acetyl-CoA

(redirected from Acetyl-coenzyme A)
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a·ce·tyl-Co·A

 (ə-sēt′l-kō′ā′, ăs′ĭ-tl-)
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Goat acetyl-coenzyme A carboxylase alpha: molecular characterization, polymorphism, and association with milk traits.
the hepatic-TG DNL index was also associated with expression of the hepatic lipogenic genes acetyl-Coenzyme A carboxylase alpha (ACACA), fatty acid synthase (FASN), and sterol regulatory element binding transcription factor 1 (SREBP-1), and changes in the expression of these genes were also closely reflected by the VLDL-TG DNL index.
Devoted to naturally occurring metal-carbon bonds, the book sums up recent work in the field, with chapters on organometallic chemistry of B12 coenzymes, cobalamin- and corrinoid-dependent enzymes, nickel-alkyl bond formation in the active site of methyl-coenzyme M reductase, and nickel-alkyl bonds in acetyl-coenzyme A synthases.
In addition, the expression of acetyl-Coenzyme A synthetase 2 (categorized as a "Fatty acid oxidation" gene) was three-fold higher in mammary than liver tissue, consistent with its function of activating acetate for use in ruminant lipid synthesis and fuel support (Smith and Prior, 1986).
Furthermore, theaflavins also inhibited acetyl-coenzyme A carboxylase activities by stimulating AMP-activated protein kinase (AMPK) through the LKB1 and reactive oxygen species pathways.
These acids are made from acetyl-coenzyme A (acetyl-CoA), which is also the starting material for biosynthesis of waxes, flavonoids, certain amino acids and other compounds.
Susceptibility to these chemicals is conditioned by a plastid-localized isoform of acetyl-coenzyme A carboxylase (ACCase; EC 6.
The licensed technology may provide the enhanced production of bio-diesel feedstocks, whereby over expression of Acetyl-Coenzyme A Carboxylase in algae leads to overproduction of triglycerides.
The expression levels of 3-hydroxyacyl-CoA dehydrogenase type-2 (HCDH), acetyl-Coenzyme A acetyltransferase 2 (ACAT) and elongation factor Tu were down-regulated, and alpha-enolase and creatine kinase were up-regulated in the livers of ketotic cows.
Coverage includes the biogeochemistry of nickel and its release into the environment; the impact of nickel on the metabolism of cyanobacteria and eukaryotic plants; the complex formation of nickel with amino acids and peptides, and with sugar residues, nucleobases, phosphates, ucleosides, and nucleic acids; synthetic models for the active sites of nickel- containing enzymes; the role of nickel in enzymes such as ureases, hydrogenases, superoxide dismutases, acireductone dioxygenases, acetyl-coenzyme A synthases, carbon monoxide dehydrogenases, and methyl-coenzyme M reductases; chaperones of nickel metabolism; the role of nickel in environmental adaptation of the gastric pathogen Helicobacer pylori; nickel-dependent gene expression; and nickel toxicity and carcinogenesis.
The role of adenosine triphosphate-citrate lyase in metabolism of acetyl-coenzyme A and function of blood platelets in diabetes mellitus.