated malonyl-[acyl-carrier protein]
?
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + malonyl-[acyl-carrier protein AcpM]
?
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + malonyl-[acyl-carrier protein from Escherichia coli]
?
show the reaction diagram
-
weak activity
-
-
?
palmitoyl-[acyl-carrier protein from Escherichia coli] + malonyl-[acyl-carrier protein from Escherichia coli]
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme catalyzes the condensation steps from C18 to C34 long-chain fatty acids
-
-
?
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
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
show the reaction diagram
-
-
-
?
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
show the reaction diagram
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein AcpM]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein AcpM]
show the reaction diagram
-
-
-
-
?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + palmitoyl-[acyl-carrier protein AcpM]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein AcpM]
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme catalyzes the condensation steps from C18 to C34 long-chain fatty acids
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
-
0.05 mM NADPH is used in assay conditions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(5R)-3-acetyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
-
(5R)-3-butanoyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
-
(5R)-3-ethyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
-
(5R)-3-hexadecanoyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
-
(5R)-3-[2-(4-chlorophenyl)ethyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
-
(5R)-3-[4-(4-chlorophenyl)butyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
-
(5R)-3-[4-(4-fluorophenyl)butyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
-
(5R)-3-[4-([1,1'-biphenyl]-4-yl)butyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
-
(5R)-3-[6-([1,1'-biphenyl]-4-yl)hexanoyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
-
(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-3-(propan-2-yl)thiophen-2(5H)-one
-
-
(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-3-(trifluoroacetyl)thiophen-2(5H)-one
-
-
(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-3-[2-(4-methylphenyl)ethyl]thiophen-2(5H)-one
-
-
(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
-
2-[(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-2-oxo-2,5-dihydrothiophene-3-carbonyl]benzoic acid
-
-
4-[(4-fluorobenzene-1-sulfonyl)amino]-N-[[1-(4-[(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-2-oxo-2,5-dihydrothiophen-3-yl]butyl)-1H-1,2,3-triazol-4-yl]methyl]benzamide
-
-
cerulenin
methyl (5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-2-oxo-2,5-dihydrothiophene-3-carboxylate
-
-
platensimycin
-
natural product inhibitor
thiolactomycin
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DMSO
-
about 130% activity at 2.5% (v/v) DMSO
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005
biotinylated malonyl-[acyl-carrier protein]
-
at pH 6.8 and 37°C
-
0.0025
C20:0-[acyl-carrier protein from Escherichia coli]
-
at pH 6.8 and 37°C
-
0.0135
malonyl-[acyl-carrier protein from Escherichia coli]
-
at pH 6.8 and 37°C
-
0.003
myristoyl-[acyl-carrier protein]
-
at pH 6.8 and 37°C
0.0026
palmitoyl-[acyl-carrier protein AcpM]
-
at pH 8.5 and 25°C
-
0.0032
palmitoyl-[acyl-carrier protein from Escherichia coli]
-
at pH 6.8 and 37°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.075
C20:0-[acyl-carrier protein from Escherichia coli]
-
at pH 6.8 and 37°C
-
0.08
malonyl-[acyl-carrier protein from Escherichia coli]
-
at pH 6.8 and 37°C
-
0.533
palmitoyl-[acyl-carrier protein AcpM]
-
at pH 8.5 and 25°C
-
0.088
palmitoyl-[acyl-carrier protein from Escherichia coli]
-
at pH 6.8 and 37°C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30
C20:0-[acyl-carrier protein from Escherichia coli]
-
at pH 6.8 and 37°C
-
5.83
malonyl-[acyl-carrier protein from Escherichia coli]
-
at pH 6.8 and 37°C
-
205
palmitoyl-[acyl-carrier protein AcpM]
-
at pH 8.5 and 25°C
-
28.33
palmitoyl-[acyl-carrier protein from Escherichia coli]
-
at pH 6.8 and 37°C
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0082
(5R)-3-acetyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.0652
(5R)-3-butanoyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.357
(5R)-3-ethyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.105
(5R)-3-hexadecanoyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.4
(5R)-3-[2-(4-chlorophenyl)ethyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.0774
(5R)-3-[4-(4-chlorophenyl)butyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.069
(5R)-3-[4-(4-fluorophenyl)butyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.0138
(5R)-3-[4-([1,1'-biphenyl]-4-yl)butyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.008
(5R)-3-[6-([1,1'-biphenyl]-4-yl)hexanoyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.305
(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-3-(propan-2-yl)thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.0121
(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-3-(trifluoroacetyl)thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.0928
(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-3-[2-(4-methylphenyl)ethyl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.047
(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.102
2-[(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-2-oxo-2,5-dihydrothiophene-3-carbonyl]benzoic acid
-
pH and temperature not specified in the publication
0.032
