D-sorbitol dehydrogenase

Figure 6.63 Substrate activation mechanisms and stereochemistry (shown in the sense of ketone reduction) for (a) aldose reductases, (b) long-chain dehydrogenases, (c) glucose-6-phosphate dehydrogenase and (d) sorbitol dehydrogenase. The glutamate ligand to Zn is shown removed in the complex with fructose, but this is speculative.

E = D-sorbitol dehydrogenase, whole cells of Gluconobacter oxidans Figure 19-7. Synthesis of key intermediate for miglitol (Bayer). 

D-Sorbitol dehydrogenase 1-Amino-D-sorbitol (N-protected) 1.00 M Aqueous... 

Sefcovicova, J., J. Eilip, P. Tomcik et al. 2011. A biopolymer-based carbon nanotube interface integrated with a redox shuttle and a D-sorbitol dehydrogenase for robust monitoring of D-sorbitol. Microchim. Acta 175 21-30. 

D-Glucose can be specifically reduced in the presence of other sugars by the enzyme, D-sorbitol dehydrogenase, using the reduced form of the coenzyme nicotinamide adenine dinucleotide (NADH). The reaction is reversible, and d-glucitol (D-sorbitol) can be specifically oxidized to D-glucose using the oxidized form of the coenzyme, NAD+. 

Miyazaki T, Tomiyama N, Shinjoh M, Hoshino T (2002) Molecular cloning and functional expression of D-sorbitol dehydrogenase from Gluconobacter suboxydans IF03255, which requires pyrroloquinoline quinone and hydrophobic protein SldB fin activity development in E. coli. Biosci Biotechnol Biochcan 66(2) 262—270... 

Shinagawa E, Matsushita K, Adachi O, Ameyama M (1982) Purification and characterization of D-sorbitol dehydrogenase from membrane of Gluconobacter suboxydans var. alpha. Agric Biol Chem46(l) 135-141... 

Toyama H, Soemphol W, Moonmangmee D, Adachi O, Matsushita K (2005) Molecular properties of membrane-bound FAD-containing D-sorbitol dehydrogenase from thermotolerant Gluconobacter frateurii isolated from Thailand. Biosci Biotechnol Biochem 69 1120-1129... 

Vongsuvanlert, V, Tani, Y, 1988. Characterization of D-sorbitol dehydrogenase involved in D-sorbitol production of a methanol yeast, Candida boidinii (kheckera sp.) no. 2201. Agricultural and Biological Chemistry 52, 419-426. 

SORBITOL DEHYDROGENASE FRUCTOSE-1,6-BISPHOSPHATASE FRUCTOSE-2,6-BISPHOSPHATASE D-Fructose 2,6-bisphosphate, 6-PHOSPHOFRUCTO-2-KINASE Fructose-1,6-bisphosphate aldolase, ALDOLASE... 

Schematic of the polyol pathway showing the NADPH-dependent reduction of open chain D-glucose to sorbitol, which is catalyzed by ALR2. This step is followed by the NAD+-dependent oxidation of sorbitol by sorbitol dehydrogenase to yield D-fructose.

Webb, D. and Gagnon, M.M. (2007) Serum sorbitol dehydrogenase activity as an indicator of chemically induced liver damage in black bream (Acanthopagrus butcheri). Environ. Bioindicators, 2, 172-182. 

A number of studies on the metabolism of 3FG and 4FG in Locusta miaratoria have been undertaken. Both 3FG and 4FG are toxic to locust with LD50 s of 4.8 mg/g and 0.6 mg/g respectively. In vitro studies showed that 3FG is metabolized in the fat body, via the NADP-linked aldose reductase, to 3-deoxy-3-fluoro-D-glucitol (3FGL). This metabolite was detected in the hemolymph of the insect and shown to be both a competitive inhibitor and a substrate for NAD-linked sorbitol dehydrogenase, thereby generating 3-deoxy-3-fluoro-D-fructose (3FF) (541. Subsequently, it was shown by in vivo radio-respirometric analysis of C02 and appropriate chase experiments, that 3FG metabolism irreversibly inhibits glycolysis and not the hexose monophosphate shunt or tricarboxylic acid cycle (55). In addition, the release of fluoride ion and H20 from D-[3- H]-3FG was also observed. Based on the mechanism of aldolase (55) and triosephosphate isomerase... 

Fig. 12.3 Classical two-step based one-step fermentation process ( Recombinant strains with different dehydrogenase). The D-glucose was hydrogenated to form D-sorbitol. The D-sorbitol was directly converted into 2-KLG with a G. oxydans strain or a E. coli strain (or any other potential strains) with the three different kinds of dehydrogenases. The 2-KLG was then esterified and lactonized to form vitamin C...

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