| EC |
1.1.1.103 |
| Accepted name: |
L-threonine 3-dehydrogenase |
| Reaction: |
L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH + H+ |
| Other name(s): |
L-threonine dehydrogenase; threonine 3-dehydrogenase; threonine dehydrogenase; TDH |
| Systematic name: |
L-threonine:NAD+ oxidoreductase |
| 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: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9067-99-6 |
| References: |
| 1. |
Green, M.L. and Elliott, W.H. The enzymic formation of aminoacetone from threonine and its further metabolism. Biochem. J. 92 (1964) 537–549. [PMID: 4284408] |
| 2. |
Hartshorne, D. and Greenberg, D.M. Studies on liver threonine dehydrogenase. Arch. Biochem. Biophys. 105 (1964) 173–178. [DOI] [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 (1976) 1245–1249. [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 (1991) 6086–6092. [PMID: 2007567] |
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| [EC 1.1.1.103 created 1972] |
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