Sorbose reductase
From Wikipedia, the free encyclopedia
In enzymology, a sorbose reductase (EC 1.1.1.289) is an enzyme that catalyzes the chemical reaction
- D-glucitol + NADP+
L-sorbose + NADPH + H+
Thus, the two substrates of this enzyme are D-glucitol and NADP+, whereas its 3 products are L-sorbose, NADPH, 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-glucitol:NADP+ oxidoreductase. This enzyme is also called Sou1p.
[edit] References
- IUBMB entry for 1.1.1.289
- BRENDA references for 1.1.1.289 (Recommended.)
- PubMed references for 1.1.1.289
- PubMed Central references for 1.1.1.289
- Google Scholar references for 1.1.1.289
- Greenberg JR, Price NP, Oliver RP, Sherman F, Rustchenko E (2005). "Candida albicans SOU1 encodes a sorbose reductase required for L-sorbose utilization". Yeast. 22: 957–69. doi:. PMID 16134116.
- Rustchenko E (2005). "Erratum report: Candida albicans SOU1 encodes a sorbose reductase required for L-sorbose utilization". Yeast 22: 1171.
- Sugisawa T, Hoshino T and Fujiwara A (1991). "Purification and properties of NADPH-linked L-sorbose reductase from Gluconobacter melanogenus N44-1". Agric. Biol. Chem. 55: 2043–2049.
- Shinjoh M, Tazoe M, Hoshino T (2002). "NADPH-dependent L-sorbose reductase is responsible for L-sorbose assimilation in Gluconobacter suboxydans IFO 3291". J. Bacteriol. 184: 861–3. PMID 11790761.

