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10109339001

Roche

Sorbitol Dehydrogenase (SDH)

from sheep liver

Synonym(s):
SDH, Sorbitol Dehydrogenase, sorbitol
Enzyme Commission number:

Quality Level

form

lyophilized

specific activity

~40 units/mg protein (At 25 °C with D-fructose as the substrate.)

packaging

pkg of 10 mg (60 mg lyophilizate)

manufacturer/tradename

Roche

optimum pH

7.5

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This Item
1012765500110165875001G3512
specific activity

~40 units/mg protein (At 25 °C with D-fructose as the substrate.)

specific activity

~350 units/mg protein (At 25 °C with glucose-6-P as the substrate.)

specific activity

~550 units/mg protein (At 25 °C (650 U/mg at 30 °C) with glucose-6-P and NAD as the substrates.)

specific activity

≥50 units/mg protein

manufacturer/tradename

Roche

manufacturer/tradename

Roche

manufacturer/tradename

Roche

manufacturer/tradename

-

optimum pH

7.5

optimum pH

9.2

optimum pH

7.0-8.5(maximal activity at 7.8)

optimum pH

-

Quality Level

100

Quality Level

100

Quality Level

100

Quality Level

-

packaging

pkg of 10 mg (60 mg lyophilizate)

packaging

pkg of 1 mL (5 mg/ml)

packaging

pkg of 1 mL (1,000 U)

packaging

-

General description

L-iditol:NAD+ 5′-oxidoreductase
Sorbitol dehydrogenase (SDH) from sheep liver has a molar mass of 152kDa. The protein is a tetramer of four identical subunits. Each of these subunits has 355 amino acid residues, of which 10 are cysteine residues. Each subunit contains a zinc atom at the active site, which is associated with three protein ligands and a water molecule. The zinc atom associates with the oxygen of the sorbitol hydroxyl or of the fructose carbonyl interconverted during catalysis.

Application

Reduces L-iditol to L-sorbose. Also acts on D-glucitol and other closely related sugar alcohols. Allows the reduction of ketones to polyols (see aldolases for the synthesis of ketoses).

Biochem/physiol Actions

Sorbitol dehydrogenase (SDH) catalyzes the reversible NAD-linked conversion of D-sorbitol to D-fructose and forms a part of the sorbitol pathway, which is a crucial bypass to glycolysis for glucose metabolism. This pathway has been found to be associated with the accumulation of sorbitol in lens, which results in diabetic cataractogenesis. SDH also oxidizes various polyols and other secondary alcohols into their corresponding ketones.

Quality

Contaminants: <0.01% ADH, <0.02% GIDH and glucose dehydrogenase, each, <0.05% LDH and MDH, each.

Unit Definition

One unit (U) sorbitol dehydrogenase will reduce 1 mol of D-fructose in one minute at +25 °C and pH 7.6 [triethanolamine buffer; 150 mM fructose (nonsaturating concentration)]. The above assay consumes 1 mol of NADH per mol of D-sorbitol formed.

Physical form

Lyophilizate (60 mg contain 10 mg enzyme protein and 50 mg maltose).

Preparation Note

Activator: The reactions (oxidation or reduction) are fastest in Tris or triethanolamine buffer.
Stabilizers: Maltose is used as stabilizer.
Storage conditions (working solution): An aqueous solution is stable at 2 to 8 °C for several weeks.

Storage and Stability

Store at 2 to 8 °C. (Store the lyophilizate dry.)

Other Notes

For life science research only. Not for use in diagnostic procedures.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

does not flash

Flash Point(C)

does not flash


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Customers Also Viewed

R I Lindstad et al.
European journal of biochemistry, 210(2), 641-647 (1992-12-01)
The relations between the kinetic parameters for both sorbitol oxidation and fructose reduction by sheep liver sorbitol dehydrogenase show that a Theorell-Chance compulsory order mechanism operates from pH 7.4 to 9.9. This is supported by many parallels with the kinetics
R I Lindstad et al.
The Biochemical journal, 330 ( Pt 1), 479-487 (1998-04-16)
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

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