Information on EC 2.3.1.179 - beta-ketoacyl-[acyl-carrier-protein] synthase II

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.3.1.179
-
RECOMMENDED NAME
GeneOntology No.
beta-ketoacyl-[acyl-carrier-protein] synthase II
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a (Z)-hexadec-11-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
show the reaction diagram
-
-
-
-
a (Z)-hexadec-11-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
show the reaction diagram
elongation condensing enzyme, catalytic mechanism involving Cys134, His337, and His303, forming the catalytic triad, as well as Phe396, and a water molecule bound to the active site, analysis of residues involved in the different reaction steps, overview
-
a (Z)-hexadec-11-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
show the reaction diagram
active site structure with the Cys-His-His active site triad and the acyl binding channel, reaction mechanism, modeling
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Claisen condensation
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biotin metabolism
-
cis-vaccenate biosynthesis
-
Fatty acid biosynthesis
-
Metabolic pathways
-
mycolate biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
(Z)-hexadec-11-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-ACP synthase I, it differs in that palmitoleoyl-ACP 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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-ketoacyl acyl synthase II
-
-
3-ketoacyl-ACP synthase
-
-
3-ketoacyl-ACP synthase 2
Q9C9P4
-
3-ketoacyl-ACP synthase II
Q9C9P4
-
3-ketoacyl-ACP synthase II
-
-
beta-ketoacyl ACP-synthase II
-
-
beta-ketoacyl acyl carrier protein synthase II
-
-
beta-ketoacyl acyl-carrier protein synthase II
Q9FBC2
-
beta-ketoacyl synthase II
P0AAI5
-
beta-ketoacyl-ACP synthase FabF3
-
KAS-II homologue
beta-ketoacyl-ACP synthase II
-
-
beta-ketoacyl-ACP synthase II
-
-
beta-ketoacyl-ACP synthase II
P0AAI5
-
beta-ketoacyl-ACP synthase II
-
-
beta-ketoacyl-ACP synthase II
-
-
beta-ketoacyl-acyl carrier protein synthase I/II
-
-
beta-ketoacyl-acyl carrier protein synthase II
-
-
beta-ketoacyl-acyl carrier protein synthase II
-
-
beta-ketoacyl-acyl carrier protein synthase II
P0AAI5
-
beta-ketoacyl-acyl carrier protein synthase II
Q000L2
-
beta-ketoacyl-acyl carrier protein synthases II
P0AAI5
-
beta-ketoacyl-acyl carrier protein synthetase II
P0AAI5
-
beta-ketoacyl-acyl-carrier protein synthase II
-
-
beta-ketoacyl-acyl-carrier-protein synthase II
-
-
beta-ketoacyl-acyl-carrier-protein synthase II
Elaeis guineensis Jacq.
-
-
-
beta-ketoacyl-[acyl carrier protein (ACP)] synthase II
-
-
beta-ketoacyl-[acyl-carrier protein (ACP)] synthase II
-
-
beta-ketoacyl-[acyl-carrier-protein] synthase II
-
-
FabF
P0AAI5
-
FabF elongation condensing enzyme
-
-
FabF of type II fatty acid biosynthesis
-
-
FabF of type II fatty acid biosynthesis
-
-
-
FabF of type II fatty acid biosynthesis
-
-
KAS II
Q9C9P4
-
KAS II
P0AAI5
-
KASII
P0AAI5
-
CAS REGISTRY NUMBER
COMMENTARY
9077-10-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Northern ecotype
-
-
Manually annotated by BRENDA team
gene fabF homologues designated as CAC3573, CAC2008 and CAA0093
-
-
Manually annotated by BRENDA team
Elaeis guineensis Jacq.
