| L-threonine 3-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 L-threonine 3-dehydrogenase homotetramer, Thermus thermophilus | |||||||||
| Identifiers | |||||||||
| EC no. | 1.1.1.103 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
| L-Threonine dehydrogenase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | TDH | ||||||
| NCBI gene | 157739 | ||||||
| HGNC | 15547 | ||||||
| RefSeq | NM_152566 | ||||||
| UniProt | Q8IZJ6 | ||||||
| Other data | |||||||
| EC number | 1.1.1.103 | ||||||
| Locus | Chr. 8 p23.1 | ||||||
| |||||||
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[edit]
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2D8A, 2DFV, and 2DQ4.
References[edit]
- Green ML, Elliott WH (1964). "The enzymic formation of aminoacetone from threonine and its further metabolism". Biochem. J. 92 (3): 537–49. doi:10.1042/bj0920537. PMC 1206098. PMID 4284408.
- Hartshorne D, Greenberg DM (1964). "Studies on liver threonine dehydrogenase". Arch. Biochem. Biophys. 105: 173–8. doi:10.1016/0003-9861(64)90250-4. PMID 14165492.
- Epperly BR, Dekker EE (April 1991). "L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies". The Journal of Biological Chemistry. 266 (10): 6086–92. doi:10.1016/S0021-9258(18)38087-6. PMID 2007567.
- Edgar AJ (October 2002). "The human L-threonine 3-dehydrogenase gene is an expressed pseudogene". BMC Genetics. 3: 18. doi:10.1186/1471-2156-3-18. PMC 131051. PMID 12361482.
