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Information on EC 2.3.1.179 - beta-ketoacyl-[acyl-carrier-protein] synthase II and Organism(s) Streptococcus pneumoniae and UniProt Accession Q9FBC2
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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: Streptococcus pneumoniae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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a (Z)-hexadec-9-enoyl-[acyl-carrier protein]
+
=
a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein]
+
+
Synonyms
kasii, kas ii, 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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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
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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
myristoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
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?
additional information
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analysis of interaction between FabF and the 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
myristoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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endogenous H2O2 (mainly produced by pyruvate oxidase) inhibits FabF activity by specifically oxidizing its active site cysteine-thiol residue
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
hanging drop vapor diffusion method. 1.3 A resolution crystal structure
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purified recombinant mutant H303A from 20% polyethylene glycol 3350, 0.2 M potassium acetate, X-ray diffraction structure determination and analysis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E383A
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
E346A
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site-directed mutagenesis, the mutant shows similar activity compared to the wild-type enzyme
E396A
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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
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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
K332A
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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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant His-tagged FabF from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
gene fabF, subcloning in Escherichia coli strain XL1-Blue, expression in Escherichia coli strain BL21(DE3)
expression of wild-type and mutant His-tagged FabF in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Price, A.C.; Rock, C.O.; White, S.W.
The 1.3-Angstrom-resolution crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae
J. Bacteriol.
185
4136-4143
2003
Streptococcus pneumoniae
Zhang, Y.; Hurlbert, J.; White, S.W.; Rock, C.O.
Roles of the active site water, histidine 303, and phenylalanine 396 in the catalytic mechanism of the elongation condensing enzyme of Streptococcus pneumoniae
J. Biol. Chem.
281
17390-17399
2006
Streptococcus pneumoniae
Parthasarathy, G.; Cummings, R.; Becker, J.W.; Soisson, S.M.
Surface-entropy reduction approaches to manipulate crystal forms of beta-ketoacyl acyl carrier protein synthase II from Streptococcus pneumoniae
Acta Crystallogr. Sect. D
D64
141-148
2008
Streptococcus pneumoniae (Q9FBC2), Streptococcus pneumoniae
Parthasarathy, G.; Cummings, R.; Becker, J.W.; Soisson, S.M.
Surface-entropy reduction approaches to manipulate crystal forms of beta-ketoacyl acyl carrier protein synthase II from Streptococcus pneumoniae
Acta Crystallogr. Sect. D
64
141-148
2008
Streptococcus pneumoniae (Q9FBC2), Streptococcus pneumoniae
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Release 2023.1 (January 2023)
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