Literature summary extracted from
Thangavelu, B.; Pavlovsky, A.G.; Viola, R.
Structure of homoserine O-acetyltransferase from Staphylococcus aureus: the first Gram-positive ortholog structure (2014), Acta Crystallogr. Sect. F, 70, 1340-1345.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.3.1.31 |
gene met2, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21(DE3) |
Staphylococcus aureus |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.3.1.31 |
purified recombinant apoenzyme, hanging-drop vapor-diffusion method, mixing of 0.001 ml of 5 mg/ml protein solution with 0.001 ml of well solution, containing 0.7 M ammonium formate, 100 mM imidazole-HCl, pH 6.5, 20°C, 5-7 days, X-ray diffraction structure determination and analysis at 2.45 A resolution |
Staphylococcus aureus |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.3.1.31 |
acetyl-CoA + L-homoserine |
Staphylococcus aureus |
- |
CoA + O-acetyl-L-homoserine |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.3.1.31 |
Staphylococcus aureus |
- |
gene met2 |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.3.1.31 |
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion excange chromatography, followed by gel electrophoresis, dialysis, and ultrafiltration |
Staphylococcus aureus |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.3.1.31 |
acetyl-CoA + L-homoserine |
- |
Staphylococcus aureus |
CoA + O-acetyl-L-homoserine |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.3.1.31 |
HTA |
- |
Staphylococcus aureus |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
2.3.1.31 |
7.5 |
- |
assay at |
Staphylococcus aureus |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
2.3.1.31 |
acetyl-CoA |
- |
Staphylococcus aureus |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.3.1.31 |
metabolism |
the enzyme reaction represents a critical control point for cell growth and viability |
Staphylococcus aureus |
2.3.1.31 |
additional information |
the enzyme structure belongs to the alpha/beta-hydrolase superfamily, consisting of two distinct domains: a core alpha/beta-domain containing the catalytic site and a lid domain assembled into a helical bundle. The active site consists of a classical catalytic triad located at the end of a deep tunnel, structure comparisons, overview. The reaction catalyzed by the enzyme involves the acetylation of the gamma-hydroxyl of homoserine through an acetyl-CoA-dependent acetylation via a double-displacement mechanism facilitated by a classic Ser-His-Asp catalytic triad which is located at the bottom of a narrow tunnel |
Staphylococcus aureus |