Information on EC 2.3.1.41 - beta-ketoacyl-acyl-carrier-protein synthase I:

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EC NUMBERCOMMENTARY
2.3.1.41-

RECOMMENDED NAMEGeneOntology No.
beta-ketoacyl-acyl-carrier-protein synthase IGO:0004315

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [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
mechanismEscherichia coli-486863, 486864
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
structureEscherichia coli-486916
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
acetylation of the synthase III-like polyketid synthase at Ser118Streptomyces peucetius-486934
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
active site cysteineSynechocystis sp.-486936
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
active site cysteineStreptomyces glaucescens-486938
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
synthaseIII/FabH: His-Asn-Cys catalytic triadEscherichia coli, Haemophilus influenzae-486939
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
synthaseIII/FabH: His-Asn-Cys catalytic triadStreptococcus pneumoniaeP0A3C5486939
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
active site cysteine; structure of active site, substrate binding pocket, and subunit structure in relation to substrate specificity of the 3 isozyme typesSynechocystis sp.-486940
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
synthaseII/FabB: His-HIs-Cys catalytic triad; synthaseIII/FabH: His-Asn-Cys catalytic triadEscherichia coli-486941
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
mechanism and active site structure and functionEscherichia coli-486943
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
active site cysteine; mechanismRattus norvegicus-486944
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
active site cysteineCoriandrum sativum-486948
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
mechanism, roles of H303, H337, C164Streptococcus pneumoniae-659029
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
catalytic active site residues are Cys163 and His333, the active site contains two oxyanion holes, stabilizing the thioester oxyanion of acetylated CoA and of acetylated Cys92, respectivelyEscherichia coliP0A953659726
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
comparison of active sites in isoforms KAS I, KAS II and related enzymes, geometry and catalytic role of equivalent residuesEscherichia coli-660470
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
beta-ketoacyl-acyl-carrier protein synthase enzyme joins short carbon units to construct fatty acyl chains by a three-step Claisen condensation reaction, the reaction starts with a trans thioesterification of the acyl primer substrate from ACP to the enzyme, subsequently, the donor substrate malonyl-ACP is decarboxylated to form a carbanion intermediate, which in the third step attacks C1 of the primer substrate giving rise to an elongated acyl chain, H298 serves as a catalytic base in the decarboxylation step, the enzyme possesses a Cys-His-His catalytic triad, Lys328 has a dual role in catalysis: its charge influences acyl transfer to the active site Cys, and the steric restraint imposed on H333, as an obligate hydrogen bond donor at Ne, is of critical importance for decarboxylation activity, active sites of the wild-type KAS I, its H298 mutants, and their acyl complexes, overviewEscherichia coli-673576
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
structure-activity analysis, reaction mechanismHomo sapiensQ9NWU1677030

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
Acyl group transfer----
condensationEscherichia coli--486914, 486917, 486918, 486939, 486943
condensationBrassica napus--486922
condensationStreptomyces peucetius--486934
condensationSynechocystis sp.--486936, 486940
condensationStreptomyces glaucescens--486938
condensationStreptococcus pneumoniaeP0A3C5-486939
condensationRattus norvegicus--486944
condensationStaphylococcus aureusP99159-486946
condensationCuphea lanceolata--486947
decarboxylationEscherichia coli--486863, 486917, 486943
decarboxylationStreptomyces glaucescens--486938
decarboxylationRattus norvegicus--486944
decarboxylationStaphylococcus aureusP99159-486946

PATHWAYKEGG LinkMetaCyc Link
7-keto-8-aminopelargonate biosynthesis I-PWY-6519
fatty acid biosynthesis initiation II-PWY-5966
fatty acid biosynthesis initiation III-PWY-5965
fatty acid elongation -- saturated-FASYN-ELONG-PWY
mycolate biosynthesis-PWYG-321
palmitate biosynthesis I (animals)-PWY-5994
palmitate biosynthesis II (bacteria and plants)-PWY-5971
palmitoleate biosynthesis I-PWY-6282
stearate biosynthesis II (bacteria and plants)-PWY-5989
superpathway of fatty acid biosynthesis initiation (E. coli)-FASYN-INITIAL-PWY

SYSTEMATIC NAMEIUBMB 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].

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
3-ketoacyl-ACP synthaseSpinacia oleracea--486931
3-ketoacyl-ACP synthaseEscherichia coli--704553
3-ketoacyl-acyl carrier protein synthase----
3-oxoacyl synthaseRattus norvegicus--661000
3-oxoacyl-[acyl-carrier-protein] synthase----
acyl-malonyl(acyl-carrier-protein)-condensing enzyme----
beta-ketoacyl ACP synthase IEscherichia coliP0A953-659726
beta-ketoacyl acyl carrier protein synthase----
beta-ketoacyl synthaseRattus norvegicus--661000
beta-ketoacyl synthetase----
beta-ketoacyl [ACP] synthaseHomo sapiensQ9NWU1-677030
beta-ketoacyl-ACP synthaseTrypanosoma bruceiQ586W9-674882
beta-ketoacyl-ACP synthaseHomo sapiensQ9NWU1-677030
beta-ketoacyl-ACP synthase IEscherichia coli--673576
beta-ketoacyl-ACP synthetase----
beta-ketoacyl-ACP-synthaseArabidopsis thalianaQ8L3X9-658746
beta-ketoacyl-acyl carrier protein synthetase----
beta-ketoacyl-CoA synthase-IHelianthus annuus--674095
beta-ketoacyl-[acyl carrier protein (ACP)] synthase IIIStaphylococcus aureus--676903
beta-ketoacyl-[acyl carrier protein] synthase----
beta-ketoacylsynthase----
condensing enzyme----
Cys-His-His-type beta-ketoacyl-acyl carrier protein synthaseEscherichia coli--673576
elongaseTrypanosoma bruceiQ586W9-674882
elongating beta-ketoacyl-acyl carrier protein synthasePlasmodium falciparum--674777
FabBEscherichia coli--704553
FabBFPlasmodium falciparum--674777
FabHStaphylococcus aureus--676903
fatty acid condensing enzyme----
KASSpinacia oleracea--486931
KASBrassica napus--486932
KASStreptomyces glaucescens--486933, 486938
KASAllium ampeloprasum--486935
KASSynechocystis sp.--486936, 486940
KASHomo sapiensQ9NWU1-677030
KAS IEscherichia coli--659726, 673576
synthase, 3-oxoacyl-[acyl-carrier-protein]----
KCSIHelianthus annuus--674095
additional informationEscherichia coli-in vertebrates, yeast and Mycobacteria beta-ketoacyl synthase activity is a domain of the multifunctional polypeptide chains of fatty acid synthase EC 2.3.1.85 and EC 2.3.1.86486863, 486864
additional informationClostridium kluyveri-in vertebrates, yeast and Mycobacteria beta-ketoacyl synthase activity is a domain of the multifunctional polypeptide chains of fatty acid synthase EC 2.3.1.85 and EC 2.3.1.86486863
additional informationStreptomyces glaucescens-enzyme shows also acetyl coenzyme A-acyl-carrier-protein transacylase activity EC 2.3.1.38, 12% compared to beta-keto-[acyl-carrier-protein] synthase activity EC 2.3.1.41486933
additional informationStreptomyces peucetius-gene DpsC, encoding apolyketide synthase, exhibits also beta-keto-[acyl-carrier-protein] synthase III activity, which is restricted for propionyl-[acyl-carrier-protein] as the only [acyl-carrier-protein]-substrate486934
additional informationSynechocystis sp.-3 structural classes of condensing enzymes486940
additional informationEscherichia coliP0A953the enzyme belongs to the superfamily of condensing enzymes which includes thiolases659726

CAS REGISTRY NUMBERCOMMENTARY
9077-10-5-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Allium ampeloprasumsynthase II486935--Manually annotated by BRENDA team
Arabidopsis thaliana-658746Q8L3X9SwissprotManually annotated by BRENDA team
Arabidopsis thalianaexpression in Escherichia coli659442Q8L3X9SwissprotManually annotated by BRENDA team
Bacillus subtilisgenes fabH1 and fabH2, 2 synthase III isozymes486937--Manually annotated by BRENDA team
Brassica juncea-285675--Manually annotated by BRENDA team
Brassica napuscv. Westar486932--Manually annotated by BRENDA team
Brassica napussynthase I and II486922, 486923--Manually annotated by BRENDA team
Carthamus tinctoriussafflower285669, 285675--Manually annotated by BRENDA team
Clostridium kluyveri-486863--Manually annotated by BRENDA team
Coriandrum sativumseed plastid-specific isoform with similarities to synthase I type486948--Manually annotated by BRENDA team
Cuphea lanceolatasynthase IV486947--Manually annotated by BRENDA team
Cuphea lutea-285675--Manually annotated by BRENDA team
Escherichia coli-486863, 486864, 486914, 486915, 486917, 486918, 486939, 660470, 673576--Manually annotated by BRENDA team
Escherichia coli-659726P0A953UniprotManually annotated by BRENDA team
Escherichia coliB; synthases I and II486919--Manually annotated by BRENDA team
Escherichia coligene fabB704553--Manually annotated by BRENDA team
Escherichia coliK12 strains UC1, WN1 is a fabF-mutant lacking synthase II, and various mutants, overview; synthases I and II486916--Manually annotated by BRENDA team
Escherichia colisynthase I486943--Manually annotated by BRENDA team
Escherichia colisynthase III, gene fabH486932, 486937--Manually annotated by BRENDA team
Escherichia colisynthases I, II, and III486941--Manually annotated by BRENDA team
Euglena gracilisZ285676--Manually annotated by BRENDA team
Haemophilus influenzae-486939--Manually annotated by BRENDA team
Helianthus annuus-674095--Manually annotated by BRENDA team
Homo sapiensexpression in Escherichia coli, without N-terminal targeting sequence659451--Manually annotated by BRENDA team
Homo sapiensthe human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase677030Q9NWU1SwissProtManually annotated by BRENDA team
Hordeum vulgarecv. Bonus486925--Manually annotated by BRENDA team
Lactococcus lactissp. lactis IL1403659294--Manually annotated by BRENDA team
Mycobacterium tuberculosis-659493, 659724--Manually annotated by BRENDA team
Mycobacterium tuberculosissynthase I, i.e. KasA486942P63454SwissProtManually annotated by BRENDA team
Mycobacterium tuberculosissynthase II, i.e. KasB486942--Manually annotated by BRENDA team
Petroselinum crispum-486921--Manually annotated by BRENDA team
Pisum sativum-285675--Manually annotated by BRENDA team
Plasmodium falciparumFabF/FabH; strain 3D7, gene fabBF, encoding the only elongating beta-ketoacyl-ACP synthase in the organism674777--Manually annotated by BRENDA team
Rattus norvegicus-486944, 661000--Manually annotated by BRENDA team
Spinacia oleracea-486925--Manually annotated by BRENDA team
Spinacia oleraceasynthase I and II285675, 486920, 486924--Manually annotated by BRENDA team
Spinacia oleraceasynthase III486931--Manually annotated by BRENDA team
Staphylococcus aureus-660466--Manually annotated by BRENDA team
Staphylococcus aureusmethicillin-resistant and vancomycin-resistant strains676903--Manually annotated by BRENDA team
Staphylococcus aureusstrain ATCC 35556; synthase III, gene fabH486946P99159GenBankManually annotated by BRENDA team
Streptococcus pneumoniae-659029--Manually annotated by BRENDA team
Streptococcus pneumoniaesynthase III, gene fabH486939P0A3C5SwissProtManually annotated by BRENDA team
Streptomyces glaucescenssynthase III, gene fabH486933, 486938--Manually annotated by BRENDA team
Streptomyces peucetiussynthase III-like activity486934--Manually annotated by BRENDA team
Synechocystis sp.isozyme II486940--Manually annotated by BRENDA team
Synechocystis sp.synthase II486936--Manually annotated by BRENDA team
Trypanosoma bruceimitochondrial beta-ketoacyl synthase; ssp. brucei, strain 427, procyclic trypanosomes674882Q586W9SwissProtManually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
metabolismEscherichia coli-FabB catalyzes the elongation of cis-3-decenoyl-ACP produced by FabA to generate the first 12-carbon cis-unsaturated fatty acid intermediate, 3-oxo-cis-5-decenoyl-ACP, which is converted to cis-5-dodecenoyl-ACP. FabB is essential in the unsaturated fatty acid, UFA, synthesis pathway, strains lacking FabB are UFA auxotroph, overview. FabB cannot be substituted by FabF704553

