The enzyme from the soil bacterium Streptomyces sp. CL190 produces acetoacetyl-CoA to be used for mevalonate production via the mevalonate pathway.
Unlike the homologous EC 2.3.1.180 (beta-ketoacyl-[acyl-carrier-protein] synthase III), this enzyme does not accept malonyl-[acyl-carrier-protein] as a substrate.
The enzyme from the soil bacterium Streptomyces sp. CL190 produces acetoacetyl-CoA to be used for mevalonate production via the mevalonate pathway.
Unlike the homologous EC 2.3.1.180 (beta-ketoacyl-[acyl-carrier-protein] synthase III), this enzyme does not accept malonyl-[acyl-carrier-protein] as a substrate.
the recombinant enzyme catalyzes a single condensation of acetyl-CoA and malonyl-CoA to give acetoacetyl-CoA and CoA. Replacement of malonyl-CoA with malonyl-(acyl carrier protein) results in loss of the condensation activity. No acetoacetyl-CoA synthesizing activity detectable through the condensation of two molecules of acetyl-CoA
Cys115 in NphT7 functions as a key catalytic residue for the condensation reaction. His256 functions as a catalytic residue for the decarboxylation of the extender substrate malonyl-CoA. No acetoacetyl-CoA synthesizing activity is detected through the condensation of two molecules of acetyl-CoA
knockdown of AACS in primary neurons caused decreases in the expression of MAP-2 and NeuN, which are markers of neuronal differentiation, as well as synaptopodin, a marker of spine apparatus
acetoacetyl-CoA synthetase is a ketone body-utilizing enzyme for the synthesis of cholesterol and fatty acids, regulation of AACS during neurite outgrowth and physiological role of AACS in neurogenesis, overview. AACS is regulated by SREBP-2 and involved in the normal development of neurons
the acetoacetyl-coenzyme A synthesizing enzyme of the thiolase superfamily is involved in the mevalonate pathway. Acetoacetyl-CoA is the precursor of 3-hydroxy-3-methylglutaryl-CoA in the mevalonate pathway, which is essential for terpenoid backbone biosynthesis. Acetoacetyl-CoA is also the precursor of poly-3-hydroxybutyrate, a polymer belonging to the polyester class produced by microorganisms
polyhydroxyalkanoate synthase, PhaC, catalyzes generation of (R)-3-hydroxybutyrate monomers from two acetyl-CoA molecules, and further of short-chain length polyhydroxyalkanoates, PHAs. The malonyl-CoA availability is a limiting factor to synthesis of poly(3-hydroxybutyrate), P(3HB), thus acetoacetyl-CoA synthetase, which is controlling the malonyl-CoA pool, is an important enzyme for increasing the P(3HB) production
alterations in acety-CoA carboxylase activity to optimize the acetyl-CoA/malonyl-CoA ratio might be an effective way to increase poly(3-hydroxybutyrate) production via the AACS-catalyzed paythway
SREBP-2, a key transcription factor of cholesterol synthesis, interacts with the AACS promoter and is increased during neurite outgrowth, and knockdown of SREBP-2 down-regulates the mRNA levels of AACS in Neuro-2a cells
consumption of malonyl-CoA and an increase in acetyl-CoA. No formation of CoA or acetoacetyl-CoA. C115A mutant enzyme yields acetyl-CoA via its malonyl-CoA decarboxylation activity, presumably by the His256 and Asn286 residues, while it has lost its condensation activity
site-directed mutagenesis, the mutant cleaves malonyl-CoA into acetyl-CoA, but does not form CoA or acetoacetyl-CoA. C115A mutant enzyme yields acetyl-CoA via its malonyl-CoA decarboxylation activity, presumably by the His256 and Asn286 residues, while it has lost its condensation activity
site-directed mutagenesis, the mutant enzyme exhibits acetoacetyl-CoA synthesizing activity, but its specific activity is approximately 40fold lower than that of wild-type NphT7
this mutant enzyme exhibits detectable acetoacetyl-CoA synthesizing activity, but its specific is approximately 40fold lower than that of wild-type NphT7
heterologous expression of different nphT7 homologues for farnesene production. acetoacetyl-CoA synthase might increase the flux through the mevalonate pathway, effect of acetoacetyl-CoA synthase on growth as well as the production of farnesene, overview. While plasmid-based expression of nphT7 does not improve final farnesene titers, the construction of an alternative pathway, which exclusively relies on the malonyl-CoA bypass, was detrimental for growth and farnesene production. The overall functionality of the bypass is limited by the efficiency of acetoacetyl-CoA synthase. Gene nphT7 from Streptomyces glaucescens shows clearly higher efficiency compared to Streptomyces sp. strain CL190, overview
