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Information on EC 2.3.1.179 - beta-ketoacyl-[acyl-carrier-protein] synthase II and Organism(s) Escherichia coli and UniProt Accession P0AAI5
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2.3.1.179 beta-ketoacyl-[acyl-carrier-protein] synthase IIIUBMB Comments
Involved in the dissociated (or type II) fatty acid biosynthesis system that occurs in plants and bacteria. While the substrate specificity of this enzyme is very similar to that of EC 2.3.1.41, beta-ketoacyl-[acyl-carrier-protein] synthase I, it differs in that palmitoleoyl-[acyl-carrier protein] is not a good substrate of EC 2.3.1.41 but is an excellent substrate of this enzyme [1,2]. The fatty-acid composition of Escherichia coli changes as a function of growth temperature, with the proportion of unsaturated fatty acids increasing with lower growth temperature. This enzyme controls the temperature-dependent regulation of fatty-acid composition, with mutants lacking this acivity being deficient in the elongation of palmitoleate to cis-vaccenate at low temperatures [3,4].
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Word Map
- 2.3.1.179
- cerulenin
- malonyl-acp
- acyl-acps
- drug development
-
cis-vaccenic
- stearoyl-acp
- thiolactomycin
- fasii
-
claisen
- biotechnology
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
=
+
+
a (Z)-hexadec-9-enoyl-[acyl-carrier protein]
+
=
a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein]
+
+
Synonyms
kas ii, kasii, fabf1, beta-ketoacyl-acp synthase ii, fabb/f, fatty acid synthesis type ii, 3-ketoacyl-acp synthase ii, beta-ketoacyl-acyl carrier protein synthase ii, kas-ii, beta-ketoacyl synthase ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(Z)-hexadec-9-enoyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating)
Involved in the dissociated (or type II) fatty acid biosynthesis system that occurs in plants and bacteria. While the substrate specificity of this enzyme is very similar to that of EC 2.3.1.41, beta-ketoacyl-[acyl-carrier-protein] synthase I, it differs in that palmitoleoyl-[acyl-carrier protein] is not a good substrate of EC 2.3.1.41 but is an excellent substrate of this enzyme [1,2]. The fatty-acid composition of Escherichia coli changes as a function of growth temperature, with the proportion of unsaturated fatty acids increasing with lower growth temperature. This enzyme controls the temperature-dependent regulation of fatty-acid composition, with mutants lacking this acivity being deficient in the elongation of palmitoleate to cis-vaccenate at low temperatures [3,4].
CAS REGISTRY NUMBER
COMMENTARY
9077-10-5
-
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
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
-
-
-
?
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
?
cis-3-decenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
-
-
-
?
dodec-5-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
-
-
-
?
palmitoleoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
cis-vaccenoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
?
tetradec-7-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
-
-
-
?
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
-
-
-
?
additional information
?
-
beta-ketoacyl-acyl carrier protein synthase II is centrally involved in the temperature regulation of the fatty acid composition of the membrane phospholipid of Escherichia coli. The genetic locus of the Cvc lesion is designated fabF
-
-
?
additional information
?
-
-
beta-ketoacyl-acyl carrier protein synthase II is centrally involved in the temperature regulation of the fatty acid composition of the membrane phospholipid of Escherichia coli. The genetic locus of the Cvc lesion is designated fabF
-
-
?
additional information
?
-
proposed role of the enzyme in the modulation of fatty acid synthesis by temperature
-
-
?
additional information
?
-
the enzyme carries out the elongation step in fatty acid synthesis
-
-
?
additional information
?
-
-
the enzyme carries out the elongation step in fatty acid synthesis
-
-
?
additional information
?
-
-
altered molecular form of acyl carrier protein associated with beta-ketoacyl-acyl carrier protein synthase II (fabF) mutants. F-ACP is a modification of ACP that is detected when beta-ketoacyl-ACP synthase II activity is impaired
-
-
?