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate
LITERATURE/
Substrate
COMMENTARY/
Product
LITERATURE/
Product
Reversibility
r=reversible
ir=irreversible
?=not specified
4-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxo-6-octadecenoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Coriandrum sativum-best substrate, highly specific for, reaction is part of petroselinic acid biosynthesis, synthase IV486948--?
acetyl-CoA + malonyl-CoA3-oxobutyryl-CoA + CoA
show the reaction diagram
Rattus norvegicus--661000formation of about 1% triacetic acid lactone-?
acetyl-CoA + malonyl-[acyl-carrier protein]acetoacyl-[acyl-carrier protein] + CO2 + CoA
show the reaction diagram
Haemophilus influenzae, Escherichia coli--486939-486939?
acetyl-CoA + malonyl-[acyl-carrier protein]acetoacyl-[acyl-carrier protein] + CO2 + CoA
show the reaction diagram
Streptococcus pneumoniaeP0A3C5synthase III, best substrate486939-486939?
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486863, 486864--?
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486914-486914ir
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486915-486915r
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486919-486919r
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea--285675--?
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Petroselinum crispum--486921-486921?
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Streptomyces glaucescens-synthase III486933--?
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Staphylococcus aureusP99159synthase III486946-486946ir
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-synthase III, recombinant enzyme from E. coli is absolutely specific for486931-486931r
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-synthase I486924--?
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosisP63454Kas A and KasB486942--?
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxobutanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Homo sapiens--659451--?
acyl-CoA + [acyl-carrier protein]acyl-[acyl-carrier protein] + CoA
show the reaction diagram
Escherichia coli-tetradecanoyl-CoA and cis-9-hexadecenoyl-CoA are poor substrates486917-486917r
acyl-CoA + [acyl-carrier protein]acyl-[acyl-carrier protein] + CoA
show the reaction diagram
Escherichia coli-catalyzes fatty acyl transfer between CoA and [acyl-carrier-protein], but no direct transfer to the enzyme as with acyl-[acyl-carrier-protein]486863--?
acyl-CoA + [acyl-carrier protein]acyl-[acyl-carrier protein] + CoA
show the reaction diagram
Escherichia coli-catalyzes fatty acyl transfer between CoA and [acyl-carrier-protein], but no direct transfer to the enzyme as with acyl-[acyl-carrier-protein]486917-486917r
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486937--?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Arabidopsis thalianaQ8L3X9-659442--?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-part of non-associated fatty acid synthase system of plants and prokaryotes486863, 486919--?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-part of non-associated fatty acid synthase system of plants and prokaryotes486914--ir
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-part of non-associated fatty acid synthase system of plants and prokaryotes486915--r
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-part of non-associated fatty acid synthase system of plants and prokaryotes486924--?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Clostridium kluyveri-part of non-associated fatty acid synthase system of plants and prokaryotes486863---
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-involved in biosynthesis of saturated fatty acids486914--ir
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-involved in biosynthesis of saturated fatty acids486915, 486917--r
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-involved in biosynthesis of saturated fatty acids486924--?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Brassica napus-involved in biosynthesis of saturated fatty acids486922--r
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Cuphea lanceolata-key enzyme for regulation of medium-chain fatty acid synthesis in seeds486947--?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Staphylococcus aureusP99159initiation of fatty acid biosynthesis, part of fatty acid synthase II486946--ir
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli, Brassica napus-involved in biosynthesis of unsaturated and saturated fatty acids486932--?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosisP63454part of fatty acid synthase system I and II, involved in cell wall mycolic acids biosynthesis, overview486942--?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Bacillus subtilis-initiation of fatty acid biosynthesis with acetyl-CoA as a primer, overview substrate specificity486937--?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-responsible for chain elongation during de novo fatty acid synthesis486863--?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Clostridium kluyveri-responsible for chain elongation during de novo fatty acid synthesis486863---
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-involved in biosynthesis of mono-unsaturated long-chain fatty acids486919--?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Streptomyces glaucescens-initiation of both straight- and branched-chain fatty acid biosynthesis resulting in a wide variety of produced fatty acids in vivo486933, 486938--?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]acyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Plasmodium falciparum-C4 to C14 acyl-[ACP]s, the enzyme readily elongates C4:0-through C10:0-PfACPs, has significantly less activity with C12:0- and C14:0-ACPs, and no capacity for elongation of C16:0-ACP and C18:0-ACP674777--?
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Helianthus annuus-the endoplasmic reticulum enzyme is involved in synthesis of very long chain fatty acids, KCS-I displays a preference for 20:0-CoA, substrate specificity, overview674095--?
butanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxohexanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Homo sapiens--659451--?
butyryl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]beta-ketohexanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486914--ir
butyryl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]beta-ketohexanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Streptomyces glaucescens-synthase III486933--?
butyryl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]beta-ketohexanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Staphylococcus aureusP99159synthase III486946--?
C10-[acyl-carrier protein] + malonyl-[acyl-carrier protein]C12-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Plasmodium falciparum--674777--?
C12-[acyl-carrier protein] + malonyl-[acyl-carrier protein]C14-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Plasmodium falciparum--674777--?
C14-[acyl-carrier protein] + malonyl-[acyl-carrier protein]C16-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Plasmodium falciparum--674777--?
C4-[acyl-carrier protein] + malonyl-[acyl-carrier protein]C6-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Plasmodium falciparum--674777--?
C6-[acyl-carrier protein] + malonyl-[acyl-carrier protein]C8-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Plasmodium falciparum-best substrate674777--?
C8-[acyl-carrier protein] + malonyl-[acyl-carrier protein]C10-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Plasmodium falciparum--674777--?
cis-3-decenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxo-cis-5-dodecenoyl-[acyl-carrier protein] + acyl-carrier protein
show the reaction diagram
Escherichia coli--486919---
cis-3-decenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxo-cis-5-dodecenoyl-[acyl-carrier protein] + acyl-carrier protein
show the reaction diagram
Escherichia coli--704553--?
cis-3-decenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxo-cis-5-dodecenoyl-[acyl-carrier protein] + acyl-carrier protein
show the reaction diagram
Escherichia coli-key step in the unsaturated fatty acid, UFA, synthesis pathway. FabB is negatively regulated by the FabR protein704553the product is not incorporated into the complex lipids of the bacterium-?
cis-9-hexadecenoyl-CoA + malonyl-[acyl-carrier protein]3-oxo-hexadecenoyl-[acyl-carrier protein] + CO2 + CoA
show the reaction diagram
Escherichia coli--486919--?
cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486863--?
cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486917--r
cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-poor substrate, synthase I486916--?
cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-poor substrate, synthase I486919--r
cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-best substrate, synthase II486916--?
cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-best substrate, synthase II486919--r
cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486864--?
cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Clostridium kluyveri--486863--?
cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-not cis-vaccenoyl-[acyl-carrier-protein], i.e. cis-11-octenoyl-[acyl-carrier-protein]486863, 486916--?
cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-not cis-vaccenoyl-[acyl-carrier-protein], i.e. cis-11-octenoyl-[acyl-carrier-protein]486917--r
cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-from C-10 to C-16, e.g. cis-5-decenoyl-[acyl-carrier-protein], cis-5-dodecenoyl-[acyl-carrier-protein], cis-7-tetradecenoyl-[acyl-carrier-protein], cis-9-hexenoyl-[acyl-carrier-protein], i.e. palmitoleoyl-[acyl-carrier-protein], poor substrates486919---
cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-from C-10 to C-16, e.g. cis-5-decenoyl-[acyl-carrier-protein], cis-5-dodecenoyl-[acyl-carrier-protein], cis-7-tetradecenoyl-[acyl-carrier-protein], cis-9-hexenoyl-[acyl-carrier-protein], i.e. palmitoleoyl-[acyl-carrier-protein], poor substrates486916--?
cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-from C-10 to C-16, e.g. cis-5-decenoyl-[acyl-carrier-protein], cis-5-dodecenoyl-[acyl-carrier-protein], cis-7-tetradecenoyl-[acyl-carrier-protein], cis-9-hexenoyl-[acyl-carrier-protein], i.e. palmitoleoyl-[acyl-carrier-protein], poor substrates486917--r
decanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]dodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486863--?
decanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]dodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Homo sapiens--659451--?
decanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]dodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea--486920--?
decanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]dodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosis--659493--?
decanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]dodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-synthase I486924--?
decanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]dodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Cuphea lanceolata-synthase IV486947--?
dodecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxotetradecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486863, 486916--?
dodecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxotetradecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Homo sapiens--659451--?
dodecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxotetradecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea--285675--?
dodecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxotetradecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosis--659493--?
eicosanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxodocosanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosis--659493--?
eicosanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxodocosanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosisP63454Kas A and KasB486942--?
hexadecanoyl-CoA + malonyl-[acyl-carrier protein]3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + CoA
show the reaction diagram
Mycobacterium tuberculosisP63454Kas A and KasB, preference for486942--?
hexadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Coriandrum sativum--486948--?
hexadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-not486863, 486864---
hexadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-poor substrate486920--?
hexadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosisP63454KasA and KasB, preference for486942--?
hexadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-only synthase II, best substrate486924--?
hexadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-i.e. palmitoyl-[acyl-carrier-protein]486916--?
hexadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-i.e. palmitoyl-[acyl-carrier-protein]486920, 486924--?
hexadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Brassica napus-i.e. palmitoyl-[acyl-carrier-protein]486923--?
hexadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-preferred substrate, synthase III285675--?
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486914--ir
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486917--r
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Homo sapiens--659451--?
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea--285675--?
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Brassica napus--486923--?
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosis--659493--?
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Synechocystis sp.--486936--?
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-characterization of hexanoyl-enzyme intermediate486918--r
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-best substrate, synthase I486920, 486924--?
isobutyryl-CoA + malonyl-[acyl-carrier protein]?
show the reaction diagram
Streptomyces glaucescens-synthase III486933, 486938--?
isobutyryl-CoA + malonyl-[acyl-carrier protein]?
show the reaction diagram
Staphylococcus aureusP99159synthase III486946--?
isobutyryl-CoA + malonyl-[acyl-carrier protein]?
show the reaction diagram
Streptomyces glaucescens-isobutyryl-CoA is a precursor of branched-chain fatty acid synthesis486938--?
Malonyl-CoAAcetyl-CoA + CO2
show the reaction diagram
Escherichia coli-decarboxylation reaction673576--?
malonyl-[acyl-carrier protein]acetyl-[acyl-carrier protein] + CO2
show the reaction diagram
Streptomyces glaucescens--486938--?
malonyl-[acyl-carrier protein]acetyl-[acyl-carrier protein] + CO2
show the reaction diagram
Escherichia coli-catalyzes malonyl-[acyl-carrier-protein] decarboxylation independent of fatty acyl-[acyl-carrier-protein]486917-486917?
malonyl-[acyl-carrier protein]acetyl-[acyl-carrier protein] + CO2
show the reaction diagram
Escherichia coli-decarboxylation with 2-3% the rate of beta-ketoacyl-[acyl-carrier-protein]-synthesis486863-486863?
malonyl-[acyl-carrier protein]acetyl-[acyl-carrier protein] + CO2
show the reaction diagram
Escherichia coli-wild-type synthase I and mutants C163A and C163S486943-486943?
malonyl-[acyl-carrier protein] + lauroyl-CoA? + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosis--659724--?
malonyl-[acyl-carrier protein] + myristoyl-CoA? + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosis--659724--?
myristoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Homo sapiens--659451--?
myristoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosis--659493--?
octadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoeicosanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosis--659493--?
octadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoeicosanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Brassica napus-synthase I and II486923--?
octanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486914--ir
octanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486918-486918r
octanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Homo sapiens--659451--?
octanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosis--659493--?
octanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Synechocystis sp.--486936--?
palmitoyl-[acyl-carrier protein] + malonyl-CoA3-oxostearoyl-[acyl-carrier protein] + CO2 + CoA
show the reaction diagram
Allium ampeloprasum--486935--?
palmitoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosis--659493--?
palmitoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Homo sapiens--659451--?
propionyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]beta-ketopentanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486914--ir
propionyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]beta-ketopentanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Streptomyces peucetius-absolutely specific for486934--?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486941-486941?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486943-486943?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486915-486915r
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486918-486918r
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Rattus norvegicus--486944-486944?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Euglena gracilis--285676-285676?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Hordeum vulgare--486925-486925?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea--285675-285675?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea--486925-486925?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea--486931-486931r
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Pisum sativum--285675-285675?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Petroselinum crispum--486921-486921?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Brassica napus--486923-486923-
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Brassica napus--486922-486922r
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Clostridium kluyveri--486863-486863?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Synechocystis sp.--486936-486936?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Synechocystis sp.--486940-486940r
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Brassica juncea--285675-285675?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Carthamus tinctorius--285669-285669?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Carthamus tinctorius, Cuphea lutea--285675-285675?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Staphylococcus aureusP99159-486946-486946ir
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Allium ampeloprasum--486935synthase II, parenchyma and lamina epidermis: palmitoyl-[acyl-carrier-protein] is the only product, sheath epidermis: acyl-[acyl-carrier-protein] up to C22 chain length486935?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Haemophilus influenzae-substrate specificity, overview486939-486939?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Bacillus subtilis-substrate specificity, overview486937-486937?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-substrate specificity, overview486916-486916-
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-substrate specificity, overview486863-486863?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-substrate specificity, overview486937-486937?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-substrate specificity, overview486939-486939?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-substrate specificity, overview486914-486914ir
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-substrate specificity, overview486917-486917r
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-substrate specificity, overview486919-486919r
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-substrate specificity, overview486920-486920?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-substrate specificity, overview486924-486924?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosisP63454substrate specificity, overview486942-486942?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Streptomyces glaucescens-substrate specificity, overview486933-486933?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Streptomyces glaucescens-substrate specificity, overview486938-486938?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Cuphea lanceolata-substrate specificity, overview486947-486947?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Streptococcus pneumoniaeP0A3C5substrate specificity, overview486939-486939?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Cuphea lanceolata-preference for medium-chain length [acyl-carrier-protein]-substrates, synthase IV486947-486947?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Streptomyces glaucescens-synthase III, broad specificity486933-486933?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Streptomyces glaucescens-synthase III, broad specificity486938-486938?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-not hexadecanoyl-[acyl-carrier-protein]486863-486863?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-not hexadecanoyl-[acyl-carrier-protein]486864-486864?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-specific for acyl-[acyl-carrier-protein] thioesters, not acyl-CoA or acyl pantetheine thioesters486863-486863?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-specific for acyl-[acyl-carrier-protein] thioesters, not acyl-CoA or acyl pantetheine thioesters486864-486864?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli, Brassica napus-fatty acid composition of Brassica napus wild-type and transgenic plants overexpressing the E. coli synthase III486932-486932?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosisP63454KasA and KasB, preference for long-chain acyl-[acyl-carrier-protein]s with at least 16 C-atoms486942-486942?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-not octodecanoyl-[acyl-carrier-protein], i.e stearoyl-[acyl-carrier-protein]486920-486920?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-not octodecanoyl-[acyl-carrier-protein], i.e stearoyl-[acyl-carrier-protein]486924-486924?
stearoyl-[acyl-carrier protein] + malonyl-CoA3-oxoeicosanoyl-[acyl-carrier protein] + CO2 + CoA
show the reaction diagram
Allium ampeloprasum-only in sheath epidermis486935--?
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486863, 486916--?
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea--486920---
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea--285675--?
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-poor substrate486917--r
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-synthase I486943--?
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-i.e. myristoyl-[acyl-carrier-protein], only synthase II486924--?
malonyl-[acyl-carrier protein] + palmitoyl-CoA? + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosis--659724--?
additional information?-Escherichia coli--486937, 486939---
additional information?-Escherichia coli-enzyme also catalyzes a malonyl-CoA-CO2 exchange reaction, overview: substrates and kinetics486917---
additional information?-Streptococcus pneumoniaeP0A3C5synthase III, FabH, has a preference for straight short-chain CoA primers486939---
additional information?-Escherichia coli-synthase I and II have nearly the same substrate specificity486919---
additional information?-Spinacia oleracea-synthase I is specific for short-chain fatty acid prolongation while synthase II is active in C18 formation from C16486924---
additional information?-Bacillus subtilis-synthase III isozymes also utilize iso- and anteiso-branched-chain acyl-CoA primers as substrates486937---
additional information?-Streptomyces glaucescens-malonyl-CoA-CO2 exchange reaction486933---
additional information?-Homo sapiens-important role in generation of the lipoic acid precursor octanoyl-acyl-carrier protein659451---
additional information?-Mycobacterium tuberculosis-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 protein659493---
additional information?-Arabidopsis thalianaQ8L3X9no substrate: acetyl-[acyl-carrier protein]659442---
additional information?-Homo sapiens-preference for acyl-[acyl-carrier protein] in decreasing order: C12, C10, C6, C8, C4, C2, C14, C16659451---
additional information?-Staphylococcus aureus-rank of activity in decreasing order: isobutyryl-CoA, hexanoyl-CoA, butyryl-CoA, isovaleryl-CoA, acetyl-CoA660466---
additional information?-Staphylococcus aureus-inhibition of FabH leads to loss of accumulation of acetoacetyl-ACP676903---
additional information?-Trypanosoma bruceiQ586W9the organism, with the unusual lipid metabolism of the trypanosome, uses a microsomal elongase pathway, ELO, for de novo fatty acid synthesis, a second FAS pathway with a type II synthase is localized to the mitochondrion and is essential for bloodstream and procyclic life cycle stages of the parasite, in vivo precursors of mitochondrial fatty acid synthesis, overview674882---
additional information?-Escherichia coli-enzyme active site structure of wild-type and mutants with or without bound C12 or C8, overview673576---
additional information?-Staphylococcus aureus-FabH produces C14 long-chain beta-ketoacyl-ACP676903---
additional information?-Homo sapiensQ9NWU1KAS catalyzes the C2 fatty acid elongation reaction using a Cys-His-His catalytic triad677030---
additional information?-Trypanosoma bruceiQ586W9octanoate, the precursor for lipoic acid synthesis, is also produced by the mitochondrial FAS674882---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)
COMMENTARY PRODUCTLITERATURE
(Product)
4-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxo-6-octadecenoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Coriandrum sativum-reaction is part of petroselinic acid biosynthesis, synthase IV486948--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli--486937--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-part of non-associated fatty acid synthase system of plants and prokaryotes486863, 486919, 486914, 486915--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-part of non-associated fatty acid synthase system of plants and prokaryotes486924--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Clostridium kluyveri-part of non-associated fatty acid synthase system of plants and prokaryotes486863--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-involved in biosynthesis of saturated fatty acids486914, 486915, 486917--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Spinacia oleracea-involved in biosynthesis of saturated fatty acids486924--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Brassica napus-involved in biosynthesis of saturated fatty acids486922--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Cuphea lanceolata-key enzyme for regulation of medium-chain fatty acid synthesis in seeds486947--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Staphylococcus aureusP99159initiation of fatty acid biosynthesis, part of fatty acid synthase II486946--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli, Brassica napus-involved in biosynthesis of unsaturated and saturated fatty acids486932--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Mycobacterium tuberculosisP63454part of fatty acid synthase system I and II, involved in cell wall mycolic acids biosynthesis, overview486942--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Bacillus subtilis-initiation of fatty acid biosynthesis with acetyl-CoA as a primer, overview substrate specificity486937--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli, Clostridium kluyveri-responsible for chain elongation during de novo fatty acid synthesis486863--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Escherichia coli-involved in biosynthesis of mono-unsaturated long-chain fatty acids486919--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Streptomyces glaucescens-initiation of both straight- and branched-chain fatty acid biosynthesis resulting in a wide variety of produced fatty acids in vivo486933, 486938--
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]acyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Plasmodium falciparum--674777--
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
Helianthus annuus-the endoplasmic reticulum enzyme is involved in synthesis of very long chain fatty acids674095--
cis-3-decenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]3-oxo-cis-5-dodecenoyl-[acyl-carrier protein] + acyl-carrier protein
show the reaction diagram
Escherichia coli-key step in the unsaturated fatty acid, UFA, synthesis pathway. FabB is negatively regulated by the FabR protein704553the product is not incorporated into the complex lipids of the bacterium-
additional information?-Homo sapiens-important role in generation of the lipoic acid precursor octanoyl-acyl-carrier protein659451--
additional information?-Staphylococcus aureus-inhibition of FabH leads to loss of accumulation of acetoacetyl-ACP676903--
additional information?-Trypanosoma bruceiQ586W9the organism, with the unusual lipid metabolism of the trypanosome, uses a microsomal elongase pathway, ELO, for de novo fatty acid synthesis, a second FAS pathway with a type II synthase is localized to the mitochondrion and is essential for bloodstream and procyclic life cycle stages of the parasite, in vivo precursors of mitochondrial fatty acid synthesis, overview674882--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Mg2+Streptococcus pneumoniae--659029

