L-arabinose 1-dehydrogenase
| L-arabinose 1-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.46 | ||||||||
| CAS no. | 9028-52-8 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a L-arabinose 1-dehydrogenase (EC 1.1.1.46) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-arabinose and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are L-arabino-1,4-lactone, reduced NADH, and a proton.[1][2]
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-arabinose:NAD+ 1-oxidoreductase. This enzyme participates in ascorbate and aldarate metabolism.
References
- ^ Enzyme 1.1.1.46 at KEGG Pathway Database.
- ^ Weimberg R, Doudoroff M (December 1955). "The oxidation of L-arabinose by Pseudomonas saccharophila". The Journal of Biological Chemistry. 217 (2): 607–24. doi:10.1016/S0021-9258(18)65926-5. PMID 13271422.