|Related Categories||Biochemicals and Reagents, Cell Biology, Coenzyme A and Other Acyl Transfer Reagents, Cofactors, Core Bioreagents,|
Substrate for acetoacetyl-CoA thiolase EC 126.96.36.199; Role in the biosynthesis of nonactin.
Acetoacetyl coenzyme A (Acetoacetyl-CoA) may be used as a substrate for a number of enzymes including; acetoacetyl-CoA thiolase (EC 2.3.1) which produces acetyl-CoA in reverse condensation reaction and (3-Hydroxy-3-methylglutar
Tandem Mass Spectrometry data independently generated by Scripps Center for Metabolomics is available to view or download in PDF. A1625.pdf Tested metabolites are featured on Scripps Center for Metabolomics METLIN Metabolite Database. To learn more, visit sigma.com/metlin.
Unprecedented acetoacetyl-coenzyme A synthesizing enzyme of the thiolase superfamily involved in the mevalonate pathway. Okamura E, Tomita T, et al. Proc. Natl. Acad. Sci. U. S. A. 107, 11265-11270, (2010)
A new pathway for poly(3-hydroxybutyrate) production in Escherichia coli and Corynebacterium glutamicum by functional expression of a new acetoacetyl-coenzyme A synthase. Matsumoto K, Yamada M, Leong CR, et al. Biosci. Biotechnol. Biochem. 75(2), 364-6, (2011)
Structure of Staphylococcus aureus1,4-dihydroxy-2-naphthoyl-CoA synthase (MenB) in complex with acetoacetyl-CoA. Ulaganathan V, Agacan MF, Buetow L, et al. Acta Crystallogr. F, Struct. Biol. Cryst. Commun. 63(Pt 11), 908-13, (2007)
Feasibility of pathways for transfer of acyl groups from mitochondria to the cytosol to form short chain acyl-CoAs in the pancreatic beta cell. MacDonald MJ, Smith AD, Hasan NM, et al. J. Biol. Chem. 282(42), 30596-606, (2007)
Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function. Haapalainen AM, Meriläinen G, Pirilä PL, et al. Biochemistry 46(14), 4305-21, (2007)
Analyses of co-operative transitions in Plasmodium falciparum beta-ketoacyl acyl carrier protein reductase upon co-factor and acyl carrier protein binding. Karmodiya K and Surolia N FEBS J. 273(17), 4093-103, (2006)
X-ray crystal structures of HMG-CoA synthase from Enterococcus faecalis and a complex with its second substrate/inhibitor acetoacetyl-CoA. Steussy CN, Vartia AA, Burgner JW, et al. Biochemistry 44(43), 14256-67, (2005)
The catalytic cycle of biosynthetic thiolase: a conformational journey of an acetyl group through four binding modes and two oxyanion holes. Kursula P, Ojala J, Lambeir AM, et al. Biochemistry 41(52), 15543-56, (2002)
Sigma factor RpoS controls alkylresorcinol synthesis through ArpR, a LysR-type regulatory protein, during encystment of Azotobacter vinelandii. Romero Y, Moreno S, Guzmán J, et al. J. Bacteriol. 195(8), 1834-44, (2013)
FT-ICR-MS characterization of intermediates in the biosynthesis of the α-methylbutyrate side chain of lovastatin by the 277 kDa polyketide synthase LovF. Meehan MJ, Xie X, Zhao X, et al. Biochemistry 50(2), 287-99, (2011)
Aldehyde-alcohol dehydrogenase and/or thiolase overexpression coupled with CoA transferase downregulation lead to higher alcohol titers and selectivity in Clostridium acetobutylicum fermentations. Sillers R, Al-Hinai MA, and Papoutsakis ET Biotechnol. Bioeng. 102(1), 38-49, (2009)
Mycobacterium tuberculosis beta-ketoacyl-ACP reductase: alpha-secondary kinetic isotope effects and kinetic and equilibrium mechanisms of substrate binding. Silva RG, Rosado LA, Santos DS, et al. Arch. Biochem. Biophys. 471(1), 1-10, (2008)
Long-chain acyl-CoA esters inhibit phosphorylation of AMP-activated protein kinase at threonine-172 by LKB1/STRAD/MO25. Taylor EB, Ellingson WJ, Lamb JD, et al. Am. J. Physiol. Endocrinol. Metab. 288(6), E1055-61, (2005)
Detection of covalent tetrahedral adducts by differential isotope shift 13C NMR: acetyl-enzyme reaction intermediate formed by 3-hydroxy-3-methylglutaryl-CoA synthase. Miziorko HM and Vinarov DA Meth. Enzymol. 354, 208-23, (2002)
Stimulation of hepatic cholesterol biosynthesis by fatty acids. Effects of oleate on cytoplasmic acetoacetyl-CoA thiolase, acetoacetyl-CoA synthetase and hydroxymethylglutaryl-CoA synthase. W.H. Salam et al. Biochem. J. 258, 563, (1989)
C.A. Clark J. Chem. Soc. Chem. Commun., 1568, (1985)
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