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3-Oxoacyl-(Acyl-Carrier-Protein) ReductaseTrimetazidineAcetyl-CoA C-Acyltransferase3-Oxoacyl-(Acyl-Carrier-Protein) SynthaseInterleukin-1betabeta 2-MicroglobulinReceptors, Adrenergic, betaIntegrin beta3Transforming Growth Factor betaIntegrin alpha5beta1Integrin beta4Integrin alpha6beta4Integrin beta Chainsbeta 2-Glycoprotein IIntegrin alpha4beta1Integrin alpha2beta1Receptors, Adrenergic, beta-2IntegrinsInterleukin-1Antigens, CD29Integrin alpha6beta1Receptors, Adrenergic, beta-1Integrin alpha1beta1Cells, CulturedCell LineGlycogen Synthase Kinase 3RNA, MessengerEstrogen Receptor betaTransforming Growth Factor beta1Base SequenceReceptors, Adrenergic, beta-3Signal TransductionCell AdhesionBeta RhythmAdrenergic beta-AgonistsFatty Acid Synthase, Type IIAcyl Carrier ProteinEncyclopedias as TopicFatty AcidsFatty Acid SynthasesAscomycotaPlant DiseasesRhizospherePlants, Genetically ModifiedAcetylesteraseBasidiomycotaCell Wall
ReductaseProteinThiolaseSynthase domainPutativeEnzymeFatty acidSubunitSpeciesEscherichiaPathwayCatalystAcetylDefectSimilarRegulatorTopicRoleSynthaseThiolase deficiencyDeficiencyHADHBDehydrogenasePolyunsaturated fattyStreptomycesFatty acidsChromosomeSubunitsPeroxisomalMoleculeMutationsCatalyzeFormationCofactors
Reductase2
  • β-Ketoacyl-(acyl carrier protein) reductase (FabG) catalyzes the key reductive reaction in the elongation cycle of fatty acid synthesis (FAS), which is a vital metabolic pathway in bacteria and a promising target for new antibiotic development. (rcsb.org)
  • 2014) A human fatty acid synthase inhibitor binds β-ketoacyl reductase in the keto-substrate site. (guidetopharmacology.org)
Protein9
  • In animals, fungi, and lower eukaryotes, Beta-ketoacyl-ACP synthases make up one of the catalytic domains of larger multifunctional proteins (Type I), whereas in most prokaryotes as well as in plastids and mitochondria, Beta-ketoacyl-ACP synthases are separate protein chains that usually form dimers (Type II). (wikipedia.org)
  • Beta-ketoacyl synthase contains two protein domains. (wikipedia.org)
  • Beta ketoacyl acyl carrier protein synthase II (KASII) from Synechocystis sp. (expasy.org)
  • The protein encoded by this gene is a bifunctional enzyme that is involved in the peroxisomal beta-oxidation pathway for fatty acids. (nih.gov)
  • Defects in this gene that affect the peroxisomal fatty acid beta-oxidation activity are a cause of D-bifunctional protein deficiency (DBPD). (nih.gov)
  • This gene encodes the beta subunit of the mitochondrial trifunctional protein, a catalyst of mitochondrial beta-oxidation of long chain fatty acids . (wikidoc.org)
  • The HADHB protein catalyzes the final step of beta-oxidation, in which 3-ketoacyl CoA is cleaved by the thiol group of another molecule of Coenzyme A . The thiol is inserted between C-2 and C-3, which yields an acetyl CoA molecule and an acyl CoA molecule, which is two carbons shorter. (wikidoc.org)
  • The genes of the alpha and beta subunits of the mitochondrial trifunctional protein are located adjacent to each other in the human genome in a head-to-head orientation. (wikidoc.org)
  • A mitochondrial protein consisting of four alpha-subunits and four beta-subunits. (bvsalud.org)
Thiolase4
  • Trifunctional enzyme subunit beta, mitochondrial (TP-beta) also known as 3-ketoacyl-CoA thiolase , acetyl-CoA acyltransferase , or beta-ketothiolase is an enzyme that in humans is encoded by the HADHB gene . (wikidoc.org)
  • Searching for up to 100 curated homologs for Pf1N1B4_5133 3-ketoacyl-CoA thiolase (EC 2.3.1.16) @ Acetyl-CoA acetyltransferase (EC 2.3.1.9) (394 a.a. (lbl.gov)
  • Acetyl-CoA acetyltransferase (EC 2.3.1.9) @ Beta-ketoadipyl CoA thiolase (EC 2.3.1. (lbl.gov)
  • Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase. (umbc.edu)
Synthase domain1
