EC Number   |
Reaction |
Reference |
|---|
    2.3.1.30 | acetyl-CoA + L-serine = CoA + O-acetyl-L-serine |
a C-terminal hexapeptide-repeat domain is common for Arabidopsis thaliana isoforms and several other enzyme DNA sequences, it has a catalytic bifunctionality as serine acetyltransferase and in interaction with O-acetylserine (thiol) lyase and is involved in cysteine biosynthesis regulation, computational modeling |
486774 |
| 2.3.1.30 | acetyl-CoA + L-serine = CoA + O-acetyl-L-serine |
binding motif for O-acetylserine (thiol) lyase is located within 10 amino acid residues at the C-terminal end |
486777 |
| 2.3.1.30 | acetyl-CoA + L-serine = CoA + O-acetyl-L-serine |
ordered kinetic mechanism with acetyl CoA bound prior to L-serine and O-acetyl-L-serine released prior to CoA. The rate-limiting step along the reaction pathway is the nucleophilic attack of the serine hydroxyl on the thioester of acetyl CoA. Product release contributes to rate-limitation at saturating concentrations of reactants. The reaction is catalyzed by an active site general base with a pK of 7, which accepts a proton from the serine hydroxyl as a tetrahedral intermediate is formed between the reactants, and donates it to the thiol of CoA as the intermediate collapses to give products |
671580 |
| 2.3.1.30 | acetyl-CoA + L-serine = CoA + O-acetyl-L-serine |
ping pong bi bi mechanism |
-, 486761 |
| 2.3.1.30 | acetyl-CoA + L-serine = CoA + O-acetyl-L-serine |
steady-state random-order mechanism |
486778 |
| 2.3.1.30 | acetyl-CoA + L-serine = CoA + O-acetyl-L-serine |
there is no conformational difference in the enzyme between the apo and the substrate-bound states, indicating lock and key binding and the absence of an induced fit mechanism |
-, 735709 |
