EC 1.1.1.103 - L-threonine 3-dehydrogenase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 1.1.1.103

Names

Accepted name:
L-threonine 3-dehydrogenase
Other names:
L-threonine dehydrogenase
threonine 3-dehydrogenase
threonine dehydrogenase
TDH
Systematic name:
L-threonine:NAD+ oxidoreductase

Reactions

Comments:

This enzyme acts in concert with EC 2.3.1.29, glycine C-acetyltransferase, in the degradation of threonine to glycine. This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex [2]. In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00058
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008743
CAS Registry Number: 9067-99-6
UniProtKB/Swiss-Prot: (187) [show] [UniProt]

References

  1. Green, M.L. and Elliott, W.H.
    The enzymic formation of aminoacetone from threonine and its further metabolism.
    Biochem. J. 92: 537-549 (1964).
  2. Hartshorne, D. and Greenberg, D.M.
    Studies on liver threonine dehydrogenase.
    Arch. Biochem. Biophys. 105: 173-178 (1964). [PMID: 14165492]
  3. Newman, E.B., Kapoor, V. and Potter, R.
    Role of L-threonine dehydrogenase in the catabolism of threonine and synthesis of glycine by Escherichia coli.
    J. Bacteriol. 126: 1245-1249 (1976). [PMID: 7548]
  4. Epperly, B.R. and Dekker, E.E.
    L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies.
    J. Biol. Chem. 266: 6086-6092 (1991). [PMID: 2007567]

[EC 1.1.1.103 created 1972]