D-threo-aldose 1-dehydrogenase
| 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, d-threo-aldose 1-dehydrogenase[1] is an enzyme that catalyzes the chemical reaction
- d-threo-aldose + NAD+ 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.
d-threo-aldose 1-dehydrogenase is capable of oxidizing l-glucose, l-xylose, d-arabinose, and l-fucose, allowing Trinickia caryophylli, the organism from which it was first isolated, to use l-Glucose as a source of energy. Oxidation of these monosaccharides is inhibited by their respective enantiomers.[2]
References
[edit]- ^ EC 1.1.1.122
- ^ Sasajima, Ken-Ichi; Sinskey, Anthony J. (1979). "Oxidation of l-glucose by a Pseudomonad". Biochimica et Biophysica Acta (BBA) - Enzymology. 571 (1): 120–126. doi:10.1016/0005-2744(79)90232-8. PMID 40609.
- 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. doi:10.1016/S0021-9258(18)93693-8. PMID 4309152.
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