Sorbitol dehydrogenase from horse liver: Purification, characterization and comparative properties

Bailey, James P.; Renz, Christopher; McGuinness, Eugene T.

doi:10.1016/0305-0491(81)90407-7

Cited by 4 publications

(1 citation statement)

References 21 publications

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“…The present study shows that sheep liver SDH catalyses the reversible NAD-linked oxidation of most polyols -including -mannitol and galactitol, the 2-and 4-epimers of sorbitol, respectivelyinto their corresponding ketoses. Numerous reports corroborate that -mannitol [12,[27][28][29][30][34][35][36][37][38] and galactitol [12,27,[29][30][31]38], as well as -arabitol [12,27,29,30,38], are substrates for SDH. Hence, the putative -cis-2,4-dihydroxy requirement for the polyol substrates of SDH is not absolute.…”

Section: Substrate Specificity Of Mammalian Sorbitol Dehydrogenasementioning

confidence: 78%

Substrate specificity of sheep liver sorbitol dehydrogenase

Lindstad

Köll

McKinley-McKee

1998

Biochemical Journal

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The substrate specificity of sheep liver sorbitol dehydrogenase has been studied by steady-state kinetics over the range pH 7-10. Sorbitol dehydrogenase stereo-selectively catalyses the reversible NAD-linked oxidation of various polyols and other secondary alcohols into their corresponding ketones. The kinetic constants are given for various novel polyol substrates, including -glucitol, -mannitol, -altritol, -altritol, -iditol and eight heptitols, as well as for many aliphatic and aromatic alcohols. The maximum velocities (k cat ) and the substrate specificity-constants (k cat \K m ) are positively correlated with increasing pH. The enzymecatalysed reactions occur by a compulsory ordered kinetic mechanism with the coenzyme as the first, or leading, substrate. With many substrates, the rate-limiting step for the overall reaction is the enzyme-NADH product dissociation. However, with several substrates there is a transition to a mechanism with partial rate-limitation at the ternary complex level, especially at

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