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
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
-
-
-
?
additional information
?
-
beta-ketoacyl-acyl carrier protein synthase II is centrally involved in the temperature regulation of the fatty acid composition of the membrane phospholipid of Escherichia coli. The genetic locus of the Cvc lesion is designated fabF
-
-
?
additional information
?
-
-
beta-ketoacyl-acyl carrier protein synthase II is centrally involved in the temperature regulation of the fatty acid composition of the membrane phospholipid of Escherichia coli. The genetic locus of the Cvc lesion is designated fabF
-
-
?
additional information
?
-
proposed role of the enzyme in the modulation of fatty acid synthesis by temperature
-
-
?
additional information
?
-
the enzyme carries out the elongation step in fatty acid synthesis
-
-
?
additional information
?
-
-
the enzyme carries out the elongation step in fatty acid synthesis
-
-
?
additional information
?
-
-
altered molecular form of acyl carrier protein associated with beta-ketoacyl-acyl carrier protein synthase II (fabF) mutants. F-ACP is a modification of ACP that is detected when beta-ketoacyl-ACP synthase II activity is impaired
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Acyl carrier protein
0.0017 mM, 50% inhibition of myristic acid transfer from myristoyl-[acyl-carrier protein] to wild-type enzyme
iodoacetamide
prior incubation of the enzymes with fatty acyl thioesters prevents inhibition
platensimycin
from Streptomyces platensis, IC50: 160 nM, anti-bacterial effect is exerted through the selective targeting of beta-ketoacyl-[acyl-carrier-protein] synthase I/II, FabF/B, in the synthetic pathway of fatty acids, platensimycin interacts specifically with the acyl-enzyme intermediate of the target protein, a specific conformational change that occurs on acylation must take place before the inhibitor can bind, overview, platensimycin shows no cross-resistance to other key antibiotic-resistant strains, binding structure with mutant C163Q
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0537
lauroyl-CoA
-
wild type protein, acceptor malonyl-CoA, 0.5 mM malonyl-CoA, pH 6.5, 25°C
0.0082
malonyl-ACP
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.59
malonyl-phosphopantetheine
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.0061
malonyl-phosphopantetheine-14-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.0062
malonyl-phosphopantetheine-16-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.0237
malonyl-phosphopantetheine-8-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.0283
malonyl-CoA
-
R206G mutant protein, donor lauroyl-CoA, 0.1 mM lauroyl-CoA, pH 6.5, 25°C
0.51
malonyl-CoA
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.047
lauroyl-CoA
-
wild type protein, acceptor malonyl-CoA, 0.5 mM malonyl-CoA, pH 6.5, 25°C
0.029
malonyl-ACP
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.022
malonyl-phosphopantetheine
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.023
malonyl-phosphopantetheine-14-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.022
malonyl-phosphopantetheine-16-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.018
malonyl-phosphopantetheine-8-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.022
malonyl-CoA
-
R206G mutant protein, donor lauroyl-CoA, 0.1 mM lauroyl-CoA, pH 6.5, 25°C
0.042
malonyl-CoA
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
lauroyl-CoA
-
wild type protein, acceptor malonyl-CoA, 0.5 mM malonyl-CoA, pH 6.5, 25°C
3.8
malonyl-ACP
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.037
malonyl-phosphopantetheine
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
4.2
malonyl-phosphopantetheine-14-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
3.8
malonyl-phosphopantetheine-16-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.083
malonyl-phosphopantetheine-8-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.083
malonyl-CoA
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.83
malonyl-CoA
-
R206G mutant protein, donor lauroyl-CoA, 0.1 mM lauroyl-CoA, pH 6.5, 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00016
platensimycin
Escherichia coli
from Streptomyces platensis, IC50: 160 nM, anti-bacterial effect is exerted through the selective targeting of beta-ketoacyl-[acyl-carrier-protein] synthase I/II, FabF/B, in the synthetic pathway of fatty acids, platensimycin interacts specifically with t
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
enzyme overexpression increases pinocembrin production in recombinant Escherichia coli
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method at room temperature, using 27% PEG 8000 as precipitant and buffered at pH 7.5 with 0.1 M HEPES. Crystal structure is determined with the multiple isomorphous replacement method and refined at 2.4 A resolution, space group P3(1)21
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C163Q
site-directed mutagenesis, interaction with platensimycin compared to the interaction with the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
determined with the multiple isomorphous replacement method and refined at 2.4 A resolution. Hanging drop vapor diffusion method at room temperature, using 27% PEG 8000 as precipitant, buffered at pH 7.5 with 0.1 M HEPES. The crystals grow to a size of 0.5 * 0.3 * 0.2 mm3 within 3 days. The lifetime of these crystals is very limited, they will dissolve within 10 days of their appearance. Addition of 0.1% mercaptoethanol to the reservoir solution significantly increases the life time of the crystals. Space group: P3(1)21 with cell dimensions a = 76.4 A, c = 146.8 A, gamma = 120°
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Garwin, J.L.; Klages, A.L.; Cronan, J.E.