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
4-phenyl-5-phenylimino-[1,2,4]dithiazolidin-3-oneStaphylococcus aureusP99159i.e. HR19; strong, synthase III486946 2D-image
5-chloro-4-phenyl-[1,2]-dithiol-3-oneStaphylococcus aureusP99159complete inhibition at 0.01 nM, synthase III; i.e. HR12486946 2D-image
acetyl-CoAEscherichia coli--486914 2D-image
acyl-CoAEscherichia coli-at high concentrations486914 2D-image
arseniteSpinacia oleracea--285675 2D-image
arseniteSpinacia oleracea-weak at 1 mM486920 2D-image
arseniteSpinacia oleracea-synthase II and I486924 2D-image
arseniteSpinacia oleracea-synthase III486931 2D-image
Butyryl-CoAStreptomyces glaucescens-synthase III mutants C122Aand C122Q: inhibition of decarboxylation activity in presence of486938 2D-image
C75Rattus norvegicus-a synthetic inhibitor of fatty acid synthase, inhibits also the beta-ketoacyl synthase, not in simple first order rate reaction, C75 is a competitive, irreversible inhibitor of the overall reaction, the beta-ketoacyl synthase activity and the enoyl reductase activity substrates do not protect the thioesterase activity of rat liver FAS from inactivation by C75, but malonyl-CoA and acetyl-CoA protect the FAS beta-ketoacyl synthase reaction from inactivation by C75 in a competitive manner, overview661000 2D-image
ceruleninCarthamus tinctorius--285669 2D-image
ceruleninSpinacia oleracea-antibiotic, protection by hexanoyl-[acyl-carrier-protein], decanoyl-[acyl-carrier-protein], and tetradecanoyl-[acyl-carrier-protein]486920 2D-image
ceruleninBrassica napus-no inhibition486923 2D-image
ceruleninSpinacia oleracea--486924 2D-image
ceruleninAllium ampeloprasum-synthase II, moderate486935 2D-image
ceruleninSynechocystis sp.-12-carbon mycotoxin, irreversible inhibition, binding motif; at 0.05 mM: wild-type is completely inactivated, mutant I108F and A193M show only 10% reduced activity486936 2D-image
ceruleninEscherichia coli, Haemophilus influenzae--486939 2D-image
ceruleninStreptococcus pneumoniaeP0A3C5-486939 2D-image
ceruleninEscherichia coli-analysis of the binding mechanism, mimicks the condensation transition state; FabB: inhibition is irreversible486941 2D-image
ceruleninMycobacterium tuberculosisP63454Kas A and KasB486942 2D-image
ceruleninStaphylococcus aureusP99159weak, synthase III486946 2D-image
ceruleninCuphea lanceolata-synthase IV486947 2D-image
ceruleninCoriandrum sativum-strong486948 2D-image
ceruleninArabidopsis thaliana--658746, 659442 2D-image
ceruleninHomo sapiens-50% inhibition at 0.2 mM659451 2D-image
ceruleninRattus norvegicus-specific inhibition of the enzyme661000 2D-image
ceruleninPlasmodium falciparum-irreversible inhibition, IC50: 0.0158 mM674777 2D-image
ceruleninHomo sapiensQ9NWU1-677030 2D-image
iodoacetamideEscherichia coli-no inhibition of malonyl-[acyl-carrier-protein]-decarboxylation486863 2D-image
iodoacetamideEscherichia coli--486864 2D-image
iodoacetamideEscherichia coli-acyl-[acyl-carrier-protein]-derivatives, e.g. acetyl-[acyl-carrier-protein], hexanoyl-CoA, octanoyl-CoA, decanoyl-CoA protect486914, 486917 2D-image
iodoacetamideEscherichia coli-after incubation with 2-mercaptethanol486915 2D-image
iodoacetamideEscherichia coli-acyl-[acyl-carrier-protein]-derivatives, e.g. acetyl-[acyl-carrier-protein], hexanoyl-CoA, octanoyl-CoA, decanoyl-CoA protect; synthase I and II486919 2D-image
iodoacetamideRattus norvegicus-kinetics486944 2D-image
N-ethylmaleimideClostridium kluyveri, Escherichia coli-no inhibition of malonyl-[acyl-carrier-protein]-decarboxylation486863 2D-image
N-ethylmaleimideEscherichia coli--486864 2D-image
N-ethylmaleimideEscherichia coli-acyl-[acyl-carrier-protein]-derivatives protect486914 2D-image
N-ethylmaleimideEscherichia coli-after incubation with 2-mercaptoethanol486915 2D-image
N-ethylmaleimideSpinacia oleracea-5 mM486920, 486924 2D-image
N-ethylmaleimideSpinacia oleracea--486931 2D-image
p-chloromercuribenzoateSpinacia oleracea-complete inhibition at 1 mM486920, 486924 2D-image
platencinStaphylococcus aureus-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, purified FabH IC50: 0.016 mM, overview676903 2D-image
SB418011Escherichia coli, Haemophilus influenzae--486939 2D-image
SB418011Streptococcus pneumoniaeP0A3C5strong, synthase III486939 2D-image
thiolactomycinStreptomyces glaucescens-synthase III486933 2D-image
thiolactomycinEscherichia coli-synthase III486939 2D-image
thiolactomycinHaemophilus influenzae--486939 2D-image
thiolactomycinStreptococcus pneumoniaeP0A3C5synthase III; weak486939 2D-image
thiolactomycinEscherichia coli-analysis of the binding mechanism, mimics malonyl-[acyl-carrier-protein]; FabB: inhibition is reversible, competitive486941 2D-image
thiolactomycinMycobacterium tuberculosisP63454Kas A and KasB486942 2D-image
thiolactomycinStaphylococcus aureusP99159synthase III; weak486946 2D-image
thiolactomycinPlasmodium falciparum-competitive inhibition, IC50: 0.0236 mM674777 2D-image
UreaEscherichia coli-about 50% inhibition at 1 M, complete inactivation at 4 M486918 2D-image
[Acyl-carrier-protein]Escherichia coli-wild-type synthase I and mutants, not mutants C163S and K328A, overview486943 2D-image
isobutyryl-CoAStreptomyces glaucescens-synthase III mutants C122Aand C122Q: inhibition of decarboxylation activity in presence of486938 2D-image
additional informationHelianthus annuus-the enzyme shows strong substrate inhibition674095-
additional informationStaphylococcus aureus-in vivo inhibition assays, no inhibition by platensimycin676903-
additional informationHomo sapiensQ9NWU1inhibitor binding structure determination677030-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2-mercaptoethanolEscherichia coli-activation486863, 486864, 486914 2D-image
2-mercaptoethanolEscherichia coli-required in high concentration, 0.5 M486915 2D-image
2-mercaptoethanolEscherichia coli-required486918 2D-image
dithiothreitolEscherichia coli-activation486863 2D-image
dithiothreitolEscherichia coli-activation; can replace 2-mercaptoethanol486915 2D-image
dithiothreitolEscherichia coli-activation; required486916 2D-image
dithiothreitolEscherichia coli-required486918 2D-image
EDTAEscherichia coli-activation486863, 486916 2D-image
EDTAEscherichia coli-7 mM, stimulates486915 2D-image
phosphateEscherichia coli-activation, 0.2 M486864 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0024-acetyl-CoAStreptomyces glaucescens-synthase III486933 2D-image
0.0062-acetyl-CoAStaphylococcus aureusP99159synthase III486946 2D-image
0.0403-acetyl-CoAStreptococcus pneumoniaeP0A3C5synthase III486939 2D-image
0.019-acetyl-[acyl-carrier protein]Escherichia coli-pH 7.0486915 2D-image
0.031-acetyl-[acyl-carrier protein]Escherichia coli-synthase I486919 2D-image
0.04-acetyl-[acyl-carrier protein]Escherichia coli-acyl-carrier-protein, fatty acyl transfer between tetradecanoyl-CoA and acyl-carrier-protein486917 2D-image
0.04-acetyl-[acyl-carrier protein]Escherichia coli-synthase II486919 2D-image
0.05-acetyl-[acyl-carrier protein]Homo sapiens-pH 6.8, 37°C659451 2D-image
0.0039-butanoyl-[acyl-carrier protein]Homo sapiens-pH 6.8, 37°C659451 2D-image
0.00071-Butyryl-CoAStreptomyces glaucescens-synthase III486933 2D-image
0.0023-Butyryl-CoAStaphylococcus aureusP99159synthase III486946 2D-image
0.403-C10-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
0.196-C12-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
0.437-C14-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
0.211-C4-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
0.116-C6-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
0.198-C8-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
0.012-cis-3-decenoyl-[acyl-carrier protein]Escherichia coli-synthase I486919 2D-image
0.014-cis-3-decenoyl-[acyl-carrier protein]Escherichia coli-synthase II486919 2D-image
0.017-cis-9-hexadecenoyl-[acyl-carrier protein]Escherichia coli-synthase II486919 2D-image
0.138-cis-9-hexadecenoyl-[acyl-carrier protein]Escherichia coli-synthase I486919 2D-image
0.0018-decanoyl-[acyl-carrier protein]Homo sapiens-pH 6.8, 37°C659451 2D-image
0.0031-decanoyl-[acyl-carrier protein]Cuphea lanceolata-synthase IV486947 2D-image
0.0133-decanoyl-[acyl-carrier protein]Spinacia oleracea-synthase II486924 2D-image
0.0023-dodecanoyl-[acyl-carrier protein]Mycobacterium tuberculosis-pH 7.0, 37°C659493 2D-image
0.0095-dodecanoyl-[acyl-carrier protein]Homo sapiens-pH 6.8, 37°C659451 2D-image
0.002-eicosanoyl-[acyl-carrier protein]Mycobacterium tuberculosisP63454isozyme Kas B486942 2D-image
0.0025-eicosanoyl-[acyl-carrier protein]Mycobacterium tuberculosisP63454isozyme Kas A486942 2D-image
0.0019-hexanoyl-[acyl-carrier protein]Homo sapiens-pH 6.8, 37°C659451 2D-image
0.0075-hexanoyl-[acyl-carrier protein]Spinacia oleracea--486920 2D-image
0.00032-isobutyryl-CoAStaphylococcus aureusP99159synthase III486946 2D-image
0.00041-isobutyryl-CoAStreptomyces glaucescens-synthase III486933 2D-image
0.004-malonyl-CoASpinacia oleracea-in presence of [acyl-carrier-protein]486920 2D-image
0.0055-malonyl-CoASpinacia oleracea--486924 2D-image
0.016-malonyl-CoASpinacia oleracea-without [acyl-carrier-protein]486920 2D-image
0.0037-malonyl-[acyl-carrier protein]Streptomyces glaucescens-synthase III486933 2D-image
0.0135-malonyl-[acyl-carrier protein]Mycobacterium tuberculosisP63454isozymes Kas A and KasB; isozymes Kas A and KasB486942 2D-image
0.0186-malonyl-[acyl-carrier protein]Streptococcus pneumoniaeP0A3C5synthase III486939 2D-image
0.0508-myristoyl-[acyl-carrier protein]Homo sapiens-pH 6.8, 37°C659451 2D-image
0.0109-octanoyl-[acyl-carrier protein]Homo sapiens-pH 6.8, 37°C659451 2D-image
0.0014-Palmitoyl-[acyl-carrier protein]Mycobacterium tuberculosisP63454isozyme Kas B486942 2D-image
0.0032-Palmitoyl-[acyl-carrier protein]Mycobacterium tuberculosisP63454isozyme Kas A486942 2D-image
0.0036-Palmitoyl-[acyl-carrier protein]Spinacia oleracea-synthase II486924 2D-image
0.0091-tetradecanoyl-[acyl-carrier protein]Spinacia oleracea--486920 2D-image
0.0139-tetradecanoyl-[acyl-carrier protein]Spinacia oleracea-synthase II486924 2D-image
0.025-malonyl-[acyl-carrier protein]Escherichia coli-pH 7.0486915 2D-image
additional information-additional informationEscherichia coli--486863, 486864-
additional information-additional informationEscherichia coli-kinetic data of synthase I and II at different temperatures with various substrates486916-
additional information-additional informationSpinacia oleracea--486920-
additional information-additional informationRattus norvegicus-mutants486944-
additional information-additional informationPlasmodium falciparum-kinetics674777-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
91.2-butanoyl-[acyl-carrier protein]Homo sapiens-pH 6.8, 37°C659451 2D-image
1.32-butyryl-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
3.07-C10-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
0.69-C12-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
1.28-C14-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
1.32-C4-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
0.96-C6-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
1.63-C8-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
3.07-decanoyl-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
551-decanoyl-[acyl-carrier protein]Homo sapiens-pH 6.8, 37°C659451 2D-image
0.69-dodecanoyl-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
303-dodecanoyl-[acyl-carrier protein]Homo sapiens-pH 6.8, 37°C659451 2D-image
0.01-eicosanoyl-[acyl-carrier protein]Mycobacterium tuberculosisP63454isozyme KasB486942 2D-image
0.075-eicosanoyl-[acyl-carrier protein]Mycobacterium tuberculosisP63454isozyme KasA486942 2D-image
0.96-hexanoyl-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
353-hexanoyl-[acyl-carrier protein]Homo sapiens-pH 6.8, 37°C659451 2D-image
0.0233-malonyl-[acyl-carrier protein]Mycobacterium tuberculosisP63454isozyme KasB486942 2D-image
0.08-malonyl-[acyl-carrier protein]Mycobacterium tuberculosisP63454isozyme KasA486942 2D-image
6-myristoyl-[acyl-carrier protein]Homo sapiens-pH 6.8, 37°C659451 2D-image
1.63-octanoyl-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
66-octanoyl-[acyl-carrier protein]Homo sapiens-pH 6.8, 37°C659451 2D-image
0.0267-Palmitoyl-[acyl-carrier protein]Mycobacterium tuberculosisP63454isozyme KasB486942 2D-image
0.0883-Palmitoyl-[acyl-carrier protein]Mycobacterium tuberculosisP63454isozyme KasA486942 2D-image
1.28-tetradecanoyl-[acyl-carrier protein]Plasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.01-thiolactomycinPlasmodium falciparum-pH 7.5, 37°C, recombinant enzyme674777 2D-image
16-C75Rattus norvegicus-pH 7.0, 22°C, inactivation of the whole reaction of FAS661000 2D-image
additional information-additional informationRattus norvegicus-inhibition kinetics661000-

