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Enzyme Activity Measurement for Mannitol-1-Phosphate 5-Dehydrogenase Using Spectrophotometric Assays

Creative Enzymes is one of the few companies in the world that provide activity measurement for mannitol-1-phosphate 5-dehydrogenase by spectrophotometric assays. We are specialized in designing activity assays to satisfy the unmet needs of enzyme detection and characterization. Creative Enzymes is able to perform highly accurate and reproducible spectrophotometric assays for mannitol-1-phosphate 5-dehydrogenase with a well-developed method.

Mannitol-1-phosphate 5-dehydrogenase (EC is the enzyme producing D-fructose 6-phosphate (F6P) from D-mannitol 1-phosphate (M1P) and nicotinamide adenine dinucleotide (NAD+). It belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ and NADP+ (nicotinamide adenine dinucleotide phosphate), as the electron acceptor. This enzyme has considerably high substrate specificity toward F6P and M1P for respective reductive and oxidative reactions. It was found to be a sulfhydryl-type enzyme, because its activity is inhibited by N-ethylmaleimide and p-hydroxymercuribenzoate, and the inhibition could be rescued by 2-mercaptoethanol. The most significant function of this enzyme is acting as the key enzyme for regulating mannitol biosynthesis and participating in fructose and mannose metabolism. The systematic name of this enzyme class is D-mannitol-1-phosphate:NAD+ 2-oxidoreductase, although it also goes with other names:

Spectrophotometric assays are often used to quantify the enzymatic activity of mannitol-1-phosphate 5-dehydrogenase, because the reduction of NAD+ to NADH during oxidation of alcohols can be conveniently detected at 340 nm. Although a spectrophotometric assay method was reported as early as 1972 (Ikawa et al.), Creative Enzymes made modifications to bring the method up-to-date to meet the customer’s high standards. The F6P-reducing activity is measured by monitoring the disappearance of NADH at 340 nm, and the reaction is initiated by adding F6P, while the M1P-oxidizing activity is measured by monitoring the NADH formation and initiated by adding M1P.

Overall, Creative Enzymes is your trustworthy partner for spectrophotometric assays for mannitol-1-phosphate 5-dehydrogenases. We have been a lead company in the enzymatic assay of mannitol-1-phosphate 5-dehydrogenase. The reliability of the test results is based on our most advanced spectrophotometric instruments and the strong team of enzymologists.

Enzyme Activity Measurement for Mannitol-1-Phosphate 5-Dehydrogenase Using Spectrophotometric Assays Figure: The crystal structure of mannitol-1-phosphate dehydrogenase from Shigella flexneri.

Ikawa T, Watanabe T, Nisizawa K. Enzymes involved in the last steps of the biosynthesis of mannitol in brown algae. Plant and cell physiology, 1972, 13(6), 1017-1029.
Iwamoto K, Kawanobe H, Ikawa T, et al. Characterization of salt-regulated mannitol-1-phosphate dehydrogenase in the red alga Caloglossa continua. Plant physiology, 2003, 133(2), 893-900.

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