L-threonine 3-dehydrogenase
| L-threonine 3-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.1.103 | ||||||||
| CAS number | 9067-99-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a L-threonine 3-dehydrogenase (EC 1.1.1.103) is an enzyme that catalyzes the chemical reaction
- L-threonine + NAD+ L-2-amino-3-oxobutanoate + NADH + H+
Thus, the two substrates of this enzyme are L-threonine and NAD+, whereas its 3 products are L-2-amino-3-oxobutanoate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-threonine:NAD+ oxidoreductase. Other names in common use include L-threonine dehydrogenase, threonine 3-dehydrogenase, and threonine dehydrogenase. This enzyme participates in glycine, serine and threonine metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2D8A, 2DFV, and 2DQ4.
References
- Green ML, Elliott WH (1964). "The enzymic formation of aminoacetone from threonine and its further metabolism". Biochem. J. 92 (3): 537&ndash, 49. PMC 1206098. PMID 4284408.
- Hartshorne D, Greenberg DM (1964). "Studies on liver threonine dehydrogenase". Arch. Biochem. Biophys. 105: 173&ndash, 8. doi:10.1016/0003-9861(64)90250-4. PMID 14165492.