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0158-ceruleninPlasmodium falciparum-irreversible inhibition, IC50: 0.0158 mM674777 2D-image
0.016-platencinStaphylococcus aureus-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, purified FabH IC50: 0.016 mM, o676903 2D-image
0.0236-thiolactomycinPlasmodium falciparum-competitive inhibition, IC50: 0.0236 mM674777 2D-image

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
3.4e-06-Mycobacterium tuberculosisP63454substrate palmitoyl-CoA486942
6e-06-Mycobacterium tuberculosisP63454substrate palmitoyl-CoA486942
3.2e-05-Mycobacterium tuberculosisP63454substrate palmitoyl-[acyl-carrier-protein]486942
8.8e-05-Mycobacterium tuberculosisP63454substrate palmitoyl-[acyl-carrier-protein]486942
0.0017-Mycobacterium tuberculosis-substrate hexanoyl-[acyl-carrier protein], pH 7.0, 37°C659493
0.005-Streptococcus pneumoniaeP0A3C5synthase III486939
0.0055-Mycobacterium tuberculosis-substrate octanoyl-[acyl-carrier protein], pH 7.0, 37°C659493
0.0062-Mycobacterium tuberculosis-substrate decanoyl-[acyl-carrier protein], pH 7.0, 37°C659493
0.0072-Mycobacterium tuberculosis-substrate dodecanoyl-[acyl-carrier protein], pH 7.0, 37°C659493
0.0083-Spinacia oleracea-purified enzyme486920
0.009-Mycobacterium tuberculosis-substrate eicosanoyl-[acyl-carrier-protein], pH 7.0, 37°C659493
0.0093-Mycobacterium tuberculosis-substrate palmitoyl-[acyl-carrier protein], pH 7.0, 37°C659493
0.0095-Mycobacterium tuberculosis-substrate myristoyl-[acyl-carrier protein], pH 7.0, 37°C659493
0.0104-Mycobacterium tuberculosis-substrate octadecanoyl-[acyl-carrier-protein], pH 7.0, 37°C659493
0.105-Plasmodium falciparum-purified recombinant enzyme with substrate C6-[acyl-carrier-protein]674777
0.403-Escherichia coli-purified enzyme486914
0.8-Brassica napus-purified synthase I486922
3.22-Euglena gracilis--285676
3.81-Escherichia coli-purified enzyme486915
5.5-Escherichia coli-synthase I486916
6.3-Escherichia coli-synthase II486916
7-Spinacia oleracea-purified native enzyme486931
7.5-Escherichia coli-purified synthase II486919
8.04-Petroselinum crispum-partially purified enzyme486921
9-Escherichia coli-purified synthase I486919
9.7-Escherichia coli--486917
14-Escherichia coli--486863
additional information-Carthamus tinctorius, Cuphea lutea, Pisum sativum-fatty acid synthase activity, malonyl-CoA incorporation285675
additional information-Spinacia oleracea--285675
additional information-Brassica napus--486922, 486923
additional information-Spinacia oleracea--486924
additional information-Spinacia oleracea-comparison of activity, recombinant and native enzyme486931
additional information-Brassica napus, Escherichia coli-wild-type and transgenic Brassica napus plants, expressing the E. coli synthase III486932
additional information-Bacillus subtilis, Escherichia coli--486937
additional information-Rattus norvegicus-mutants486944
additional information-Arabidopsis thalianaQ8L3X9enzyme from fresh extract synthesizes prominent amounts of C14 and C16 acyl chains. After storage at -20°C for one or several weeks, enzyme synthesizes predominantly C8 acyl chains659442
additional information-Escherichia coli-transfer of [3H]myristate from ACP to wild-type and Lys328 mutant KAS I673576
additional information-Plasmodium falciparum--674777
additional information-Trypanosoma bruceiQ586W9-674882
additional information-Staphylococcus aureus-development of an elongation assay with FabF, EC 2.3.1.179, and FabH676903