-
-
-
Manually annotated by BRENDA team
enzyme is encoded by the fabJ gene
SwissProt
Manually annotated by BRENDA team
subspecies lactis IL1403
-
-
Manually annotated by BRENDA team
strain H37Rv, gene mtkasB, i.e. Rv2246
-
-
Manually annotated by BRENDA team
syn. Jessenia bataua
-
-
Manually annotated by BRENDA team
gene PffabB/F
-
-
Manually annotated by BRENDA team
; methicillin-resistant and vancomycin-resistant strains
-
-
Manually annotated by BRENDA team
-
Q9FBC2
SwissProt
Manually annotated by BRENDA team
gene fabF
Q9FBC2
SwissProt
Manually annotated by BRENDA team
PCC 6803
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
endogenous H2O2 (mainly produced by pyruvate oxidase) inhibits FabF activity by specifically oxidizing its active site cysteine-thiol residue
physiological function
Q9C9P4
KAS2 is necessary for embryo development
physiological function
-
encoded in the gene cluster required for biosynthesis of the calcium dependent antibiotics
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(Z)-hexadec-11-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
(Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
-
(Z)-hexadec-11-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
(Z)-3-oxooctadeca-13-enoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
cis-3-decenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
decanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
dodec-5-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
show the reaction diagram
P0AAI5
-
-
-
?
malonyl-ACP + lauroyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-CoA + lauroyl-CoA
?
show the reaction diagram
-
-
-
-
?
malonyl-phosphopantetheine + lauroyl-CoA
?
show the reaction diagram
-
-
-
-
?
malonyl-phosphopantetheine-14-mer + lauroyl-CoA
?
show the reaction diagram
-
-
-
-
?
malonyl-phosphopantetheine-16-mer + lauroyl-CoA
?
show the reaction diagram
-
-
-
-
?
myristoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
palmitoleoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
cis-vaccenoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
P0AAI5
-
-
-
?
palmitoleoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
cis-vaccenoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
palmitoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
tetradec-7-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
show the reaction diagram
P0AAI5
-
-
-
?
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
show the reaction diagram
P0AAI5
-
-
-
?
malonyl-phosphopantetheine-8-mer + lauroyl-CoA
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
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
?
-
P0AAI5
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 is involved in elongation of palmitoyl-[acyl-carrier-protein] to stearoyl-[acyl-carrier-protein]
-
-
-
additional information
?
-
-
the enzyme plays a key role in synthesis of C18 fatty acids, enzyme is inactive with stearoyl-[acyl-carrier-protein]
-
-
-
additional information
?
-
-
KASII elongates 16:0-acyl carrier protein to 18:0-acyl carrier protein in the plastid, where it competes with three other enzymes at the first major branch point in fatty acid biosynthesis
-
-
-
additional information
?
-
-
the beta-ketoacyl acyl carrier protein synthase II is a mycobacterial elongation condensing enzyme involved in FAS-II, FAS-II is considered to elongate medium chain length fatty acyl primers to provide long chain, C56, precursors of mycolic acids, mycolic acids are long chain alpha-alkyl branched, beta-hydroxy fatty acids that represent a characteristic component of the Mycobacterium tuberculosis cell wall
-
-
-
additional information
?
-
-
analysis of interaction between FabF and the acyl-carrier protein
-
-
-
additional information
?
-
-
FabF produces C14 long-chain beta-ketoacyl-ACP
-
-
-
additional information
?
-
-
the enzyme catalyzes the Claisen-type condensation reaction
-
-
-
additional information
?
-
-
FabF1 is able to catalyze all of the elongation reactions required in the synthesis of saturated fatty acids. The single 3-ketoacyl-[acyl-carrier-protein] synthase FabF of this bacterium performs the elongation functions required in both branches of the fatty acid synthetic pathway. The enzyme can both elongate palmitoleoyl-[acyl-carrier-protein] to cis-vaccenoyl-[acyl-carrier-protein] and elongate the cis double bond containing the product of FabA
-
-
-
additional information
?
-
Q9C9P4
KAS II catalyzes the elongation of 16:0 fatty acid-[acyl-carrier-protein] to 18:0 fatty acid-[acyl-carrier-protein] in plastids
-
-
-
additional information
?
-
-
of the enzymes encoded by fabF homologues designated as CAC3573, CAC2008 and CAA0093, only the first of these genes, fabF1, functions in fatty acid synthesis and can functionally replace Escherichia coli FabF in vivo, overview
-
-
-
additional information
?
-
-
PfFabB/F does not elongate C16DELTA9-[acyl-carrier-protein], substrate specificity, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(Z)-hexadec-11-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
(Z)-3-oxooctadec-13-enoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
-
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
-
-
-
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
?
-
P0AAI5
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 is involved in elongation of palmitoyl-[acyl-carrier-protein] to stearoyl-[acyl-carrier-protein]
-
-
-
additional information
?
