Crystallization (Comment) | Organism |
---|---|
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] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.95 | - |
acetyl-CoA | - |
Leptospira interrogans | |
1.6 | - |
L-homoserine | - |
Leptospira interrogans |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
40000 | - |
SDS-PAGE | Leptospira interrogans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Leptospira interrogans | Q8F4I0 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + L-homoserine | - |
Leptospira interrogans | CoA + O-acetyl-L-homoserine | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | crystal structure | Leptospira interrogans |
Synonyms | Comment | Organism |
---|---|---|
homoserine O-acetyltransferase | - |
Leptospira interrogans |
HTA | - |
Leptospira interrogans |