L-threonine 3-dehydrogenase

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
Search PMC articles PubMed articles NCBI proteins

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
Search for Structures Swiss-model Domains InterPro

In enzymology, L-threonine 3-dehydrogenase (EC 1.1.1.103) is an enzyme that catalyzes the chemical reaction

L-threonine

+ NAD⁺

 

 

 

H⁺

 

H⁺

 

(S)-2-amino-3-ketobutyric acid

+ NADH

 

The two substrates of this enzyme are L-threonine and oxidised nicotinamide adenine dinucleotide (NAD⁺). Its products are (S)-2-amino-3-ketobutyric acid, reduced NADH, and a proton. ^{[1] [2] [3] [4] [5]}

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

1. Enzyme 1.1.1.103 at KEGG Pathway Database.
2. 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.
3. 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.
4. 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.
5. 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.