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Literature summary for 2.3.1.31 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.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene met2, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli strain BL21(DE3) Staphylococcus aureus

Crystallization (Commentary)

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Staphylococcus aureus
-
gene met2
-

Purification (Commentary)

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 and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + L-homoserine
-
Staphylococcus aureus CoA + O-acetyl-L-homoserine
-
?

Synonyms

Synonyms Comment Organism
HTA
-
Staphylococcus aureus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Staphylococcus aureus

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
Staphylococcus aureus

General Information

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