Serine O-acetyltransferase
Protein domain
From Wikipedia, the free encyclopedia
Serine O-acetyltransferase (EC 2.3.1.30) is an enzyme that catalyzes the chemical reaction
- acetyl-CoA + L-serine CoA + O-acetyl-L-serine
| Serine O-acetyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Serine acetyltransferase hexamer, Haemophilus influenzae | |||||||||
| Identifiers | |||||||||
| EC no. | 2.3.1.30 | ||||||||
| CAS no. | 9023-16-9 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The two substrates of this enzyme are L-serine and acetyl-CoA. Its products are O-acetyl-L-serine and CoA.
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:L-serine O-acetyltransferase. Other names in common use include SATase, L-serine acetyltransferase, serine acetyltransferase, and serine transacetylase. This enzyme participates in cysteine metabolism and sulfur metabolism.[1]
Structural studies
N terminal protein domain
In molecular biology, the protein domain SATase is short for Serine acetyltransferase and refers to an enzyme that catalyses the conversion of L-serine to L-cysteine in Escherichia coli.[2] Its role is to catalyse the activation of L-serine by acetyl-CoA. This entry refers to the N-terminus of the protein which has a sequence that is conserved in plants and bacteria.[3]
Function
The N-terminal domain of the protein Serine O-acetyltransferase catalyses the O-acetylation of the amino acid and has been characterised in Escherichia coli, Salmonella typhimurium.[4] and Phaseolus vulgaris.[5]
The enzyme acts together with cysteine synthase to convert serine into cysteine, a precursor to the essential amino acid, methionine. Serine acetyltransferase has been overexpressed in transgenic plants. These should contain more essential sulphur amino acids meaning a healthier diet for humans and animals.[6]
Structure
The amino-terminal alpha-helical domain particularly the amino acid residues His158 (histidine in position 158) and Asp143 (aspartic acid in position 143) form a catalytic triad with the substrate for acetyl transfer.[7] There are eight alpha helices that form the N-terminal domain.[7]
