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Literature summary for 1.1.1.103 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.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant pET-tdh plasmid expressed in Escherichia coli BL21 (DE3) Thermococcus kodakarensis

Crystallization (Commentary)

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

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 [Da] Molecular Weight Maximum [Da] Comment Organism
38016
-
4 * 38016, electrospray mass spectrometry and gel filtration Thermococcus kodakarensis

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis Q5JI69
-
-

Purification (Commentary)

Purification (Comment) Organism
by sonication, heating of the cell lysate, anion exchange and hydrophobic interaction chromatography Thermococcus kodakarensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-threonine + NAD+
-
Thermococcus kodakarensis (2S)-2-amino-3-oxobutanoate + NADH + H+
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 38016, electrospray mass spectrometry and gel filtration Thermococcus kodakarensis

Synonyms

Synonyms Comment Organism
L-threonine dehydrogenase
-
Thermococcus kodakarensis
TDH
-
Thermococcus kodakarensis

Cofactor

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