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
5.56.1Escherichia coli-synthase II486919
67.5Helianthus annuus--674095
6.3-Brassica napus--486923
6.67.7Streptomyces glaucescens-synthase III486933
6.8-Mycobacterium tuberculosisP63454isozyme KasA, HEPES buffer486942
6.8-Escherichia coli-assay at486943
6.8-Escherichia coli-decarboxylation assay at, inactive at pH 4.0-5.0673576
77.8Escherichia coli--486863, 486915
7-Escherichia coli-assay at486914
7-Streptomyces glaucescens-assay at486933
7-Bacillus subtilis, Escherichia coli-assay at486937
7-Mycobacterium tuberculosisP63454isozyme KasB, phosphate buffer486942
7-Rattus norvegicus-assay at661000
7-Staphylococcus aureus-assay at676903
7.2-Escherichia coli-synthase I486919
7.2-Staphylococcus aureusP99159synthase III486946
7.5-Coriandrum sativum-assay at486948
7.5-Plasmodium falciparum-assay at674777
7.5-Trypanosoma bruceiQ586W9assay at674882
8-Allium ampeloprasum-assay at486935
8.18.5Spinacia oleracea--486924

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.27.6Escherichia coli-synthase II, about half-maximal activity at pH 5.2 and pH 7.6486919
5.67.2Brassica napus-synthase II, about half-maximal activity at pH 5.6 and pH 7.2486923
5.88Staphylococcus aureusP99159synthase III486946
5.96.8Brassica napus-synthase I, about half-maximal activity at pH 5.9 and pH 6.8486923
68.2Spinacia oleracea--486920
6.38Escherichia coli-synthase I, about half-maximal activity at pH 6.3 and pH 8.0486919
6.58Escherichia coli--486863
6.58Escherichia coli-sharp drop in activity below pH 6.5 and above pH 8.0486915
6.89.1Spinacia oleracea--486924

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
20-Escherichia coli-assay at486943
22-Rattus norvegicus-assay at room temperature661000
22-Escherichia coli-assay at room temperature673576
25-Escherichia coli-assay at486914, 486915
25-Spinacia oleracea-assay at486920
27-Escherichia coli-assay at486916
30-Escherichia coli-assay at486864
30-Petroselinum crispum-assay at486921
30-Streptomyces glaucescens-assay at486933
30-Staphylococcus aureus-assay at676903
35-Euglena gracilis-assay at285676
37-Escherichia coli-assay at486916, 486917
37-Spinacia oleracea-assay at486920
37-Brassica napus-assay at486923
37-Bacillus subtilis, Escherichia coli-assay at486937
37-Mycobacterium tuberculosisP63454; 486942
37-Plasmodium falciparum-assay at674777
37-Trypanosoma bruceiQ586W9assay at674882

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
3042Mycobacterium tuberculosisP6345430-50% activity at 30 and 42°C; 30-50% activity at 30 and 42°C486942

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
brainHomo sapiens-low level659451Manually annotated by BRENDA team
cell suspension culturePetroselinum crispum--486921Manually annotated by BRENDA team
epidermisAllium ampeloprasum-sheath and lamina, and underlying parenchyma486935Manually annotated by BRENDA team
heartHomo sapiens-most abundant659451Manually annotated by BRENDA team
kernelHelianthus annuus--674095Manually annotated by BRENDA team
kidneyHomo sapiens--659451Manually annotated by BRENDA team
leafSpinacia oleracea--285675, 486920, 486924, 486925, 486931Manually annotated by BRENDA team
leafBrassica juncea, Carthamus tinctorius, Cuphea lutea, Pisum sativum--285675Manually annotated by BRENDA team
leafHordeum vulgare--486925Manually annotated by BRENDA team
leafAllium ampeloprasum--486935Manually annotated by BRENDA team
liverHomo sapiens--659451Manually annotated by BRENDA team
lungHomo sapiens-low level659451Manually annotated by BRENDA team
placentaHomo sapiens-low level659451Manually annotated by BRENDA team
seedCarthamus tinctorius-germinating285669, 285675Manually annotated by BRENDA team
seedBrassica juncea, Spinacia oleracea-germinating285675Manually annotated by BRENDA team
seedBrassica napus-germinating486922, 486923Manually annotated by BRENDA team
seedCuphea lanceolata-embryo486947Manually annotated by BRENDA team
seedCoriandrum sativum-germinating; specific isoform486948Manually annotated by BRENDA team
skeletal muscleHomo sapiens-most abundant659451Manually annotated by BRENDA team
spleenHomo sapiens-low level659451Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
chloroplastEuglena gracilis--9507285676Manually annotated by BRENDA team
chloroplastHordeum vulgare, Spinacia oleracea-stroma9507486925Manually annotated by BRENDA team
chloroplastCoriandrum sativum--9507486948Manually annotated by BRENDA team
cytosolEscherichia coli--5829486864Manually annotated by BRENDA team
endoplasmic reticulum membraneHelianthus annuus--5789674095Manually annotated by BRENDA team
microsomeHelianthus annuus---674095Manually annotated by BRENDA team
microsomeTrypanosoma bruceiQ586W9enzyme in the fatty acid synthase complex-674882Manually annotated by BRENDA team
mitochondrionArabidopsis thalianaQ8L3X9-5739659442Manually annotated by BRENDA team
mitochondrionHomo sapiens--5739659451Manually annotated by BRENDA team
mitochondrionTrypanosoma bruceiQ586W9enzyme in the elongase complex5739674882Manually annotated by BRENDA team
mitochondrionHomo sapiensQ9NWU1beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase5739677030Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
2ebd, downloadSCOP (2ebd)CATH (2ebd)Aquifex aeolicus (strain VF5)
1w0i, downloadSCOP (1w0i)CATH (1w0i)Arabidopsis thaliana
2ix4, downloadSCOP (2ix4)CATH (2ix4)Arabidopsis thaliana
3lrf, downloadSCOP (3lrf)CATH (3lrf)Brucella abortus (strain 2308)
3u0e, downloadSCOP (3u0e)CATH (3u0e)Brucella abortus (strain 2308)
3u0f, downloadSCOP (3u0f)CATH (3u0f)Brucella abortus (strain 2308)
3kzu, downloadSCOP (3kzu)CATH (3kzu)Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
4efi, downloadSCOP (4efi)CATH (4efi)Burkholderia xenovorans (strain LB400)
1b3n, downloadSCOP (1b3n)CATH (1b3n)Escherichia coli (strain K12)
1dd8, downloadSCOP (1dd8)CATH (1dd8)Escherichia coli (strain K12)
1ebl, downloadSCOP (1ebl)CATH (1ebl)Escherichia coli (strain K12)
1ek4, downloadSCOP (1ek4)CATH (1ek4)Escherichia coli (strain K12)
1f91, downloadSCOP (1f91)CATH (1f91)Escherichia coli (strain K12)
1fj4, downloadSCOP (1fj4)CATH (1fj4)Escherichia coli (strain K12)
1fj8, downloadSCOP (1fj8)CATH (1fj8)Escherichia coli (strain K12)
1g5x, downloadSCOP (1g5x)CATH (1g5x)Escherichia coli (strain K12)
1h4f, downloadSCOP (1h4f)CATH (1h4f)Escherichia coli (strain K12)
1hn9, downloadSCOP (1hn9)CATH (1hn9)Escherichia coli (strain K12)
1hnd, downloadSCOP (1hnd)CATH (1hnd)Escherichia coli (strain K12)
1hnh, downloadSCOP (1hnh)CATH (1hnh)Escherichia coli (strain K12)
1hnj, downloadSCOP (1hnj)CATH (1hnj)Escherichia coli (strain K12)
1hnk, downloadSCOP (1hnk)CATH (1hnk)Escherichia coli (strain K12)
1kas, downloadSCOP (1kas)CATH (1kas)Escherichia coli (strain K12)
1mzs, downloadSCOP (1mzs)CATH (1mzs)Escherichia coli (strain K12)
2aq7, downloadSCOP (2aq7)CATH (2aq7)Escherichia coli (strain K12)
2aqb, downloadSCOP (2aqb)CATH (2aqb)Escherichia coli (strain K12)
2buh, downloadSCOP (2buh)CATH (2buh)Escherichia coli (strain K12)
2bui, downloadSCOP (2bui)CATH (2bui)Escherichia coli (strain K12)
2byw, downloadSCOP (2byw)CATH (2byw)Escherichia coli (strain K12)
2byx, downloadSCOP (2byx)CATH (2byx)Escherichia coli (strain K12)
2byy, downloadSCOP (2byy)CATH (2byy)Escherichia coli (strain K12)
2byz, downloadSCOP (2byz)CATH (2byz)Escherichia coli (strain K12)
2bz3, downloadSCOP (2bz3)CATH (2bz3)Escherichia coli (strain K12)
2bz4, downloadSCOP (2bz4)CATH (2bz4)Escherichia coli (strain K12)
2eft, downloadSCOP (2eft)CATH (2eft)Escherichia coli (strain K12)
2gfv, downloadSCOP (2gfv)CATH (2gfv)Escherichia coli (strain K12)
2gfw, downloadSCOP (2gfw)CATH (2gfw)Escherichia coli (strain K12)
2gfx, downloadSCOP (2gfx)CATH (2gfx)Escherichia coli (strain K12)
2gfy, downloadSCOP (2gfy)CATH (2gfy)Escherichia coli (strain K12)
2gyo, downloadSCOP (2gyo)CATH (2gyo)Escherichia coli (strain K12)
2vb7, downloadSCOP (2vb7)CATH (2vb7)Escherichia coli (strain K12)
2vb8, downloadSCOP (2vb8)CATH (2vb8)Escherichia coli (strain K12)
2vb9, downloadSCOP (2vb9)CATH (2vb9)Escherichia coli (strain K12)
2vba, downloadSCOP (2vba)CATH (2vba)Escherichia coli (strain K12)
1h4f, downloadSCOP (1h4f)CATH (1h4f)Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
2buh, downloadSCOP (2buh)CATH (2buh)Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
2bui, downloadSCOP (2bui)CATH (2bui)Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
2byw, downloadSCOP (2byw)CATH (2byw)Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
2byx, downloadSCOP (2byx)CATH (2byx)Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
2byy, downloadSCOP (2byy)CATH (2byy)Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
2byz, downloadSCOP (2byz)CATH (2byz)Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
2bz3, downloadSCOP (2bz3)CATH (2bz3)Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
2bz4, downloadSCOP (2bz4)CATH (2bz4)Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
2c9h, downloadSCOP (2c9h)CATH (2c9h)Homo sapiens
2iwy, downloadSCOP (2iwy)CATH (2iwy)Homo sapiens
2iwz, downloadSCOP (2iwz)CATH (2iwz)Homo sapiens
3tjm, downloadSCOP (3tjm)CATH (3tjm)Homo sapiens
1hzp, downloadSCOP (1hzp)CATH (1hzp)Mycobacterium tuberculosis
1m1m, downloadSCOP (1m1m)CATH (1m1m)Mycobacterium tuberculosis
1u6e, downloadSCOP (1u6e)CATH (1u6e)Mycobacterium tuberculosis
1u6s, downloadSCOP (1u6s)CATH (1u6s)Mycobacterium tuberculosis
2ahb, downloadSCOP (2ahb)CATH (2ahb)Mycobacterium tuberculosis
2aj9, downloadSCOP (2aj9)CATH (2aj9)Mycobacterium tuberculosis
2gp6, downloadSCOP (2gp6)CATH (2gp6)Mycobacterium tuberculosis
2qnx, downloadSCOP (2qnx)CATH (2qnx)Mycobacterium tuberculosis
2qny, downloadSCOP (2qny)CATH (2qny)Mycobacterium tuberculosis
2qnz, downloadSCOP (2qnz)CATH (2qnz)Mycobacterium tuberculosis
2qo0, downloadSCOP (2qo0)CATH (2qo0)Mycobacterium tuberculosis
2qo1, downloadSCOP (2qo1)CATH (2qo1)Mycobacterium tuberculosis
2qx1, downloadSCOP (2qx1)CATH (2qx1)Mycobacterium tuberculosis
2wgd, downloadSCOP (2wgd)CATH (2wgd)Mycobacterium tuberculosis
2wge, downloadSCOP (2wge)CATH (2wge)Mycobacterium tuberculosis
2wgf, downloadSCOP (2wgf)CATH (2wgf)Mycobacterium tuberculosis
2wgg, downloadSCOP (2wgg)CATH (2wgg)Mycobacterium tuberculosis
3led, downloadSCOP (3led)CATH (3led)Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
2vkz, downloadSCOP (2vkz)CATH (2vkz)Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
2was, downloadSCOP (2was)CATH (2was)Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
2wat, downloadSCOP (2wat)CATH (2wat)Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
1zow, downloadSCOP (1zow)CATH (1zow)Staphylococcus aureus (strain MW2)
2gqd, downloadSCOP (2gqd)CATH (2gqd)Staphylococcus aureus (strain MW2)
1ox0, downloadSCOP (1ox0)CATH (1ox0)Streptococcus pneumoniae
1oxh, downloadSCOP (1oxh)CATH (1oxh)Streptococcus pneumoniae
2alm, downloadSCOP (2alm)CATH (2alm)Streptococcus pneumoniae
2rjt, downloadSCOP (2rjt)CATH (2rjt)Streptococcus pneumoniae
1tqy, downloadSCOP (1tqy)CATH (1tqy)Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
1mzj, downloadSCOP (1mzj)CATH (1mzj)Streptomyces lividans
1e5m, downloadSCOP (1e5m)CATH (1e5m)Synechocystis sp. (strain PCC 6803 / Kazusa)
1ub7, downloadSCOP (1ub7)CATH (1ub7)Thermus thermophilus
3row, downloadSCOP (3row)CATH (3row)Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568)
3fk5, downloadSCOP (3fk5)CATH (3fk5)Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
38000-Streptomyces peucetius-synthase III-like polyketid synthase, gel filtration, amino acid sequence determination486934
56000-Spinacia oleracea-synthase I, gel filtration285675, 486920, 486924
57500-Spinacia oleracea-synthase II, gel filtration285675, 486924
60000-Streptococcus pneumoniaeP0A3C5synthase III, gel filtration486939
63000-Spinacia oleracea-synthase III, gel filtration486931
66000-Escherichia coli-equilibrium centrifugation486863
66000-Escherichia coli-synthase I, gel filtration486919
67600-Escherichia coli-gel filtration486914
67600-Staphylococcus aureusP99159gel filtration486946
70000-Petroselinum crispum-about, gel filtration486921
72000-Streptomyces glaucescens-recombinant enzyme, gel filtration486933
76000-Escherichia coli-synthase II, gel filtration486919
80000-Escherichia coli-synthase I, sedimentation equilibrium method486916
85000-Escherichia coli-synthase II, sedimentation equilibrium method486916
86700-Brassica napus-synthase I, gel filtration486922, 486923
87400-Brassica napus-synthase II, gel filtration486923
87800-Brassica napus-synthase II, gel filtration486922
90000-Hordeum vulgare, Spinacia oleracea-gel filtration486925
118000-Euglena gracilis-gel filtration285676
additional information-Escherichia coli-amino acid composition, synthase I and II486916
additional information-Bacillus subtilis, Escherichia coli-amino acid sequence alignment486937
additional information-Escherichia coli, Haemophilus influenzae-amino acid sequence alignment486939
additional information-Streptococcus pneumoniaeP0A3C5amino acid sequence alignment486939
additional information-Escherichia coli-synthase I mutants486943
additional information-Staphylococcus aureusP99159amino acid sequence alignment486946
additional information-Coriandrum sativum-amino acid sequence alignment486948

