Cloned (Comment) | Organism |
---|---|
gene met2, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21(DE3) | Staphylococcus aureus |
Crystallization (Comment) | Organism |
---|---|
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + L-homoserine | Staphylococcus aureus | - |
CoA + O-acetyl-L-homoserine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | - |
gene met2 | - |
Purification (Comment) | Organism |
---|---|
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + L-homoserine | - |
Staphylococcus aureus | CoA + O-acetyl-L-homoserine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
HTA | - |
Staphylococcus aureus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Staphylococcus aureus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
acetyl-CoA | - |
Staphylococcus aureus |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme reaction represents a critical control point for cell growth and viability | Staphylococcus aureus |
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 |