D-threo-aldose 1-dehydrogenase
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| D-threo-aldose 1-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.122 | ||||||||
| CAS no. | 9082-70-6 | ||||||||
| 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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In enzymology, a D-threo-aldose 1-dehydrogenase (EC 1.1.1.122) is an enzyme that catalyzes the chemical reaction
- a D-threo-aldose + NAD+ a D-threo-aldono-1,5-lactone + NADH + H+
Thus, the two substrates of this enzyme are D-threo-aldose and NAD+, whereas its 3 products are D-threo-aldono-1,5-lactone, 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 D-threo-aldose:NAD+ 1-oxidoreductase. Other names in common use include L-fucose dehydrogenase, (2S,3R)-aldose dehydrogenase, dehydrogenase, L-fucose, and L-fucose (D-arabinose) dehydrogenase. This enzyme participates in ascorbate and aldarate metabolism.
References
- Sasajima KI, Sinskey AJ (1979). "Oxidation of L-glucose by a Pseudomonad". Biochim. Biophys. Acta. 571 (1): 120–6. doi:10.1016/0005-2744(79)90232-8. PMID 40609.
- Schachter H, Sarney J, McGuire EJ, Roseman S (1969). "Isolation of diphosphopyridine nucleotide-dependent L-fucose dehydrogenase from pork liver". J. Biol. Chem. 244 (17): 4785–92. PMID 4309152.