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Bacillus subtilis-x * 39800, FabH2, SDS-PAGE; x * 42700, FabH1, SDS-PAGE486937
?Arabidopsis thalianaQ8L3X9x * 47000, SDS-PAGE659442
?Homo sapiens-x * 45800, SDS-PAGE, recombinant protein without N-terminal targeting sequence, with His-tag659451
dimerEscherichia coli-2 * 35000, SDS-PAGE; 2 * 37000, gel filtration after 6 M guanidinium chloride treatment486863
dimerEscherichia coli-2 * 34000, SDS-PAGE486864
dimerEscherichia coli-2 * 43000-44000, synthase I, SDS-PAGE; 2 * 44000-45000, synthase II, SDS-PAGE486916
dimerBrassica napus-2 * 43000, SDS-PAGE486922, 486923
dimerHordeum vulgare-2 * 45000, SDS-PAGE; 2 * 46000, alpha2, synthase I, SDS-PAGE486925
dimerSpinacia oleracea-2 * 46000, SDS-PAGE486925
dimerSpinacia oleracea-2 * 40500, synthase III, SDS-PAGE486931
dimerStreptomyces glaucescens-2 * 37000, recombinant synthase III, SDS-PAGE486933
dimerSynechocystis sp.-crystal structure analysis of subunits486940
dimerStaphylococcus aureusP991592 * 37000, recombinant synthase III, SDS-PAGE486946
dimerArabidopsis thalianaQ8L3X9crystallization data658746
dimerHomo sapiensQ9NWU1secondary structure, a dimer with an alpha-beta-alpha-beta-alpha-thiolase fold capped by an alpha-helical region connecting the strands of the N-terminal beta-sheet, crystal structure analysis677030
monomerStreptomyces peucetius-1 * 38000, synthase III-like polyketid synthase, SDS-PAGE486934
additional informationEscherichia coli-vertebrates, yeast and Mycobacteria fatty acid synthetases contain all individual activities on one or two multifunctional polypeptide chains, plant, Escherichia coli and other prokaryotic fatty acid synthases are non-associated systems of individual enzymes486863, 486864
additional informationClostridium kluyveri-vertebrates, yeast and Mycobacteria fatty acid synthetases contain all individual activities on one or two multifunctional polypeptide chains, plant, Escherichia coli and other prokaryotic fatty acid synthases are non-associated systems of individual enzymes486863
additional informationEscherichia coli-synthase I mutants486943
additional informationEscherichia coliP0A953comparison of crystal structures of the active sites of Escherichia coli KAS I with human cytosolic acetoacetyl-CoA thiolase and bacterial thiolase, active sites with four highly conserved loop structures, overview659726
additional informationEscherichia coli-comparison of active sites in isoforms KAS I, KAS II and related enzymes660470
additional informationEscherichia coli-analysis of wild-type and mutant active sites with bound substrates at different pH, overview673576

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
proteolytic modificationArabidopsis thalianaQ8L3X920 amino acid mitochondrial targeting sequence659442
proteolytic modificationHomo sapiens-mitochondrial targeting sequence of 38 residues659451

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Arabidopsis thalianaQ8L3X9658746
-Escherichia coli-486863, 486864
comparison of crystal structures of the active sites of Escherichia coli KAS I with human cytosolic acetoacetyl-CoA thiolase and bacterial thiolase, overviewEscherichia coliP0A953659726
purified recombinant wild-type and mutant enzymes, free or bound to C8 and C12, respectively, X-ray diffraction structure determination and analysis at 1.8-2.4 A resolutionEscherichia coli-673576
structure analysis, three-dimensional model of enzyme complexed with inhibitors thiolactomycin and ceruleninEscherichia coli-486941
purified recombinant enzyme free or complexed with acyl-CoA, hanging drop vapour diffusion method, 0.002 ml of protein solution, containing 0.087 mg of protein with or without 4 mM hexanoyl-CoA, mixed with 0.002 ml of reservoir solution containing 24% w/v PEG 3350 and 0.2 M NH4Cl, 5-8 days at room temperature, rod-shaped single crystals, X-ray diffraction structure determination and analysis at 1.6 A resolution, structure modelingHomo sapiensQ9NWU1677030
in complex with lauroyl-CoAMycobacterium tuberculosis-659724
-Staphylococcus aureus-660466
-Streptococcus pneumoniae-659029
hanging drop vapour diffusion method, protein solution: 25 mM Tris-HCl, pH 8.0, 300 mM NaCl, 75 mM imidazole, reservoir solution: 0.085 M tri-sodium citrate, 0.17 M ammonium acetate, 22% w/v polyethylene glycol 4000, 15% v/v glycerol as cryo-protectant, 15% w/v 1,2,3-heptanetriol, x-ray structure analysis, three-dimensional modelSynechocystis sp.-486940

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
43-Escherichia coli-t1/2 synthase I: 18 min, t1/2 synthase II: 81 min486919
100-Escherichia coli-inactivation after 1 min486864

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
dithiothreitol stabilizesBrassica napus-486923
proteinase inhibitors stabilize during purificationBrassica napus-486923
Triton X-100 facilitates extraction from oil seedsBrassica napus-486923
unstable during purificationBrassica napus-486922
2-mercaptoethanol stabilizesEscherichia coli-486914
EDTA stabilizesEscherichia coli-486914
unstable during purificationEscherichia coli-486914
freezing and thawing inactivatesEuglena gracilis-285676
dithiothreitol stabilizesSpinacia oleracea-486931
glycerol stabilizesSpinacia oleracea-486931
Triton X-100 stabilizesSpinacia oleracea-486931

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
oxidation by formic acidEscherichia coli-486918

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
0°C, unstable in crude extracts lacking glycerol. Enzyme from fresh extract synthesizes prominent amounts of C14 and C16 acyl chains. After storage at -20°C for one or several weeks, enzyme synthesizes predominantly C8 acyl chainsArabidopsis thalianaQ8L3X9659442
-70° to -20°C, 90% loss of activity within 7 daysBrassica napus-486923
-20°C, 90% loss of activity within 1 yearEscherichia coli-486864
-20°C, at least 1 monthEscherichia coli-486864
-20°C, complete loss of activity in the presence of EDTA and 2-mercaptoethanolEscherichia coli-486914
-20°C, several monthsEscherichia coli-486915
-20°C, t1/2: 1 monthSpinacia oleracea-486920
-70°C, at least 1 monthSpinacia oleracea-486924
-80°C, several weeks in the presence of 20% v/v glycerol, 0.1% Triton X-100 and dithiothreitolSpinacia oleracea-486931

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
recombinant enzymeArabidopsis thalianaQ8L3X9659442
recombinant His-tagged proteins FabH1 and FabH2 from E. coliBacillus subtilis-486937
-Brassica napus-486923
synthases I and IIBrassica napus-486922
recombinant His-tagged seed-specific isoform from E. coliCoriandrum sativum-486948
recombinant His-tagged synthase IV from E. coliCuphea lanceolata-486947
-Escherichia coli-486863, 486864, 486914
isolation of hexanoyl-enzyme intermediate complexEscherichia coli-486918
partialEscherichia coli-486915
recombinant synthase I and mutants as His-tagged protein from E. coliEscherichia coli-486943
recombinant synthases I, i.e. FabA, II, i.e. FabB, and III, i.e.FabHEscherichia coli-486941
synthases I and IIEscherichia coli-486916, 486919
-Euglena gracilis-285676
recombinant His-tagged protein from E. coliHaemophilus influenzae-486939
native enzyme from kernel microsomes, solubilization and separation from KAS II by treatment with Triton X-100 and anion exchange chromatographyHelianthus annuus-674095
recombinant His-tagged enzyme from Escherichia coli strains XL-1 blue and M15Homo sapiensQ9NWU1677030
3 proteins alpha2, alpha,beta and beta2Hordeum vulgare-486925
recombinant His-tagged protein from E. coli; recombinant His-tagged protein from E. coliMycobacterium tuberculosisP63454486942
partialPetroselinum crispum-486921
recombinant soluble NusA-fusion protein FabBF from Escherichia coli strain BL21(DE3) by and gel filtrationPlasmodium falciparum-674777
native fatty acid synthase from liver in several steps including gel filtration as the last stepRattus norvegicus-661000
synthase ISpinacia oleracea-486920
synthase I; synthases IISpinacia oleracea-285675
synthase III, native wild-type and recombinant from E. coli E103SSpinacia oleracea-486931
synthases IISpinacia oleracea-486924
recombinant His-tagged synthase III from E. coliStaphylococcus aureusP99159486946
recombinant His-tagged synthase III from E. coliStreptococcus pneumoniaeP0A3C5486939
recombinant from E. coli as His-tagged proteinStreptomyces glaucescens-486933
recombinant from E. coli as His-tagged protein; wild-type and mutantsStreptomyces glaucescens-486938
synthase III-like polyketid synthase recombinant from Streptomyces lividansStreptomyces peucetius-486934
synthase II, recombinant from E. coliSynechocystis sp.-486936

