| First Author | Maret W | Year | 1988 |
| Journal | Biochemistry | Volume | 27 |
| Issue | 5 | Pages | 1622-8 |
| PubMed ID | 3365415 | Mgi Jnum | J:323241 |
| Mgi Id | MGI:7262843 | Doi | 10.1021/bi00405a035 |
| Citation | Maret W, et al. (1988) Purification and characterization of human liver sorbitol dehydrogenase. Biochemistry 27(5):1622-8 |
| abstractText | Sorbitol dehydrogenase from human liver was purified to homogeneity by affinity chromatography on immobilized triazine dyes, conventional cation-exchange chromatography, and high-performance liquid chromatography. The major form is a tetrameric, NAD-specific enzyme containing one zinc atom per subunit. Human liver sorbitol dehydrogenase oxidizes neither ethanol nor other primary alcohols. It catalyzes the oxidation of a secondary alcohol group of polyol substrates such as sorbitol, xylitol, or L-threitol. However, the substrate specificity of human liver sorbitol dehydrogenase is broader than that of the liver enzymes of other sources. The present report describes the stereospecific oxidation of (2R,3R)-2,3-butanediol, indicating a more general function of sorbitol dehydrogenase in the metabolism of secondary alcohols. Thus, the enzyme complements the substrate specificities covered by the three classes of human liver alcohol dehydrogenase. |
