L-threonine 3-dehydrogenase
(Redirected from
L-threonine dehydrogenase
)| L-threonine 3-dehydrogenase | |||||||||
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ExPASy NiceZyme view | | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| L-Threonine dehydrogenase | |||||||
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| Identifiers | |||||||
| Symbol | TDH | ||||||
Chr. 8 p23.1 | |||||||
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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
.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): 537–49. PMID 4284408.
- Hartshorne D, Greenberg DM (1964). "Studies on liver threonine dehydrogenase". Arch. Biochem. Biophys. 105: 173–8. 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. PMID 2007567.
- Edgar AJ (October 2002). "The human L-threonine 3-dehydrogenase gene is an expressed pseudogene". BMC Genetics. 3: 18. PMID 12361482.