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
complements KAS II defect in Escherichia coliArabidopsis thalianaQ8L3X9659442
expression of His-tagged FabH1 and FabH2 in Escherichia coli INValphaF'Bacillus subtilis-486937
construction of a cDNA library from developing seeds, DNA sequence analysis, expression as His-tagged enzyme in Escherichia coliCoriandrum sativum-486948
expression of His-tagged synthase IV in Escherichia coli BL21 (DE3)Cuphea lanceolata-486947
expression of synthase I and mutants as His-tagged proteins in Escherichia coliEscherichia coli-486943
synthase III, overexpression in Escherichia coli strain JM101, construction of binary expression vectors for transformation of Brassica napusEscherichia coli-486932
synthases I, II, and III, recombinant expressionEscherichia coli-486941
expression as His-tagged protein in Escherichia coliHaemophilus influenzae-486939
expression of the His-tagged enzyme in Escherichia coli strains XL-1 blue and M15Homo sapiensQ9NWU1677030
cDNA cloned into lambda2AB-IIHordeum vulgare-486925
expression of KasA and KasB as His-tagged protein in Escherichia coli; expression of KasA and KasB as His-tagged protein in Escherichia coliMycobacterium tuberculosisP63454486942
gene fabBF, DNA and amino acid sequence determination and analysis, sequence comparisons, expression of the soluble NusA-fusion protein FabBF in Escherichia coli strain BL21(DE3)Plasmodium falciparum-674777
synthase III, overexpression of His-tagged FabH in Escherichia coli BL21 (DE3)Staphylococcus aureusP99159486946
overexpression of His-tagged FabH in Escherichia coli BL21 (DE3)Streptococcus pneumoniaeP0A3C5486939
overexpression of fabH in Escherichia coli as His-tagged protein, synthase IIIStreptomyces glaucescens-486933
plasmid-based expression of synthase III wild-type and mutants in Streptomyces glaucescens and His-tagged in Escherichia coliStreptomyces glaucescens-486938
expression of synthase III-like polyketid synthase in Streptomyces lividansStreptomyces peucetius-486934
expression in Escherichia coliSynechocystis sp.-486940
expression of wild-type and mutant synthase II in Escherichia coliSynechocystis sp.-486936

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
C163AEscherichia coli-synthase I, site-directed mutagenesis, active site mutant, no activity, but decarboxylates malonyl-[acyl-carrier-protein]486943
C163SEscherichia coli-synthase I, site-directed mutagenesis, active site mutant, increased activity, decarboxylates malonyl-[acyl-carrier-protein]486943
D306AEscherichia coli-synthase I, site-directed mutagenesis, active site mutant, increased activity486943
E309AEscherichia coli-synthase I, site-directed mutagenesis, active site mutant, reduced activity486943
H298AEscherichia coli-synthase I, site-directed mutagenesis, active site mutant, reduced activity486943
H298EEscherichia coli-site-directed mutagenesis, the mutant is decarboxylation deficient, residual decarboxylase activity in the range of pH 6.0–8.0, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure673576
H298QEscherichia coli-site-directed mutagenesis, the mutant is completely decarboxylation deficient, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure673576
H333AEscherichia coli-synthase I, site-directed mutagenesis, active site mutant, increased activity486943
K328AEscherichia coli-synthase I, site-directed mutagenesis, active site mutant, reduced activity486943
K328AEscherichia coli-site-directed mutagenesis, the mutant is completely decarboxylation deficient, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure673576
K328EEscherichia coli-site-directed mutagenesis, the mutant is almost completely decarboxylation deficient673576
K328FEscherichia coli-site-directed mutagenesis, the mutant is completely decarboxylation deficient673576
K328HEscherichia coli-site-directed mutagenesis, the mutant is completely decarboxylation deficient673576
K328IEscherichia coli-site-directed mutagenesis, the mutant is almost completely decarboxylation deficient673576
R161AMycobacterium tuberculosis-69.6% of wild-type activity659493
R46AMycobacterium tuberculosis-7.3% of wild-type activity659493
R46A/R161AMycobacterium tuberculosis-0.3% of wild-type activity659493
T97FMycobacterium tuberculosis-no enzymic activity659493
W42AMycobacterium tuberculosis-21.5% of wild-type activity659493
W42A/R161AMycobacterium tuberculosis-0.2% of wild-type activity659493
C122AStreptomyces glaucescens-site-directed mutagenesis, 75% enhanced production of straight-chain fatty acids relative to branched-chain fatty acids compared to wild-type486938
C122QStreptomyces glaucescens-site-directed mutagenesis, 500% enhanced production of straight-chain fatty acids relative to branched-chain fatty acids compared to wild-type486938
C122SStreptomyces glaucescens-site-directed mutagenesis, enhanced production of straight-chain fatty acids relative to branched-chain fatty acids compared to wild-type486938
A193MSynechocystis sp.-site-directed mutagenesis, hydrophobic acyl-binding pocket is decreased in size by 2.55fold, 12fold reduced catalytic activity486936
additional informationBrassica napus-transformation of Brassica napus via Agrobacterium tumefaciens infection with binary vector overexpressing Escherichia coli fabH gene, targeted expression in cytoplasm and plastids is seed specific, modified fatty acid profile of seed oil486932
K328REscherichia coli-site-directed mutagenesis, the mutant is almost completely decarboxylation deficient, crystal structure determination with the free mutant enzyme, comparison to the wild-type enzyme structure673576
additional informationEscherichia coli-transformation of Brassica napus via Agrobacterium tumefaciens infection with binary vector overexpressing Escherichia coli fabH gene, targeted expression in cytoplasm and plastids is seed specific, modified fatty acid profile of seed oil486932
additional informationEscherichia coli-introduction of temperature-sensitive mutation in fabB into strain K27 by phage P1-mediated transduction using closely linked Tn10 insertion as selectable marker. A fabB mutant strain accumulates less cis-5-dodecenoic acid than the parental wild-type strain. The wild-type strain also accumulates 2.7fold more cis-7-tetradecenoate than the fabB(Ts) strain. The combination of null mutations in fadD and fabA or fabB is synthetically lethal even in the presence of oleic acid supplementation. A temperature-sensitive mutation is used rather than null mutations because a strain having fabB null mutation has an obligate requirement for an unsaturated fatty acid and FabD is required for uptake of the supplement704553
additional informationLactococcus lactis-in-frame deletion of enzyme active site region, mutant strain retains about 10% enzymic activity and fails to grow in the absence of supplementation with exogenous long-chain fatty acids. Mutant requires only long-chain unsaturated fatty acids, no saturated fatty acids659294
C161QRattus norvegicus-site-directed mutagenesis, active site Cys mutant, no condensation activity, but 377fold increased decarboxylation activity486944
additional informationRattus norvegicus-triple and quadruple mutants of fatty acid synthase complex including mutation sites in the beta-ketoacyl-[acyl-carrier-protein] synthase. e.g. H293A, H331A, K326A,S581A, kinetics, overview486944
I108FSynechocystis sp.-site-directed mutagenesis, hydrophobic acyl-binding pocket is decreased in size by 1.75fold, 38fold reduced catalytic activity towards octanoyl-[acyl-carrier-protein] compared to the activity towards hexanoy-[acyl-carrier-protein]486936
additional informationTrypanosoma bruceiQ586W9construction of FAS or ELO enzyme-deficient mutant strains by RNA interference or gene disruption, ACP depletion by RNAi or gene knockout reduces lipoic acid levels and drastically decreases protein lipoylation674882

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
drug developmentHomo sapiensQ9NWU1the enzyme is a target for antibacterial drugs677030
pharmacologyMycobacterium tuberculosisP63454involved in biosynthesis of cell wall mycolic acids, therefor target for discovery of anti-tuberculosis agents486942
drug developmentPlasmodium falciparum-the enzyme is a target for antibacterial drugs674777
drug developmentStaphylococcus aureus-the enzyme is a target for antibacterial drugs676903
pharmacologyStaphylococcus aureusP99159synthase III is a target for drug development against multi-drug resistant strains486946
medicineSynechocystis sp.-target for the development of drugs for the treatment of cancer and tuberculosis486936, 486940
nutritionSynechocystis sp.-target for the engineering of plant seed oils486936, 486940
pharmacologySynechocystis sp.-target for the development of drugs for the treatment of cancer and tuberculosis, involved in biosynthesis of precursors of pharmacological agents486936, 486940

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
Breast NeoplasmsTriclosan inhibits enoyl-reductase of type I fatty acid synthase in vitro and is cytotoxic to MCF-7 and SKBr-3 breast cancer cells. PubMed
Myocardial InfarctionCondensing enzyme levels in the serum after experimental myocardial infarction. PubMed
NeoplasmsApplication of a flexible synthesis of (5R)-thiolactomycin to develop new inhibitors of type I fatty acid synthase. PubMed
TuberculosisA novel interaction linking the FAS-II and phthiocerol dimycocerosate (PDIM) biosynthetic pathways. PubMed
TuberculosisAcetylene-based analogues of thiolactomycin, active against Mycobacterium tuberculosis mtFabH fatty acid condensing enzyme. PubMed
TuberculosisBiphenyl-based analogues of thiolactomycin, active against Mycobacterium tuberculosis mtFabH fatty acid condensing enzyme. PubMed
TuberculosisIdentification of 2-Aminothiazole-4-Carboxylate Derivatives Active against Mycobacterium tuberculosis H(37)R(v) and the beta-Ketoacyl-ACP Synthase mtFabH. PubMed
TuberculosisInhibition of a Mycobacterium tuberculosis beta-ketoacyl ACP synthase by isoniazid. PubMed
TuberculosisMycolic acid biosynthesis and enzymic characterization of the beta-ketoacyl-ACP synthase A-condensing enzyme from Mycobacterium tuberculosis. PubMed
TuberculosisPurification and biochemical characterization of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthases KasA and KasB. PubMed
TuberculosisX-ray crystal structure of Mycobacterium tuberculosis beta-ketoacyl acyl carrier protein synthase II (mtKasB). PubMed