-
-
the enzyme plays a key role in synthesis of C18 fatty acids
-
-
-
additional information
?
-
-
KASII elongates 16:0-acyl carrier protein to 18:0-acyl carrier protein in the plastid, where it competes with three other enzymes at the first major branch point in fatty acid biosynthesis
-
-
-
additional information
?
-
-
the beta-ketoacyl acyl carrier protein synthase II is a mycobacterial elongation condensing enzyme involved in FAS-II, FAS-II is considered to elongate medium chain length fatty acyl primers to provide long chain, C56, precursors of mycolic acids, mycolic acids are long chain alpha-alkyl branched, beta-hydroxy fatty acids that represent a characteristic component of the Mycobacterium tuberculosis cell wall
-
-
-
additional information
?
-
-
FabF1 is able to catalyze all of the elongation reactions required in the synthesis of saturated fatty acids. The single 3-ketoacyl-[acyl-carrier-protein] synthase FabF of this bacterium performs the elongation functions required in both branches of the fatty acid synthetic pathway. The enzyme can both elongate palmitoleoyl-[acyl-carrier-protein] to cis-vaccenoyl-[acyl-carrier-protein] and elongate the cis double bond containing the product of FabA
-
-
-
additional information
?
-
Q9C9P4
KAS II catalyzes the elongation of 16:0 fatty acid-[acyl-carrier-protein] to 18:0 fatty acid-[acyl-carrier-protein] in plastids
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mn2+
-
divatent cations such Mn neutralize inhibition by EDTA
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Acyl carrier protein
-
0.0017 mM, 50% inhibition of myristic acid transfer from myristoyl-[acyl-carrier protein] to wild-type enzyme
arsenite
-
1 mM, 42% inhibition
cerulenin
-
0.05 mM, 50% inhibition
cerulenin
-
0.1 mM, 50% inhibition
cerulenin
-
binding structure with mutant C163Q
cerulenin
-
blocking active site cysteine
dihydroplatensimycin
-
IC50: 97 nM
NEM
-
5 mM, complete inhibition
PCMB
-
1 mM, complete inhibition
platencin
-
; exhibits a broad-spectrum Gram-positive antibacterial activity through inhibition of fatty acid biosynthesis, targets the two essential proteins, beta-ketoacyl-[acyl carrier protein] synthase II and III, i.e. FabF and FabH, FabF IC50: 113 nM, overview
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
platensimycin
-
from Streptomyces platensis, IC50: 48 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
platensimycin
-
; from a strain of Streptomyces platensis MA7339, specifically targets FabF, IC50: 290 nM, exhibits Gram-positive antibacterial activity
thiolactomycin
-
binding structure, modeling
thiolactomycin
-
binding structure with mutant C163Q, IC50: 1.1 mM
iodoacetamide
-
prior incubation of the enzymes with fatty acyl thioesters prevents inhibition
additional information
-
in vivo inhibition assays
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.014
-
acetyl-[acyl-carrier protein]
-
pH 7.2
0.017
-
cis-3-decenoyl-[acyl-carrier protein]
-
pH 7.2
0.0133
-
decanoyl-[acyl-carrier protein]
-
-
0.024
-
dodec-5-enoyl-[acyl-carrier protein]
-
27C; 37C
0.0537
-
Lauroyl-CoA
-
wild type protein, acceptor malonyl-CoA, 0.5 mM malonyl-CoA, pH 6.5, 25C
0.0082
-
malonyl-ACP
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25C
0.0055
-
malonyl-CoA
-
-
0.0283
-
malonyl-CoA
-
R206G mutant protein, donor lauroyl-CoA, 0.1 mM lauroyl-CoA, pH 6.5, 25C
0.51
-
malonyl-CoA
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
0.59
-
malonyl-phosphopantetheine
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
-
0.0061
-
malonyl-phosphopantetheine-14-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
-
0.0062
-
malonyl-phosphopantetheine-16-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
-
0.0237
-
malonyl-phosphopantetheine-8-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
-
0.0139
-
myristoyl-[acyl-carrier protein]
-
-
0.04
-
palmitoleoyl-[acyl-carrier protein]
-
pH 7.2
0.097
-
palmitoleoyl-[acyl-carrier protein]
-
27C
0.216
-
palmitoleoyl-[acyl-carrier protein]
-
37C
0.0036
-
palmitoyl-[acyl-carrier protein]
-
-
0.043
-
tetradec-7-enoyl-[acyl-carrier protein]
-
27C
0.06
-
tetradec-7-enoyl-[acyl-carrier protein]
-
37C
0.047
-
tetradecanoyl-[acyl-carrier protein]
-
27C
0.068
-
tetradecanoyl-[acyl-carrier protein]
-
37C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.047
-
Lauroyl-CoA
-
