EC Number   |
Subunits |
Reference |
|---|
    1.1.1.3 | hexamer |
in absence of L-threonine |
642340 |
| 1.1.1.3 | tetramer |
in presence of L-threonine |
642340 |
| 1.1.1.3 | More |
primary and secondary structure comparison, the bifunctional enzyme contains 2 homologous subdomains defined by a common loop-alpha helix-loop-beta strand-loop-beta strand motif, the enzymes' regulatory domain is composed of 2 subdomains, amino acid residues 414-453 and 495-534 |
642341 |
| 1.1.1.3 | dimer |
StHSD is composed of a nucleotide-binding region (residues 1-130 and 285-304), a dimerization region (residues 131-145 and 256-284), and a catalytic region (residues 146-255). Presence of a disulfide bond formed between two cysteine residues (position 304) in the C-terminal regions of the two subunits |
-, 762453 |
| 1.1.1.3 | More |
structural basis for the catalytic mechanism of homoserine dehydrogenase, overview |
-, 739791 |
| 1.1.1.3 | More |
structure homology modelling, three-dimensional structure analysis and molecular dynamics simulation, overview |
-, 740548 |
| 1.1.1.3 | homodimer |
the enzyme is a dimer in solution as well as in the crystal. Enzyme HSD from stapylococcus aureus is an elongated molecule with three domains: a nucleotide cofactor binding domain at the N-terminus, a central catalytic domain and a C-terminal ACT domain, structure overview |
-, 739791 |
| 1.1.1.3 | More |
the unusual oligomeric assembly can be attributed to the additional C-terminal ACT domain of enzyme BsHSD. Circular dichroism spectroscopy analysis exhibits a typical pattern for alpha/beta proteins, the enzyme structure includes a Rossman fold. The enzyme's nucleotide-binding domain and substrate-binding domain are commonly found in all HSDs from any organism, but the C-terminal ACT domain is an additional regulatory domain that is present in only a subset of HSDs |
-, 761687 |
| 1.1.1.3 | ? |
x * 35492, sequence calculation |
761404 |
| 1.1.1.3 | homopentamer or homohexamer |
x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation |
-, 760736 |
