Cloned (Comment) | Organism |
---|---|
recombinant pET-tdh plasmid expressed in Escherichia coli BL21 (DE3) | Thermococcus kodakarensis |
Crystallization (Comment) | Organism |
---|---|
at room temperature using hanging-drop vapour diffusion method, at 2.4 A resolution. The enzyme is a homotetramer, each monomer consisting of 350 amino acids that form two domains, a catalytic domain and a NAD+-binding domain, which contains an alpha/beta Rossmann fold motif. An extended twelve-stranded beta-sheet is formed by the association of pairs of monomers in the tetramer | Thermococcus kodakarensis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | the active site catalytic zinc ion is absent from the TDH structure | Thermococcus kodakarensis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
38016 | - |
4 * 38016, electrospray mass spectrometry and gel filtration | Thermococcus kodakarensis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus kodakarensis | Q5JI69 | - |
- |
Purification (Comment) | Organism |
---|---|
by sonication, heating of the cell lysate, anion exchange and hydrophobic interaction chromatography | Thermococcus kodakarensis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-threonine + NAD+ | - |
Thermococcus kodakarensis | (2S)-2-amino-3-oxobutanoate + NADH + H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | 4 * 38016, electrospray mass spectrometry and gel filtration | Thermococcus kodakarensis |
Synonyms | Comment | Organism |
---|---|---|
L-threonine dehydrogenase | - |
Thermococcus kodakarensis |
TDH | - |
Thermococcus kodakarensis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | binding site of the essential co-factor NAD+ is present in all subunits, it occupies the active site pocket and is bound predominantly by Van der Waal interactions and hydrogen bonds with the surrounding amino acid residues | Thermococcus kodakarensis |