wild type protein, acceptor malonyl-CoA, 0.5 mM malonyl-CoA, pH 6.5, 25C
0.029
-
malonyl-ACP
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25C
0.022
-
malonyl-CoA
-
R206G mutant protein, donor lauroyl-CoA, 0.1 mM lauroyl-CoA, pH 6.5, 25C
0.042
-
malonyl-CoA
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
0.022
-
malonyl-phosphopantetheine
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
-
0.023
-
malonyl-phosphopantetheine-14-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
-
0.022
-
malonyl-phosphopantetheine-16-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
-
0.018
-
malonyl-phosphopantetheine-8-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1
-
Lauroyl-CoA
-
wild type protein, acceptor malonyl-CoA, 0.5 mM malonyl-CoA, pH 6.5, 25C
12519
3.8
-
malonyl-ACP
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25C
21863
0.083
-
malonyl-CoA
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
12844
0.83
-
malonyl-CoA
-
R206G mutant protein, donor lauroyl-CoA, 0.1 mM lauroyl-CoA, pH 6.5, 25C
12844
0.037
-
malonyl-phosphopantetheine
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
0
4.2
-
malonyl-phosphopantetheine-14-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
0
3.8
-
malonyl-phosphopantetheine-16-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
0
0.083
-
malonyl-phosphopantetheine-8-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25C
0
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000113
-
platencin
-
exhibits a broad-spectrum Gram-positive antibacterial activity through inhibition of fatty acid biosynthesis, targets the two essential proteins, beta-ketoacyl-[acyl carrier protein] synthase II and III, i.e. FabF and FabH, FabF IC50: 113 nM, overview
0.000048
-
platensimycin
-
from Streptomyces platensis, IC50: 48 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 th
0.00016
-
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 t
0.00029
-
platensimycin
-
from a strain of Streptomyces platensis MA7339, specifically targets FabF, IC50: 290 nM, exhibits Gram-positive antibacterial activity
1.1
-
thiolactomycin
-
binding structure with mutant C163Q, IC50: 1.1 mM
0.000097
-
dihydroplatensimycin
-
IC50: 97 nM
additional information
-
additional information
-
IC50 for platencin is 0.00195 ng/ml, IC50 for platensimycin is 0.00013 ng/ml
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
development of an elongation assay with FabF and FabH, EC 2.3.1.41
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
6.1
-
-
6.8
7
-
assay at
7
-
-
assay at
7.5
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.1
-
Q9C9P4
KAS2, sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
sheath, lamina epidermis and underlying parenchyma
Manually annotated by BRENDA team
-
activity rises rapidly by approximately 30 days after flowering and reaches a peak of activity at between 44 and 52 days after flowering
Manually annotated by BRENDA team
-
modulation of Arabidopsis KASII levels is sufficient to convert its temperate oilseed composition to that of a palm-like tropical oil
Manually annotated by BRENDA team
Q9C9P4
high KAS2 expression level, especially in cotyledonary stage embryos
Manually annotated by BRENDA team
-
shortening of the photoperiod does not significantly affect the expression of the enzyme. Low positive temperatures stimulate the gene expression after 1 week of treatment
Manually annotated by BRENDA team
additional information
Q9C9P4
KAS2 is expressed in all plant organs, except for roots and hypocotyls
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bartonella henselae (strain ATCC 49882 / Houston 1)
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Burkholderia vietnamiensis (strain G4 / LMG 22486)
Burkholderia vietnamiensis (strain G4 / LMG 22486)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Neisseria meningitidis (strain alpha14)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Rickettsia rickettsii (strain Sheila Smith)
Staphylococcus aureus (strain MW2)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
56000
-
-
gel filtration
76000
-
-
gel filtration
84000
-
-
nondenaturing PAGE
85000
-
-
equilibrium sedimentation
87800
-
-
gel filtration
88000
-
-
recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q9C9P4
x * 57600, KAS2, sequence calculation
dimer
-
2 * 44000-45000, SDS-PAGE
dimer
-