  • Certain experiments have also suggested the presence of "fatty acid transport tunnels" within the beta-ketoacyl-ACP synthase domain that lead to one of many "fatty acid cavities", which essentially acts as the active site. (wikipedia.org)
Putative3
  • SCO0127 putative multi-domain beta keto-acyl synthase 112932:119654 forward MW:235996 0009. (kitasato-u.ac.jp)
  • SCO0126 putative multi-domain beta keto-acyl synthase 106637:112885 forward MW:214716 0012. (kitasato-u.ac.jp)
  • SCO6457 putative beta-galactosidase 7142206:7146129 forward MW:145522 0027. (kitasato-u.ac.jp)
Enzyme6
  • In molecular biology, Beta-ketoacyl-ACP synthase EC 2.3.1.41, is an enzyme involved in fatty acid synthesis. (wikipedia.org)
  • Beta-ketoacyl-ACP synthase is a highly conserved enzyme that is found in almost all life on earth as a domain in fatty acid synthase (FAS). (wikipedia.org)
  • Residues from both domains contribute to substrate binding and catalysis In animals and in prokaryotes, beta-ketoacyl-ACP synthase is a domain on type I FAS, which is a large enzyme complex that has multiple domains to catalyze multiple different reactions. (wikipedia.org)
  • So far a relatively unexplored target is the cell wall enzyme β-ketoacyl-ACP-synthase "KasA", which plays a crucial role in maintaining the membrane impermeability and hence the cell ability to resist to With 9.6 million new cases and 1.5 million deaths in 2014, tuberculosis (TB) is alongside with AIDS the most deadly infection. (uni-wuerzburg.de)
  • So far a relatively unexplored target is the cell wall enzyme β-ketoacyl-ACP-synthase "KasA", which plays a crucial role in maintaining the membrane impermeability and hence the cell ability to resist to the immune response and drug therapy. (uni-wuerzburg.de)
  • Entry into the beta-oxidation cycle requires the action of acyl-CoA dehydrogenase, the first enzyme in the sequence, which removes electrons from the alpha-carbon and the beta-carbon, introducing a double bond. (medscape.com)
Fatty acid1
Subunit1
  • In synthase II, each subunit consists of a five-stranded beta pleated sheet surrounded by multiple alpha helices, shown in the image on the left. (wikipedia.org)
Species1
  • It typically uses malonyl-CoA as a carbon source to elongate ACP-bound acyl species, resulting in the formation of ACP-bound β-ketoacyl species such as acetoacetyl-ACP. (wikipedia.org)
Escherichia1
  • Beta-ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue. (genebiosystems.com)
Pathway2
  • The beta-oxidation cycle permits the cell to extract energy from the breakdown of fatty acids with linkage to an accessory pathway for the formation of acetoacetate. (medscape.com)
  • Beta-oxidation is a complex mitochondrial pathway that is dependent on the presence of adequate cytosolic carnitine and 2 mitochondrial membrane-bound enzymes: CPT I and CPT II. (medscape.com)
Catalyst1
  • It also acts as a catalyst for the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids. (nih.gov)
Acetyl3
  • Beta-ketoacyl-ACP synthase III, perhaps the most well known of this family of enzymes, catalyzes a Claisen condensation between acetyl CoA and malonyl ACP. (wikipedia.org)
  • Cleavage of the 3-keto compound at the now unstable alpha-beta carbon bond and transfer of another CoA moiety to the new fragment results in 2 products: acetyl-CoA, composed of the carbonyl and original alpha-carbon from the starting molecule, and a new fatty acyl-CoA that is 2 carbons shorter than the original molecule. (medscape.com)
  • Acetyl CoA is generated from fatty acids through repeated beta-oxidation cycles. (msdmanuals.com)
Defect1
  • This deficiency is the most common defect in the beta-oxidation cycle. (msdmanuals.com)
Similar1
  • The presence of similar ketoacyl synthases present in all living organisms point to a common ancestor. (wikipedia.org)
Regulator1