4-[(4-fluorobenzene-1-sulfonyl)amino]-N-[[1-(4-[(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-2-oxo-2,5-dihydrothiophen-3-yl]butyl)-1H-1,2,3-triazol-4-yl]methyl]benzamide
-
pH and temperature not specified in the publication
0.0219
methyl (5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-2-oxo-2,5-dihydrothiophene-3-carboxylate
-
pH and temperature not specified in the publication
0.1754
thiolactomycin
-
pH and temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0047 - 0.252
thiolactomycin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0057
-
with palmitoyl-CoA as substrate, at pH 6.8 and 37°C
0.0878
-
palmitoyl-[acyl-carrier protein] as substrate, at pH 6.8 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 42
-
the enzyme displays about 2-3fold higher specific activities at 37°C compared with 30 or 42°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cf. EC 2.3.1.41
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-enzyme and mutant C171Q bound to thiolactomycin, vapor diffusion method, using 10% (v/v) isopropanol, 0.2 M NaCl, 0.1 M HEPES pH 7.5 and 10 mM tris(2-carboxyethyl)phosphine hydrochloride (for apoenzyme), or 20% (w/v) polyethylene glycol 3350 and 0.2 M potassium formate (for mutant C171Q)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C171Q
acyl-enzyme mimic
D66N
dimer non-active site mutant protein displays much more structural flexibility than wild type at the ligand binding site
F413L
dimer non-active site mutant protein displays much more structural flexibility than wild type at the ligand binding site
G269S
dimer non-active site mutant protein displays much more structural flexibility than wild type at the ligand binding site
G312S
dimer non-active site mutant protein displays much more structural flexibility than wild type at the ligand binding site
C171Q
D66N
-
the mutation occurs in isonicotinic acid hydrazide-resistant clinical isolates of Mycobacterium tuberculosis
F413L
-
the mutation occurs in isonicotinic acid hydrazide-resistant clinical isolates of Mycobacterium tuberculosis
G269S
G312S
-
the mutation occurs in isonicotinic acid hydrazide-resistant clinical isolates of Mycobacterium tuberculosis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography, MonoQ column chromatography and Superdex S200 gel filtration
metal ion affinity chromatography and G-25 resin gel filtration
-
Q-Sepharose column chromatography and HiTrap column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Mycobacterium smegmatis strain mc2155
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Mycobacterium bovis BCG vaccine strain 1173P2
-
expressed in Mycobacterium smegmatis
-
expressed in Mycobacterium smegmatis strain mc2155
-
gene kasA, recombinant expression in Mycobacterium smegmatis strain mc2155
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kapilashrami, K.; Bommineni, G.R.; Machutta, C.A.; Kim, P.; Lai, C.T.; Simmerling, C.; Picart, F.; Tonge, P.J.
Thiolactomycin-based beta-ketoacyl-AcpM synthase A (KasA) inhibitors: fragment-based inhibitor discovery using transient one-dimensional nuclear overhauser effect NMR spectroscopy
J. Biol. Chem.
288
6045-6052
2013
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Jayaraman, M.; Rajendra, S.; Ramadas, K.
Structural insight into conformational dynamics of non-active site mutations in KasA A Mycobacterium tuberculosis target protein
Gene
720
144082
2019
Mycobacterium tuberculosis (P9WQD9), Mycobacterium tuberculosis H37Rv (P9WQD9)
Manually annotated by BRENDA team
Kremer, L.; Douglas, J.D.; Baulard, A.R.; Morehouse, C.; Guy, M.R.; Alland, D.; Dover, L.G.; Lakey, J.H.; Jacobs, W.R.; Brennan, P.J.; Minnikin, D.E.; Besra, G.S.
Thiolactomycin and related analogues as novel anti-mycobacterial agents targeting KasA and KasB condensing enzymes in Mycobacterium tuberculosis
J. Biol. Chem.
275
16857-16864
2000
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team
Schaeffer, M.L.; Agnihotri, G.; Volker, C.; Kallender, H.; Brennan, P.J.; Lonsdale, J.T.
Purification and biochemical characterization of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthases KasA and KasB
J. Biol. Chem.
276
47029-47037
2001
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team
Machutta, C.A.; Bommineni, G.R.; Luckner, S.R.; Kapilashrami, K.; Ruzsicska, B.; Simmerling, C.; Kisker, C.; Tonge, P.J.
Slow onset inhibition of bacterial beta-ketoacyl-acyl carrier protein synthases by thiolactomycin
J. Biol. Chem.
285
6161-6169
2010
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Mdluli, K.; Slayden, R.A.; Zhu, Y.; Ramaswamy, S.; Pan, X.; Mead, D.; Crane, D.D.; Musser, J.M.; Barry, C.E.
Inhibition of a Mycobacterium tuberculosis beta-ketoacyl ACP synthase by isoniazid
Science
280
1607-1610
1998
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Luckner, S.; Machutta, C.; Tonge, P.; Kisker, C.
Crystal structures of Mycobacterium tuberculosis KasA show mode of action within cell wall biosynthesis and its inhibition by thiolactomycin
Structure
17
1004-1013
2009
Mycobacterium tuberculosis (P9WQD9), Mycobacterium tuberculosis H37Rv (P9WQD9)
Manually annotated by BRENDA team
Slayden, R.; Barry III, C.
The role of KasA and KasB in the biosynthesis of meromycolic acids and isoniazid resistance in Mycobacterium tuberculosis
Tuberculosis
82
149-160
2002
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team
Schaeffer, M.L.; Carson, J.D.; Kallender, H.; Lonsdale, J.T.
Development of a scintillation proximity assay for the Mycobacterium tuberculosis KasA and KasB enzymes involved in mycolic acid biosynthesis
Tuberculosis
84
353-360
2004
Mycobacterium tuberculosis
Manually annotated by BRENDA team