Mannitol 2-dehydrogenase (NADP )
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Mannitol 2-dehydrogenase (NADP )
In enzymology, a mannitol 2-dehydrogenase () is an enzyme that catalysis, catalyzes the chemical reaction :D-mannitol + NAD+ \rightleftharpoons D-fructose + NADH + H+ Thus, the two substrate (biochemistry), substrates of this enzyme are D-mannitol and nicotinamide adenine dinucleotide, NAD+, whereas its 3 product (chemistry), products are D-fructose, nicotinamide adenine dinucleotide, NADH, and hydrogen ion, H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The List of enzymes, systematic name of this enzyme class is D-mannitol:NAD+ 2-oxidoreductase. Other names in common use include D-mannitol dehydrogenase, and mannitol dehydrogenase. This enzyme participates in Fructose metabolism, fructose and mannose metabolism. Structural studies As of late 2007, two tertiary structure, structures have been solved for this class of enzymes, with Protein Data Bank, PDB accession codes and . Refer ...
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Enzymology
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ...
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