  • aEuro dime This information helps to avoid understaging also to result in satisfactory treatment method.Myostatin, part of the particular transforming development factor-beta superfamily, is often a effective damaging regulator regarding bone muscle growth and is also protected in many varieties, through rats for you to people. (jak1inhibitor.com)
Topic1
  • Beta-ketoacyl-synthase's mechanism is a topic of debate among chemists. (wikipedia.org)
Role1
  • In addition to its intrinsic importance in the use of alternative fuels, the process of beta-oxidation clearly illustrates the role of vitamin cofactors in metabolism. (medscape.com)
Synthase16
  • In molecular biology, Beta-ketoacyl-ACP synthase EC 2.3.1.41, is an enzyme involved in fatty acid synthesis. (wikipedia.org)
  • Beta-ketoacyl-ACP synthase is a highly conserved enzyme that is found in almost all life on earth as a domain in fatty acid synthase (FAS). (wikipedia.org)
  • Beta-ketoacyl-ACP synthase III, perhaps the most well known of this family of enzymes, catalyzes a Claisen condensation between acetyl CoA and malonyl ACP. (wikipedia.org)
  • Beta-ketoacyl synthase contains two protein domains. (wikipedia.org)
  • Residues from both domains contribute to substrate binding and catalysis In animals and in prokaryotes, beta-ketoacyl-ACP synthase is a domain on type I FAS, which is a large enzyme complex that has multiple domains to catalyze multiple different reactions. (wikipedia.org)
  • Further examination of beta-ketoacyl-ACP synthases I and II of E. coli revealed that both are homodimeric, but synthase II is slightly larger. (wikipedia.org)
  • In synthase II, each subunit consists of a five-stranded beta pleated sheet surrounded by multiple alpha helices, shown in the image on the left. (wikipedia.org)
  • Certain experiments have also suggested the presence of "fatty acid transport tunnels" within the beta-ketoacyl-ACP synthase domain that lead to one of many "fatty acid cavities", which essentially acts as the active site. (wikipedia.org)
  • The main function of beta-ketoacyl-ACP synthase is to produce fatty acids of various lengths for use by the organism. (wikipedia.org)
  • The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. (nih.gov)
  • The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. (nih.gov)
  • So far a relatively unexplored target is the cell wall enzyme β-ketoacyl-ACP-synthase "KasA", which plays a crucial role in maintaining the membrane impermeability and hence the cell ability to resist to With 9.6 million new cases and 1.5 million deaths in 2014, tuberculosis (TB) is alongside with AIDS the most deadly infection. (uni-wuerzburg.de)
  • So far a relatively unexplored target is the cell wall enzyme β-ketoacyl-ACP-synthase "KasA", which plays a crucial role in maintaining the membrane impermeability and hence the cell ability to resist to the immune response and drug therapy. (uni-wuerzburg.de)
  • Antifungal activity is via inhibition of 1,3-beta-glucan synthase production of BETA-GLUCANS. (lookformedical.com)
  • A ácido graxo sintase (en inglés Fatty acid synthase ou FAS ) é un encima que nos humanos está codificado no xene FASN [ 1 ] situado no cromosoma 17 e que intervén na síntese de ácidos graxos . (wikipedia.org)
  • The beta-ketoacyl-acyl carrier protein (ACP) synthase III encoded by mtfabH (mtFabH) links FAS-I and FAS-II, catalyzing the condensation of FAS-I-derived acyl-CoAs with malonyl-acyl carrier protein (ACP). (birmingham.ac.uk)
Thiolase deficiency2
  • Medium-chain ketoacyl-CoA thiolase deficiency is a disorder associated with vomiting, dehydration, metabolic acidosis, liver dysfunction, and rhabdomyolysis. (nih.gov)
  • The cause of medium-chain ketoacyl-CoA thiolase deficiency is unknown. (nih.gov)
Deficiency2
  • TFP deficiency is confirmed by the identification of deficiencies in all three TFP enzymatic activities (long-chain enoyl-CoA hydratase, long-chain 3-hydroxyacyl-CoA dehydrogenase, and long-chain 3-ketoacyl-CoA thiolase) in lymphocytes or skin fibroblasts. (nih.gov)
