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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 .
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]
These genes include carbamate kinase (arcC), shikimate dehydrogenase (aroE), glycerol kinase (glpF), guanylate kinase (gmk), phosphate acetyltransferase (pta), triosephosphate isomerase (tpi) and acetyl coenzyme A acetyltransferase (yqiL) as specified by the MLST website. However, it is not uncommon for up to ten housekeeping genes to be used.
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]
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.
Glucose Hexokinase ATP ADP Glucose 6-phosphate Glucose-6-phosphate isomerase Fructose 6-phosphate Phosphofructokinase-1 ATP ADP Fructose 1,6-bisphosphate Fructose-bisphosphate aldolase Dihydroxyacetone phosphate + + Glyceraldehyde 3-phosphate Triosephosphate isomerase 2 × Glyceraldehyde 3-phosphate 2 × Glyceraldehyde-3-phosphate dehydrogenase NAD + + P i NADH + H + NAD + + P i NADH + H + 2 ...
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).
The first step of this reaction is phosphorylation of the substrate via phosphotransferase during transport. In the case of glucose, the product of this phosphorylation is glucose-6-phosphate (Glc-6P). Due to the negative charge of the phosphate, this Glc-6P can no longer freely leave the cell.
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