homodimer, crystal structure, mtKasB adopts a thiolase fold but contains unique structural features in the capping region that may be crucial to its preference for longer fatty acyl chains than its counterparts from other bacteria, residues 1-260 and 261-415 form topologically equivalent N and C-terminal betaalphabetaalphabetaalphabetabeta motifs, overview, structure comparisons
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure determination and analysis at 2.6 A resolution
-
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
-
purified recombinant enzyme, sitting drop vapour diffusion method, from 100 mM Caps, pH 10.5, 20% w/v PEG 8000, 200 mM NaCl, and 5 mM C16-CoA, with spermidine-HCl and Foscholine-9 detergent added, X-ray diffraction crystal structure determination and analysis at 2.4-3.0 A resolution, molecular replacement, structure modeling
-
hanging drop vapor diffusion method. 1.3 A resolution crystal structure
-
hanging-drop vapour-diffusion method
Q9FBC2
purified recombinant mutant H303A from 20% polyethylene glycol 3350, 0.2 M potassium acetate, X-ray diffraction structure determination and analysis
-
purified recombinant wild-type and mutant E383A enzymes, hanging-drop vapour-diffusion method at room temperature, 0.001 ml of protein solution, containing 10 mg/mlprotein in 20 mM Tris-HCl, pH 8.0, 50 mM NaCl, and 10% glycerol, is mixed with 0.001 ml of precipitating solution, containing 0.2 M sodium acetate, 0.1 M Tris-HCl, pH 8.5, and 30% PEG 4000, formation of different crystal forms, X-ray diffraction structure determinations and analysis at 1.3-2.1 A resolution
Q9FBC2
rod-shaped crystals of the purified enzyme are grown in two weeks by the hanging-drop vapor-diffusion method, 1.54 A resolution, space group P3(1)21, cells dimensions: a = b = 100.8 A, c = 74.7 A
P73283, -
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
43
-
-
t1/2: 81 min
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
to homogeneity (>9000-fold purification), ion exchange chromatography (CM-Sepharose, HR-DEAE), hydroxyapatite and affinity chromatography (ACP-Sepharose)
-
immobilized metal ion affinity chromatography (Ni2+)
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration to near homogeneity
-
immobilized metal ion affinity chromatography (Ni2+)
-
recombinant wild-type and mutant His-tagged FabF from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
AtKAS2, DNA and amino acid sequence determination and analysis, sequence comparisons, expression pattern, the promoter is active in various tissues, also in the embryo
Q9C9P4
gene fabF1, expression in Escherichia coli strain BL21(DE3), and in strain K1060, a strain that carries an unconditional fabB allele, and in Escherichia coli strain CY242, which carries the same fabB(Ts) allele as strain CY244, but fabF1 fails to complement growth of the temperature sensitive fabB mutant strain CY242 at 42C
-
overexpressed in Enterococcus faecalis
-
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
-
His-tagged protein expressed in Escherichia coli pLysS
-
expressed in Arabidopsis thaliana
-, Q000L2
Lactococcus lactis FabF can functionally replace both the FabB (EC 2.3.1.41) and FabF (2.3.1.179) proteins of Escherichia coli and the FabH protein of Lactococcus lactis
-
gene mtkasB, expression of His-tagged enzyme in Escherichia coli
-
His-tagged protein expressed in Escherichia coli is insoluble and not functional, GFP fusion protein expressed in Arabidopsis thaliana, Arabidopsis plants expressing GFP fusions have elevated levels of arachidic acid (C20:0) and erucic acid (C22:1) at the expense of stearic acid (C18:0) and oleic acid (C18:1)
-
gene PffabB/Fm, FabB/F is encoded at locus MAL6P1.165, cloning and expression, expression in and complementation of Escherichia coli strain CY244, which is deficient in FabB and FabF, the latter by mutations S220N and G262M
-
construction of plasmids pXspFabF(M1) and pXspFabF(M2). The resulting plasmids are transformed into Escherichia coli XL1-Blue competent cells. Subsequently, pXSpFabF(M1) and pXspFabF(M2) isolated from Escherichia coli XL1-Blue cells are transformed into the expression strain Escherichia coli BL21 (DE3)
Q9FBC2
expression of wild-type and mutant His-tagged FabF in Escherichia coli strain BL21(DE3)
-
gene fabF, subcloning in Escherichia coli strain XL1-Blue, expression in Escherichia coli strain BL21(DE3)
