Glutaconate CoA-transferase

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glutaconate CoA-transferase
Identifiers
EC no. 2.8.3.12
CAS no. 79078-99-2
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In enzymology, a glutaconate CoA-transferase (EC 2.8.3.12) is an enzyme that catalyzes the chemical reaction

acetyl-CoA + (E)-glutaconate acetate + glutaconyl-1-CoA

Thus, the two substrates of this enzyme are acetyl-CoA and (E)-glutaconate, whereas its two products are acetate and glutaconyl-1-CoA.

This enzyme belongs to the family of transferases, specifically the CoA-transferases. The systematic name of this enzyme class is acetyl-CoA:(E)-glutaconate CoA-transferase. This enzyme participates in styrene degradation and butanoate metabolism.

Related Research Articles

Acetyl-CoA synthetase (ACS) or Acetate—CoA ligase is an enzyme involved in metabolism of acetate. It is in the ligase class of enzymes, meaning that it catalyzes the formation of a new chemical bond between two large molecules.

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Glutaconyl-CoA is an intermediate in the metabolism of lysine. It is an organic compound containing a coenzyme substructure, which classifies it as a fatty ester lipid molecule. Being a lipid makes the molecule hydrophobic, which makes it insoluble in water. The molecule has a molecular formula of C26H40N7O19P3S, and a molecular weight 879.62 grams per mole.

Acetyl-S-ACP:malonate ACP transferase is an enzyme with systematic name acetyl-(acyl-carrier-protein):malonate S-(acyl-carrier-protein)transferase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Coenzyme A transferases</span> Coenzyme A transferases

Coenzyme A transferases (CoA-transferases) are transferase enzymes that catalyze the transfer of a coenzyme A group from an acyl-CoA donor to a carboxylic acid acceptor. Among other roles, they are responsible for transfer of CoA groups during fermentation and metabolism of ketone bodies. These enzymes are found in all three domains of life.

References