Literature summary extracted from
Bowyer, A.; Mikolajek, H.; Stuart, J.W.; Wood, S.P.; Jamil, F.; Rashid, N.; Akhtar, M.; Cooper, J.B.
Structure and function of the l-threonine dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis (2009), J. Struct. Biol., 168, 294-304.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.1.1.103 |
recombinant pET-tdh plasmid expressed in Escherichia coli BL21 (DE3) |
Thermococcus kodakarensis |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.1.1.103 |
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
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.1.1.103 |
additional information |
the active site catalytic zinc ion is absent from the TDH structure |
Thermococcus kodakarensis |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
1.1.1.103 |
38016 |
- |
4 * 38016, electrospray mass spectrometry and gel filtration |
Thermococcus kodakarensis |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.1.1.103 |
Thermococcus kodakarensis |
Q5JI69 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.1.1.103 |
by sonication, heating of the cell lysate, anion exchange and hydrophobic interaction chromatography |
Thermococcus kodakarensis |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.1.1.103 |
L-threonine + NAD+ |
- |
Thermococcus kodakarensis |
(2S)-2-amino-3-oxobutanoate + NADH + H+ |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.1.1.103 |
homotetramer |
4 * 38016, electrospray mass spectrometry and gel filtration |
Thermococcus kodakarensis |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.1.1.103 |
L-threonine dehydrogenase |
- |
Thermococcus kodakarensis |
1.1.1.103 |
TDH |
- |
Thermococcus kodakarensis |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.1.1.103 |
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 |
|