Structural, enzymatic, and genetic studies of beta-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli
J. Biol. Chem.
255
11949-11956
1980
Escherichia coli (P0AAI5)
D'Agnolo, G.; Rosenfeld, I.S.; Vagelos, P.R.
Multiple forms of beta-ketoacyl-acyl carrier protein synthetase in Escherichia coli
J. Biol. Chem.
250
5289-5294
1975
Escherichia coli (P0AAI5)
McGuire, K.A.; McGuire, J.N.; Von Wettstein-Knowles, P.
Acyl carrier protein (ACP) inhibition and other differences between beta-ketoacyl synthase (KAS) I and II
Biochem. Soc. Trans.
28
607-610
2000
Escherichia coli (P0AAI5), Escherichia coli
Huang, W.; Jia, J.; Edwards, P.; Dehesh, K.; Schneider, G.; Lindqvist, Y.
Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes
EMBO J.
17
1183-1191
1998
Escherichia coli (P0AAI5), Escherichia coli
Jackowski, S.; Rock, C.O.
Altered molecular form of acyl carrier protein associated with beta-ketoacyl-acyl carrier protein synthase II (fabF) mutants
J. Bacteriol.
169
1469-1473
1987
Escherichia coli
Magnuson, K.; Carey, M.R.; Cronan, J.E.
The putative fabJ gene of Escherichia coli fatty acid synthesis is the fabF gene
J. bacteriol.
177
3593-3595
1995
Escherichia coli (P0AAI5), Escherichia coli
Garwin, J.L.; Klages, A.L.; Cronan, J.E., Jr.
beta-Ketoacyl-acyl carrier protein synthase II of Escherichia coli. Evidence for function in the thermal regulation of fatty acid synthesis
J. Biol. Chem.
255
3263-3265
1980
Escherichia coli (P0AAI5), Escherichia coli
Wang, J.; Soisson, S.M.; Young, K.; Shoop, W.; Kodali, S.; Galgoci, A.; Painter, R.; Parthasarathy, G.; Tang, Y.S.; Cummings, R.; Ha, S.; Dorso, K.; Motyl, M.; Jayasuriya, H.; Ondeyka, J.; Herath, K.; Zhang, C.; Hernandez, L.; Allocco, J.; Basilio, A.; Tormo, J.R.; Genilloud, O.; Vicente, F.; Pelaez, F.
Platensimycin is a selective FabF inhibitor with potent antibiotic properties
Nature
441
358-361
2006
Staphylococcus aureus, Escherichia coli (P0AAI5)
Borgaro, J.; Chang, A.; MacHutta, C.; Zhang, X.; Tonge, P.
Substrate recognition by beta-ketoacyl-ACP synthases
Biochemistry
50
10678-10686
2011
Escherichia coli
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