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Vitamins can serve as precursors to many organic cofactors (e.g., vitamins B 1, B 2, B 6, B 12, niacin, folic acid) or as coenzymes themselves (e.g., vitamin C). However, vitamins do have other functions in the body. [29] Many organic cofactors also contain a nucleotide, such as the electron carriers NAD and FAD, and coenzyme A, which carries ...
Control of Acetyl-CoA Carboxylase. The AMP regulated kinase triggers the phosphorylation of the enzyme (thus inactivating it) and the phosphatase enzyme removes the phosphate group. The regulation of mammalian ACC is complex, in order to control two distinct pools of malonyl-CoA that direct either the inhibition of beta oxidation or the ...
32 100705 Ensembl ENSG00000076555 ENSMUSG00000042010 UniProt O00763 E9Q4Z2 RefSeq (mRNA) NM_001093 NM_133904 RefSeq (protein) NP_001084 NP_598665 NP_001390456 NP_001390457 NP_001390458 Location (UCSC) Chr 12: 109.12 – 109.27 Mb Chr 5: 114.28 – 114.39 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Acetyl-CoA carboxylase 2 also known as ACC-beta or ACC2 is an enzyme that in humans ...
Acetyl-CoA can be carboxylated in the cytosol by acetyl-CoA carboxylase, giving rise to malonyl-CoA, a substrate required for synthesis of flavonoids and related polyketides, for elongation of fatty acids to produce waxes, cuticle, and seed oils in members of the Brassica family, and for malonation of proteins and other phytochemicals. [21]
Thiamine pyrophosphate (TPP or ThPP), or thiamine diphosphate (ThDP), or cocarboxylase [1] is a thiamine (vitamin B 1) derivative which is produced by the enzyme thiamine diphosphokinase. Thiamine pyrophosphate is a cofactor that is present in all living systems, in which it catalyzes several biochemical reactions.
Usually, they are named after the substrate whose decarboxylation they catalyze, for example pyruvate decarboxylase catalyzes the decarboxylation of pyruvate. Examples [ edit ]
Many of these vitamin K-dependent proteins are involved in coagulation so the function of the encoded enzyme is essential for hemostasis. [5] Most gla domain-containing proteins depend on this carboxylation reaction for posttranslational modification. [6] In humans, the gamma-glutamyl carboxylase enzyme is most highly expressed in the liver.
Acetyl-CoA is formed into malonyl-CoA by acetyl-CoA carboxylase, at which point malonyl-CoA is destined to feed into the fatty acid synthesis pathway. Acetyl-CoA carboxylase is the point of regulation in saturated straight-chain fatty acid synthesis, and is subject to both phosphorylation and allosteric regulation. Regulation by phosphorylation ...