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In enzymology, a phosphate acetyltransferase (EC 2.3.1.8) is an enzyme that catalyzes the chemical reaction acetyl-CoA + phosphate ⇌ {\displaystyle \rightleftharpoons } CoA + acetyl phosphate The substrates of this enzyme are acetyl-CoA and phosphate , whereas its two products are CoA and acetyl phosphate .
In enzymology, a glycerol-3-phosphate O-acyltransferase (EC 2.3.1.15) is an enzyme that catalyzes the chemical reaction acyl-CoA + sn-glycerol 3-phosphate ⇌ {\displaystyle \rightleftharpoons } CoA + 1-acyl-sn-glycerol 3-phosphate
Pymol-generated image of E1 subunit of pyruvate dehydrogenase complex in E. Coli. The E1 subunit, called the pyruvate dehydrogenase subunit, is either a homodimer (comprising two “α” chains, e.g. in Escherichia coli) or a heterotetramer of two different chains (two “α” and two “β” chains).
Thus, the two substrates of this enzyme are acetyl-CoA and 1-alkyl-sn-glycero-3-phosphate, whereas its two products are CoA and 1-alkyl-2-acetyl-sn-glycero-3-phosphate. This enzyme belongs to the family of transferases , specifically those acyltransferases transferring groups other than aminoacyl groups.
The systematic name of this enzyme class is acetyl-CoA:[acyl-carrier-protein] S-acetyltransferase. Other names in common use include acetyl coenzyme A-acyl-carrier-protein transacylase, acetyl-CoA:ACP transacylase, [acyl-carrier-protein]acetyltransferase, [ACP]acetyltransferase, and ACAT. This enzyme participates in fatty acid biosynthesis.
An acetyltransferase (also referred to as a transacetylase) is any of a class of transferase enzymes that transfers an acetyl group in a reaction called acetylation.In biological organisms, post-translational modification of a protein via acetylation can profoundly transform its functionality by altering various properties like hydrophobicity, solubility, and surface attributes. [1]
A simplified reaction mechanism for N-acetylglutamate synthase (NAGS). Two mechanisms for N-acetyltransferase function have been proposed: a two-step, ping-pong mechanism involving transfer of the relevant acetyl group to an activated cysteine residue [10] and a one-step mechanism through direct attack of the amino nitrogen on the carbonyl group. [11]
In enzymology, glucosamine-phosphate N-acetyltransferase (GNA) (EC 2.3.1.4) is an enzyme that catalyzes the transfer of an acetyl group from acetyl-CoA to the primary amine in glucosamide-6-phosphate, generating a free CoA and N-acetyl-D-glucosamine-6-phosphate.