Q9FBC2
His-tagged protein expressed in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli BL21(DE3)
-
expression in Escherichia coli
P73283, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
during seed maturation
-, Q000L2
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C163Q
-
site-directed mutagenesis, interaction with platensimycin compared to the interaction with the wild-type enzyme
C164A
-
site-directed mutagenesis, inactive mutant
C164A/H337A
-
site-directed mutagenesis, inactive mutant
C164A/K332A
-
site-directed mutagenesis, inactive mutant
E346A
-
site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
E383A
Q9FBC2
crystal structure determination and comparison to the wild-type enzyme, the mutation E383A appears to play a key role in disfavouring the less desirable triclinic crystal form and in generating a new surface for a packing interaction that stabilizes the new crystal form
E396A
-
site-directed mutagenesis, the mutant shows no condensation activity but retains about 50% of wild-type transacylation activity with acyl-ACP and ACP, and 40% of wild-type decarboxylation activity
H303A
-
site-directed mutagenesis, the mutant shows 74% reduced condensation activity, 40% reduced transacylation activity, and 5fold increased decarboxylation activity, compared to the wild-type enzyme
H337A
-
site-directed mutagenesis, inactive mutant
K332A
-
site-directed mutagenesis, the mutant shows no condensation activity but retains about 30% of wild-type transacylation activity with acyl-ACP and ACP, and 10% of wild-type decarboxylation activity
F107I
-
less efficient than wild type protein
F107L
-
less efficient than wild type protein
F107S
-
suggested that the Ser residue has less significant effects than the Ile and Leu mutations
L337F
Q9C9P4
the point mutation, mutant fab1-1, causes a partially deficient KAS2 activity
additional information
-
construction of KASII knockout mutants by T-DNA disruption, knockout alleles fab1-1 and fab1-2, strong seed-specific hairpin-RNAi reductions in FAB1 expression resulted in abortion of about 1/4 of the embryos in an apparent phenocopy of fab1-2 homozygosity, in less severe FAB1 hairpin-RNAi individuals, embryos developed normally and exhibited a 1:2:1 segregation ratio for palmitate accumulation, thus, early embryo development appears sensitive to elevated 16:0, whereas at later stages, up to 53% of 16:0, i.e. a 7-fold increase over wild-type levels, is tolerated, Fab1-1 mutant plants show about 60% of wild-type enzyme activity and about 17% palm-like oil accumulation compared to the wild-type plants, phenotypes, overview
additional information
Q9C9P4
construction of a KAS2 T-DNA insertion mutant, the mutation causes arrest of embryonal development and embryo lethality, phenotype, overview
additional information
-
expression of Clostridium acetobutylicium FabF1 restores thermal control of fatty acid composition to an Escherichia coli FabF null mutant strain. FabF1 expression leads a modest conversion of cis-3-decenoyl-[acyl-carrier-protein] to trans-2-cis-5-dodecadienoyl-[acyl carrier-protein]. An Escherichia coli fabF- strain in which Clostridium acetobutylicium FabF1 is expressed from the lac promoter of a low copy number vector closely mimicks the changes in fatty acid composition seen in wild type Escherichia coli strains upon changes in growth temperature. Expression of Clostridium acetobutylicium FabF1 restores cis-vaccenate synthesis at all temperatures, but is much more effective at 30C than at 37C or 42C
R206G
-
R206 impairs the binding of CoA
additional information
-
in vitro complementation of the enzyme-deficient Escherichia coli CY244 strain, shows that Plasmodium falciparum FabB/F functions like Escherichia coli FabF as the growth of the mutant cells can be rescued only in the presence of oleic acid
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
modulating KASII activity is sufficient to convert the composition of a temperate seed oil into that of a palm-like tropical oil, overview
drug development
-
the enzyme is a target for antibacterial drugs
drug development
-
the enzyme, along with the other enzyme involved in the FAS-II complex, is a potential target for development of anti-tubercular drugs
drug development
-
the enzyme is a target for antibacterial drugs