heterologous expression of different nphT7 homologues for farnesene production. acetoacetyl-CoA synthase might increase the flux through the mevalonate pathway, effect of acetoacetyl-CoA synthase on growth as well as the production of farnesene, overview. While plasmid-based expression of nphT7 does not improve final farnesene titers, the construction of an alternative pathway, which exclusively relies on the malonyl-CoA bypass, was detrimental for growth and farnesene production. The overall functionality of the bypass is limited by the efficiency of acetoacetyl-CoA synthase. Gene nphT7 from Streptomyces glaucescens shows clearly higher efficiency compared to Streptomyces sp. strain CL190, overview
engineering the production of polyhydroxyalkanoates (PHAs) into high biomass bioenergy crops has the potential to provide a sustainable supply of bioplastics and energy from a single plant feedstock. One of the major challenges in engineering C4 plants for the production of poly[(R)-3-hydroxybutyrate] (PHB) is the significantly lower level of polymer produced in the chloroplasts of mesophyll cells compared to bundle sheath cells, thereby limiting the full PHB yield potential of the plant. The access to substrate for PHB synthesis may limit polymer production in mesophyll cell chloroplasts. The use of an acetoacetyl-CoA synthase, that catalyses the conversion of acetyl-CoA and malonyl-CoA to acetoacetyl-CoA with the release of carbon dioxide, in place of a beta-ketothiolase, the first enzyme in the bacterial PHA pathway, enhances poly-3-hydroxybutyrate production in sugarcane mesophyll cells. The engineered cells shows increased production of PHB and increased polymer molecular weight. PhaA is the main contributor to low PHB yield in mesophyll cells. Phenotypes of transgenic sugarcane leafs, overview
heterologous expression of different nphT7 homologues for farnesene production. acetoacetyl-CoA synthase from might increase the flux through the mevalonate pathway, effect of acetoacetyl-CoA synthase on growth as well as the production of farnesene, overview. While plasmid-based expression of nphT7 does not improve final farnesene titers, the construction of an alternative pathway, which exclusively relies on the malonyl-CoA bypass, was detrimental for growth and farnesene production. The overall functionality of the bypass is limited by the efficiency of acetoacetyl-CoA synthase. Gene nphT7 from Streptomyces glaucescens shows clearly higher efficiency compared to Streptomyces sp. strain CL190, overview
co-expression of polyhydroxyalkanoate synthase, PhaC, from Ralstonia eutropha with acetoacetyl-CoA synthetase in Escherichia coli and Corynebacterium glutamicum leading to enhanced production of polyhydroxybutanoates, by cloning the AACS gene into the phaABC operon of Ralstonia eutropha. Overexpression of AACS leads to a great enhancement of the malonyl-CoA pool in Escherichia coli
gene nphT7, organized in the mevalonate pathway gene cluster, functional expression in Streptomyces albus, overexpression of N-terminally His8-tagged enzyme in Escherichia coli
gene nphT7, recombinant expression in Saccharomyces cerevisiae strain CEN, analysis of the effect of acetoacetyl-CoA synthase on growth as well as the production of farnesene and compares different homologues regarding their efficiency
recombinant expression of AACS in Corynebacterium glutamicum and Escherichia coli leads to aquired ability to form poly(3-hydroxybutyrate) in the transformed organisms by 19.7 wt% and 10.5 wt%, respectively, biosynthetic pathway, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
SREBP-2, a key transcription factor of cholesterol synthesis, interacts with the AACS promoter and is increased during neurite outgrowth, and knockdown of SREBP-2 down-regulates the mRNA levels of AACS in Neuro-2a cells
histological changes, decreased steroid hormone concentrations and decreased cholesterol supply are observed in nicotine-treated fetal adrenals. The expression of genes regulating ketone metabolic process decreases in nicotine-treated fetal adrenals. Acetoacetyl-CoA synthetase (AACS), the enzyme utilizing ketones for cholesterol supply, displays decreased expression and increased DNA methylation in the proximal promoter of AACS
nphT7 can be used to significantly increase the concentration of acetoacetyl-CoA in cells, eventually leading to the production of useful terpenoids and poly-3-hydroxybutyrate
usage of the enzyme for recombinant high-level production of poly(3-hydroxybutyrate), P(3HB), in Escherichia coli and Corynebacterium glutamicum. P(3HB) is the natural aliphatic polyester that can be processed into a wide variety of consumer products, including plastics, films and fibers
Matsumoto, K.; Yamada, M.; Leong, C.; Jo, S.; Kuzuyama, T.; Taguchi, S.
A new pathway for poly(3-hydroxybutyrate) production in Escherichia coli and Corynebacterium glutamicum by functional expression of a new acetoacetyl-coenzyme A synthase
DNA hypermethylation of acetoacetyl-CoA synthetase contributes to inhibited cholesterol supply and steroidogenesis in fetal rat adrenals under prenatal nicotine exposure