Biomaterial Database

Kinetic analysis of rat liver sorbitol dehydrogenase. 1983

N C Leissing, and E T McGuinness

1. A steady state kinetic investigation was performed on an improved preparation of rat-liver sorbitol dehydrogenase (L-iditol: NAD-oxidoreductase, EC 1.1.1.14). 2. Data analyses indicate the enzyme follows a rapid equilibrium random mechanism in the direction of sorbitol oxidation and a random mechanism in the direction of fructose reduction. 3. Kinetic constants were: K m NAD 0.082 mM; K m sorbitol 0.38 mM; K m NADH 67 microns; K m fructose 136 mM. 4. Evidence is adduced to indicate the more rapid reverse (fructose reduction) reaction is susceptible to metabolic control by formation of abortive enzyme fructose-NAD and enzyme-NADH-sorbitol complexes.

UI	MeSH Term	Description	Entries
D007064	L-Iditol 2-Dehydrogenase	An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14	Iditol Dehydrogenase,Sorbitol Dehydrogenase,Polyol Dehydrogenase,2-Dehydrogenase, L-Iditol,Dehydrogenase, Iditol,Dehydrogenase, Polyol,Dehydrogenase, Sorbitol,L Iditol 2 Dehydrogenase
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008099	Liver	A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.	Livers
D008956	Models, Chemical	Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.	Chemical Models,Chemical Model,Model, Chemical
D009243	NAD	A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)	Coenzyme I,DPN,Diphosphopyridine Nucleotide,Nadide,Nicotinamide-Adenine Dinucleotide,Dihydronicotinamide Adenine Dinucleotide,NADH,Adenine Dinucleotide, Dihydronicotinamide,Dinucleotide, Dihydronicotinamide Adenine,Dinucleotide, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide,Nucleotide, Diphosphopyridine
D010084	Oxidation-Reduction	A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).	Redox,Oxidation Reduction
D002621	Chemistry	A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D013379	Substrate Specificity	A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.	Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D013401	Sugar Alcohol Dehydrogenases	Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.	Sugar Alcohol Oxidoreductases,Alcohol Dehydrogenases, Sugar,Alcohol Oxidoreductases, Sugar,Dehydrogenases, Sugar Alcohol,Oxidoreductases, Sugar Alcohol