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Literature summary extracted from

  • Wang, M.; Liu, L.; Wang, Y.; Wei, Z.; Zhang, P.; Li, Y.; Jiang, X.; Xu, H.; Gong, W.
    Crystal structure of homoserine O-acetyltransferase from Leptospira interrogans (2007), Biochem. Biophys. Res. Commun., 363, 1050-1056.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.31 crystal structure of HTA from Leptospira interrogans is determined at 2.2 A resolution using selenomethionyl single-wavelength anomalous diffraction method. HTA is modular and consists of two structurally distinct domains: a core alpha/beta domain containing the catalytic site and a helical bundle called the lid domain. Structure fold belongs to alpha/beta hydrolase superfamily with the characteristic catalytic triad residues in the active site. The catalytic His and Ser are both present in two conformations, which may be involved in the catalytic mechanism for acetyl transfer Leptospira interrogans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.31 0.95
-
 acetyl-CoA
-
 Leptospira interrogans
2.3.1.31 1.6
-
 L-homoserine
-
 Leptospira interrogans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.31 40000
-
 SDS-PAGE Leptospira interrogans

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.31 Leptospira interrogans Q8F4I0
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.31 acetyl-CoA + L-homoserine
-
 Leptospira interrogans CoA + O-acetyl-L-homoserine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.31 homodimer crystal structure Leptospira interrogans

Synonyms

EC Number Synonyms Comment Organism
2.3.1.31 homoserine O-acetyltransferase
-
 Leptospira interrogans
2.3.1.31 HTA
-
 Leptospira interrogans