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
285669Shimakata, T.; Stumpf, P.K.The procaryotic nature of the fatty acid synthetase of developing Carthamus tinctorius L. (Safflower) seedsArch. Biochem. Biophys.217144-1541982Carthamus tinctorius PubMed
285675Shimakata, T.; Stumpf, P.K.The purification and function of acetyl coenzyme A:acyl carrier protein transacylaseJ. Biol. Chem.2583592-35981983Brassica juncea, Carthamus tinctorius, Cuphea lutea, Pisum sativum, Spinacia oleracea PubMed
285676Hendren, R.W.; Bloch, K.Fatty acid synthetases from Euglena gracilis. Separation of component activities of the ACP-dependent fatty acid synthetase and partial purification of the beta-ketoacyl-ACP synthetaseJ. Biol. Chem.2551504-15081980Euglena gracilis PubMed
486863Vagelos, R.P.Acyl group transfer (acyl carrier protein)The Enzymes, 3rd Ed. (Boyer, P.D., ed.)8155-1991973Clostridium kluyveri, Escherichia coli-
486864Prescott, D.J.; Vagelos, P.R.Acyl carrier proteinAdv. Enzymol. Relat. Areas Mol. Biol.36269-3111972Escherichia coli PubMed
486914Toomey, R.E.; Wakil, S.J.Studies on the mechanism of fatty acid synthesis. XVI. Preparation and general properties of acyl-malonyl acyl carrier protein-condensing enzyme from Escherichia coliJ. Biol. Chem.2411159-11651966Escherichia coli PubMed
486915Alberts, A.W.; Majerus, P.W.; Vagelos, P.R.beta-Ketoacyl acyl carrier protein synthaseMethods Enzymol.1457-601969Escherichia coli-
486916Garwin, 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 coliJ. Biol. Chem.25511949-119561980Escherichia coli PubMed
486917Alberts, A.W.; Bell, R.M.; Vagelos, P.R.Acyl carrier protein. XV. Studies of beta-ketoacyl-acyl carrier protein synthetaseJ. Biol. Chem.2473190-31981972Escherichia coli PubMed
486918D'Agnolo, G.; Rosenfeld, I.S.; Vagelos, P.R.beta-Ketoacyl-acyl carrier protein synthetase. Characterization of the acyl-enzyme intermediateJ. Biol. Chem.2505283-52881975Escherichia coli PubMed
486919D'Agnolo, G.; Rosenfeld, I.S.; Vagelos, P.R.Multiple forms of beta-ketoacyl-acyl carrier protein synthetase in Escherichia coliJ. Biol. Chem.2505289-52941975Escherichia coli PubMed
486920Shimakata, T.; Stumpf, P.L.Purification and characterization of beta-ketoacyl-[acyl-carrier-protein] synthetase I from Spinacia oleracea leavesArch. Biochem. Biophys.22039-451983Spinacia oleracea PubMed
486921Schuz, R.; Ebel, J.; Hahlbrock, K.Partial purification of beta-ketoacyl-acyl acrrier protein synthase from a higher plantFEBS Lett.140207-2091982Petroselinum crispum-
486922MacKintosh, R.W.; Hardie, D.G.; Slabas, A.R.beta-Ketoacyl-acyl-carrier protein synthase from developing seeds of oilseed rape (Brassica napus)Biochem. Soc. Trans.17686-6871989Brassica napus-
486923MacKintosh, R.W.; Hardie, D.G.; Slabas, A.R.A new assay procedure to study the induction of beta-ketoacyl-ACP synthase I and II, and the complete purification of beta-ketoacyl-ACP synthase I from developing seeds of oilseed rape (Brassica napus)Biochim. Biophys. Acta1002114-1241989Brassica napus-
486924Shimakata, T.; Stumpf, P.L.Isolation and function of spinach leaf beta-ketoacyl-[acyl-carrier-protein] synthasesProc. Natl. Acad. Sci. USA795808-58121982Spinacia oleracea PubMed
486925Siggaard-Andersen, M.; Kauppinen, S.; von Wettstein-Knowles, P.Primary structure of a cerulenin-binding beta-ketoacyl-[acyl carrier protein] synthase from barley chloroplastsProc. Natl. Acad. Sci. USA884114-41181991Hordeum vulgare, Spinacia oleracea PubMed
486931Clough, R.; Matthis, A.L.; Barnum, S.R.; Jaworski, J.G.Purification and characterization of 3-ketoacyl-acyl carrier protein synthase III from spinach. A condensing enzyme utilizing acetyl-coenzyme A to initiate fatty acid synthesisJ. Biol. Chem.26720992-209981992Spinacia oleracea PubMed
486932Verwoert, I.I.G.S.; van der Linden, K.H.; Walsh, M.C.; Nijkamp, H.J.J.; Stuitje, A.R.Modification of Brassica napus seed oil by expression of the Escherichia coli fabH gene, encoding 3-ketoacyl-acyl carrier protein synthase IIIPlant Mol. Biol.27875-8861995Brassica napus, Escherichia coli PubMed
486933Han, L.; Lobo, S.; Reynolds, K.A.Characterization of beta-ketoacyl-acyl carrier protein synthase III from Streptomyces glaucescens and its role in initiation of fatty acid biosynthesisJ. Bacteriol.1804481-44861998Streptomyces glaucescens PubMed
486934Bao, W.; Sheldon, P.J.; Hutchinson, C.R.Purification and properties of the Streptomyces peucetius DpsC beta-ketoacyl:acyl carrier protein synthase III that specifies the propionate-starter unit for type II polyketide biosynthesisBiochemistry389752-97571999Streptomyces peucetius PubMed
486935Domergue, F.; Post-Beittenmiller, D.Biochemical characterization of 3-ketoacyl-acyl carrier protein synthase II from leek epidermisBiochem. Soc. Trans.28610-6132000Allium ampeloprasum PubMed
486936Val, D.; Banu, G.; Seshadri, K.; Lindqvist, Y.; Dehesh, K.Re-engineering ketoacyl synthase specificityStructure8565-5662000Synechocystis sp. PubMed
486937Choi, K.H.; Heath, R.J.; Rock, C.O.beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesisJ. Bacteriol.182365-3702000Bacillus subtilis, Escherichia coli PubMed
486938Smirnova, N.; Reynolds, K.A.Engineered fatty acid biosynthesis in Streptomyces by altered catalytic function of beta-ketoacyl-acyl carrier protein synthase IIIJ. Bacteriol.1832335-23422001Streptomyces glaucescens PubMed
486939Khandekar, S.S.; Gentry, D.R.; Van Aller, G.S.; Warren, P.; Xiang, H.; Silverman, C.; Doyle, M.L.; Chambers, P.A.; Konstantinidis, A.K.; Brandt, M.; Daines, R.A.; Lonsdale, J.T.Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae beta-ketoacyl-acyl carrier protein synthase III (FabH)J. Biol. Chem.27630024-300302001Escherichia coli, Haemophilus influenzae, Streptococcus pneumoniae PubMed
486940Moche, M.; Dehesh, K.; Edwards, P.; Lindqvist, Y.The crystal structure of beta-ketoacyl-acyl carrier protein synthase II from Synechocystis sp. at 1.54.ANG. resolution and its relationship to other condensing enzymesJ. Mol. Biol.305491-5032001Synechocystis sp. PubMed
486941Price, A.C.; Choi, K.H.; Heath, R.J.; Li, Z.; White, S.W.; Rock, C.O.Inhibition of beta-ketoacyl-acyl carrier protein synthases by thiolactomycin and cerulenin. Structure and mechanismJ. Biol. Chem.2766551-65592001Escherichia coli PubMed
486942Schaeffer, 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 KasBJ. Biol. Chem.27647029-470372001Mycobacterium tuberculosis PubMed
486943McGuire, K.A.; Siggaard-Andersen, M.; Bangera, M.G.; Olsen, J.G.; von Wettstein-Knowles, P.beta-Ketoacyl-[acyl carrier protein] synthase I of Escherichia coli: aspects of the condensation mechanism revealed by analyses of mutations in the active site pocketBiochemistry409836-98452001Escherichia coli PubMed
486944Witkowski, A.; Joshi, A.K.; Smith, S.Mechanism of the beta-ketoacyl synthase reaction catalyzed by the animal fatty acid synthaseBiochemistry4110877-108872002Rattus norvegicus PubMed
486946He, X.; Reynolds, K.A.Purification, characterization, and identification of novel inhibitors of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureusAntimicrob. Agents Chemother.461310-13182002Staphylococcus aureus PubMed
486947Schutt, B.S.; Abbadi, A.; Loddenkotter, B.; Brummel, M.; Spener, F.beta-Ketoacyl-acyl carrier protein synthase IV: a key enzyme for regulation of medium-chain fatty acid synthesis in Cuphea lanceolata seedsPlanta215847-8542002Cuphea lanceolata PubMed
486948Mekhedov, S.; Cahoon, E.B.; Ohlrogge, J.An unusual seed-specific 3-ketoacyl-ACP synthase associated with the biosynthesis of petroselinic acid in corianderPlant Mol. Biol.47507-5182001Coriandrum sativum PubMed
658746Olsen, J.G.; Rasmussen, A.V.; von Wettstein-Knowles, P.; Henriksen, A.Structure of the mitochondrial beta-ketoacyl-[acyl carrier protein] synthase from Arabidopsis and its role in fatty acid synthesisFEBS Lett.577170-1742004Arabidopsis thaliana PubMed
659029Price, 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 pneumoniaeJ. Bacteriol.1854136-41432003Streptococcus pneumoniae PubMed
659294Lai, C.Y.; Cronan, J.E.beta-Ketoacyl-acyl carrier protein synthase III (FabH) is essential for bacterial fatty acid synthesisJ. Biol. Chem.27851494-515032003Lactococcus lactis PubMed
659442Yasuno, R.; von Wettstein-Knowles, P.; Wada, H.Identification and molecular characterization of the beta-ketoacyl-[acyl carrier protein] synthase component of the Arabidopsis mitochondrial fatty acid synthaseJ. Biol. Chem.2798242-82512004Arabidopsis thaliana PubMed
659451Zhang, L.; Joshi, A.K.; Hofmann, J.; Schweizer, E.; Smith, S.Cloning, expression, and characterization of the human mitochondrial beta-ketoacyl synthase. Complementation of the yeast CEM1 knock-out strainJ. Biol. Chem.28012422-124292005Homo sapiens PubMed
659493Brown, 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 specificityJ. Biol. Chem.28032539-325472005Mycobacterium tuberculosis PubMed
659724Musayev, 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 AJ. Mol. Biol.3461313-13212005Mycobacterium tuberculosis PubMed
659726Kursula, P.; Sikkilae, H.; Fukao, T.; Kondo, N.; Wierenga, R.K.High resolution crystal structures of human cytosolic thiolase (CT): A comparison of the active sites of human CT, bacterial thiolase, and bacterial KAS IJ. Mol. Biol.347189-2012005Escherichia coli PubMed
660466Qiu, X.; Choudhry, A.E.; Janson, C.A.; Grooms, M.; Daines, R.A.; Lonsdale, J.T.; Khandekar, S.S.Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureusProtein Sci.142087-20942005Staphylococcus aureus PubMed
660470Dawe, J.H.; Porter, C.T.; Thornton, J.M.; Tabor, A.B.A template search reveals mechanistic similarities and differences in beta-ketoacyl synthases (KAS) and related enzymesProteins52427-4352003Escherichia coli PubMed
661000Rendina, A.R.; Cheng, D.Characterization of the inactivation of rat fatty acid synthase by C75: inhibition of partial reactions and protection by substratesBiochem. J.388895-9032005Rattus norvegicus PubMed
673576von Wettstein-Knowles, P.; Olsen, J.G.; McGuire, K.A.; Henriksen, A.Fatty acid synthesis. Role of active site histidines and lysine in Cys-His-His-type beta-ketoacyl-acyl carrier protein synthasesFEBS J.273695-7102006Escherichia coli PubMed
674095Salas, J.J.; Martinez-Force, E.; Garces, R.Very long chain fatty acid synthesis in sunflower kernelsJ. Agric. Food Chem.532710-27162005Helianthus annuus PubMed
674777Lack, G.; Homberger-Zizzari, E.; Folkers, G.; Scapozza, L.; Perozzo, R.Recombinant expression and biochemical characterization of the unique elongating beta-ketoacyl-acyl carrier protein synthase involved in fatty acid biosynthesis of Plasmodium falciparum using natural and artificial substratesJ. Biol. Chem.2819538-95462006Plasmodium falciparum PubMed
674882Stephens, J.L.; Lee, S.H.; Paul, K.S.; Englund, P.T.Mitochondrial fatty acid synthesis in Trypanosoma bruceiJ. Biol. Chem.2824427-44362007Trypanosoma brucei PubMed
676903Wang, J.; Kodali, S.; Lee, S.H.; Galgoci, A.; Painter, R.; Dorso, K.; Racine, F.; Motyl, M.; Hernandez, L.; Tinney, E.; Colletti, S.L.; Herath, K.; Cummings, R.; Salazar, O.; Gonzalez, I.; Basilio, A.; Vicente, F.; Genilloud, O.; Pelaez, F.; Jayasuriya, H.; Young, K.; Cully, D.F.; Singh, S.B.Discovery of platencin, a dual FabF and FabH inhibitor with in vivo antibiotic propertiesProc. Natl. Acad. Sci. USA1047612-76162007Staphylococcus aureus PubMed
677030Christensen, C.E.; Kragelund, B.B.; von Wettstein-Knowles, P.; Henriksen, A.Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthaseProtein Sci.16261-2722007Homo sapiens PubMed
704553Feng, Y.; Cronan, J.E.Escherichia coli unsaturated fatty acid synthesis: complex transcription of the fabA gene and in vivo identification of the essential reaction catalyzed by FabBJ. Biol. Chem.28429526-295352009Escherichia coli PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.41)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)