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Information on EC 2.3.1.41 - beta-ketoacyl-[acyl-carrier-protein] synthase I and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WQD9
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2.3.1.41 beta-ketoacyl-[acyl-carrier-protein] synthase IIUBMB Comments
This enzyme is responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. The enzyme can use fatty acyl thioesters of ACP (C2 to C16) as substrates, as well as fatty acyl thioesters of Co-A (C4 to C16) . The substrate specificity is very similar to that of EC 2.3.1.179, beta-ketoacyl-ACP synthase II, with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C16Delta9) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature [4,5].
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Word Map
- 2.3.1.41
- polyketide
- cerulenin
- malonyl-coa
-
thioesterase
- elongase
-
enoyl
- thiolactomycin
-
transacylase
-
mycolic
- malonyl-acp
- acyl-acps
-
very-long-chain
-
dehydrase
- 4'-phosphopantetheine
- cuphea
-
vlcfas
-
cis-vaccenic
-
malonyl-coa:acp
-
actinorhodin
- platensimycin
- acetyl-acp
- drug development
-
6-methylsalicylic
- 3-oxoacyl-acps
-
claisen
- pharmacology
- nutrition
- medicine
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
condensing enzyme, beta-ketoacyl synthase, kas i, beta-ketoacyl-acp synthase, beta-ketoacyl synthetase, 3-ketoacyl-acyl carrier protein synthase, 3-ketoacyl-acp synthase, beta-ketoacyl-acp synthase i, beta-ketoacyl-acyl carrier protein synthase i, fatty acid condensing enzyme, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-ketoacyl-acyl carrier protein synthase
-
-
-
-
3-oxoacyl-[acyl-carrier-protein] synthase
-
-
-
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acyl-malonyl(acyl-carrier-protein)-condensing enzyme
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-
-
-
beta-ketoacyl acyl carrier protein synthase
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-
-
-
beta-ketoacyl synthetase
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-
-
-
beta-ketoacyl-ACP synthetase
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-
-
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beta-ketoacyl-acyl carrier protein synthetase
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-
-
-
beta-ketoacyl-[acyl carrier protein] synthase
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-
-
-
beta-ketoacylsynthase
-
-
-
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condensing enzyme
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-
-
-
fatty acid condensing enzyme
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-
-
-
synthase, 3-oxoacyl-[acyl-carrier-protein]
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating)
This enzyme is responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. The enzyme can use fatty acyl thioesters of ACP (C2 to C16) as substrates, as well as fatty acyl thioesters of Co-A (C4 to C16) [4]. The substrate specificity is very similar to that of EC 2.3.1.179, beta-ketoacyl-ACP synthase II, with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C16Delta9) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature [4,5].
CAS REGISTRY NUMBER
COMMENTARY
9077-10-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
-
-
-
?
decanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
dodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
?
dodecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxotetradecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
?
eicosanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxodocosanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
?
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
?
malonyl-[acyl-carrier protein] + lauroyl-CoA
? + CO2 + [acyl-carrier protein]
-
-
-
-
?
malonyl-[acyl-carrier protein] + myristoyl-CoA
? + CO2 + [acyl-carrier protein]
-
-
-
-
?
malonyl-[acyl-carrier protein] + palmitoyl-CoA
? + CO2 + [acyl-carrier protein]
-
-
-
-
?
myristoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
?
octadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoeicosanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
?
octanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
?
palmitoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
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-
-
-
?
additional information
?
-
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enzyme is able to use Escherichia coli acyl-carrier protein. Enzyme extends longer, physiologically relevant acyl-CoA primers when paired with its native acyl-carrier protein than with Escherichia coli acyl-carrier protein
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0058
malonyl-ACP
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
0.009
malonyl-CoA
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
0.0086
malonyl-phosphopantetheine-14-mer
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
0.0051
malonyl-phosphopantetheine-16-mer
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
0.0047
malonyl-phosphopantetheine-8-mer
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donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
0.0004
palmitoyl-CoA
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acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 8.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.47
malonyl-ACP
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
0.35
malonyl-CoA
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
0.38
malonyl-phosphopantetheine-14-mer
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
0.3
malonyl-phosphopantetheine-16-mer
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
0.35
malonyl-phosphopantetheine-8-mer
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
0.08
palmitoyl-CoA
-
acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 8.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
86.7
malonyl-ACP
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
38.3
malonyl-CoA
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
48.3
malonyl-phosphopantetheine-14-mer
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
60
malonyl-phosphopantetheine-16-mer
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
75
malonyl-phosphopantetheine-8-mer
-
donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0072
-
substrate dodecanoyl-[acyl-carrier protein], pH 7.0, 37°C
0.0104
-
substrate octadecanoyl-[acyl-carrier-protein], pH 7.0, 37°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D66N
the non-active site mutation alters the structural stability of the mutant protein structures
F413L
the non-active site mutation alters the structural stability of the mutant protein structures
G269S
the non-active site mutation alters the structural stability of the mutant protein structures
G312S
the non-active site mutation alters the structural stability of the mutant protein structures
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brown, A.K.; Sridharan, S.; Kremer, L.; Lindenberg, S.; Dover, L.G.; Sacchettini, J.C.; Besra, G.S.
Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-ACP synthase III mtFabH: Factors influencing catalysis and substrate specificity
J. Biol. Chem.
280
32539-32547
2005
Mycobacterium tuberculosis
Musayev, F.; Sachdeva, S.; Scarsdale, J.N.; Reynolds, K.A.; Wright, H.T.
Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A
J. Mol. Biol.
346
1313-1321
2005
Mycobacterium tuberculosis
Borgaro, J.; Chang, A.; MacHutta, C.; Zhang, X.; Tonge, P.
Substrate recognition by beta-ketoacyl-ACP synthases
Biochemistry
50
10678-10686
2011
Escherichia coli, Mycobacterium tuberculosis
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