Serine O-acetyltransferase
| 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 | ||||||||
| |||||||||
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
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
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1S80, PDB: 1SSM, PDB: 1SSQ, PDB: 1SST, PDB: 1T3D, PDB: 1Y7L, and PDB: 2ISQ.
N terminal protein domain
| SATase N terminal domain | |||||||
|---|---|---|---|---|---|---|---|
 The structure of the enzyme serine acetyltransferase- apoenzyme (truncated) | |||||||
| Identifiers | |||||||
| Symbol | SATase_N | ||||||
| Pfam | PF06426 | ||||||
| InterPro | IPR010493 | ||||||
| |||||||
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]
References
- ↑ Enzyme 2.3.1.30 at KEGG Pathway Database.
- ↑ Denk D, Böck A (March 1987). "L-cysteine biosynthesis in Escherichia coli: nucleotide sequence and expression of the serine acetyltransferase (cysE) gene from the wild-type and a cysteine-excreting mutant". J. Gen. Microbiol. 133 (3): 515–25. doi:10.1099/00221287-133-3-515. PMID 3309158.
- ↑ Saito K, Yokoyama H, Noji M, Murakoshi I (July 1995). "Molecular cloning and characterization of a plant serine acetyltransferase playing a regulatory role in cysteine biosynthesis from watermelon". J. Biol. Chem. 270 (27): 16321–6. doi:10.1074/jbc.270.27.16321. PMID 7608200.
- ↑ Kredich NM, Tomkins GM (1966). "The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium". J. Biol. Chem. 241 (21): 4955–65. doi:10.1016/S0021-9258(18)99657-2. PMID 5332668.
- ↑ Smith IK, Thompson JF (1971). "Purification and characterization of L-serine transacetylase and O-acetyl-L-serine sulfhydrylase from kidney bean seedlings (Phaseolus vulgaris)". Biochim. Biophys. Acta. 227 (2): 288–95. doi:10.1016/0005-2744(71)90061-1. PMID 5550822.
- ↑ Tabe L, Wirtz M, Molvig L, Droux M, Hell R (March 2010). "Overexpression of serine acetlytransferase produced large increases in O-acetylserine and free cysteine in developing seeds of a grain legume". J. Exp. Bot. 61 (3): 721–33. doi:10.1093/jxb/erp338. PMC 2814105. PMID 19939888.
- 1 2 Pye VE, Tingey AP, Robson RL, Moody PC (September 2004). "The structure and mechanism of serine acetyltransferase from Escherichia coli". J. Biol. Chem. 279 (39): 40729–36. doi:10.1074/jbc.M403751200. PMID 15231846.