L-threonine 3-dehydrogenase | |||||||||
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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 | ||||||||
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L-Threonine dehydrogenase | |||||||
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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 | ||||||
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In enzymology, a L-threonine 3-dehydrogenase (EC 1.1.1.103) is an enzyme that catalyzes the chemical reaction
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.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2D8A, 2DFV, and 2DQ4.
Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other, nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD+ and NADH (H for hydrogen), respectively.
In enzymology, a homoserine dehydrogenase (EC 1.1.1.3) is an enzyme that catalyzes the chemical reaction
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