  • Schematic demonstrating mitochondrial fatty acid beta-oxidation and effects of long-chain acyl CoA dehydrogenase deficiency (LCHAD) deficiency. (medscape.com)
HADHB3
  • The HADHB gene encodes long-chain ketoacyl-CoA thiolase (LCTH) activity, whereas the HADHA gene contains the information for the long-chain enoyl-CoA hydratase and long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) functions. (nih.gov)
  • Four alpha subunits are produced from the HADHA gene, and four beta subunits are produced from the HADHB gene. (medlineplus.gov)
  • Protective effect of fish oil targeting hadhaa (3-ketoacyl-CoA thiolase, alpha subunit a and hadhb (3-ketoacyl-CoA thiolase, beta subunit) against high cholesterol diet (HCD) induced atherosclerosis on Zebrafish. (ifiscollections.org)
Dehydrogenase3
  • Entry into the beta-oxidation cycle requires the action of acyl-CoA dehydrogenase, the first enzyme in the sequence, which removes electrons from the alpha-carbon and the beta-carbon, introducing a double bond. (medscape.com)
  • TFP has three enzymatic activities - long-chain enoyl-CoA hydratase, long-chain 3-hydroxyacyl-CoA dehydrogenase, and long-chain 3-ketoacyl-CoA thiolase. (nih.gov)
  • Isoform 1: Mainly acts as a reductive enzyme that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. (nih.gov)
Polyunsaturated fatty1
  • The potential inhibitory effect of polyunsaturated fatty acids, particularly docosahexaenoic acid, on mitochondrial \beta -oxidation is discussed. (iospress.com)
Streptomyces1
  • Grandes complejos de enzimas constituidos por cierto número de componentes enzimáticos que se encuentran en STREPTOMYCES y biosintetizan MACRÓLIDOS y otros policétidos. (bvsalud.org)
Fatty acids4
  • The beta-oxidation cycle permits the cell to extract energy from the breakdown of fatty acids with linkage to an accessory pathway for the formation of acetoacetate. (medscape.com)
  • These alpha-alkyl, beta-hydroxy fatty acids are formed by the condensation of two fatty acids, a long meromycolic acid and a shorter C(24)-C(26) fatty acid. (birmingham.ac.uk)
  • Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids. (nih.gov)
  • Catalyzes the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids. (nih.gov)
Chromosome1
  • The genes for the alpha and beta subunits have been localized to chromosome 2. (medscape.com)
Subunits2
  • The beta subunits contain one of the enzymes, known as long-chain 3-keto-acyl-CoA thiolase. (medlineplus.gov)
  • The beta subunits contain the third enzyme. (nih.gov)
Peroxisomal2
  • It is pointed out that docosahexaenoic acid appears more effective as regards induction of peroxisomal \beta -oxidation. (iospress.com)
  • Regarding the substrate specificity of \beta -oxidation pathway, mitochondrial and peroxisomal \beta -oxidation rate of \alpha -18:3-CoA, relative to 16:0- and 18:2-CoAs, was higher irrespective of the substrate/albumin ratios in the assay mixture or dietary fat sources. (iospress.com)
Molecule1
  • Cleavage of the 3-keto compound at the now unstable alpha-beta carbon bond and transfer of another CoA moiety to the new fragment results in 2 products: acetyl-CoA, composed of the carbonyl and original alpha-carbon from the starting molecule, and a new fatty acyl-CoA that is 2 carbons shorter than the original molecule. (medscape.com)
Mutations1
  • These mutations change single amino acids used to make the beta subunit. (medlineplus.gov)
Catalyze1
  • Beta-ketoacyl-ACP synthases I and II only catalyze acyl-ACP reactions with malonyl ACP. (wikipedia.org)
Formation1
  • It typically uses malonyl-CoA as a carbon source to elongate ACP-bound acyl species, resulting in the formation of ACP-bound β-ketoacyl species such as acetoacetyl-ACP. (wikipedia.org)
Cofactors1
  • In addition to its intrinsic importance in the use of alternative fuels, the process of beta-oxidation clearly illustrates the role of vitamin cofactors in metabolism. (medscape.com)