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Enzyme Activity Measurement for Mannose-1-Phosphate Guanylyltransferase

Creative Enzymes provides the most precise activity measurement for mannose-1-phosphate guanylyltransferase to the customers. We are a group of brilliant scientists who have been working on enzyme activity assays for many years. The unique advantage of our spectrophotometric analysis allows us to surpass our competitors and assures the reliability of the test results.

GDP-mannose (GDP-Man), an activated form of mannose, plays a key role in the biosynthetic pathway that produces the N-linked oligosaccharides of many membrane and secretory glycoproteins of eukaryotic cells. Activation of mannose requires three enzymes: phosphomannose isomerase (PMI), phosphomannomutase, and mannose-1-phosphate guanylyltransferase (EC Mannose-1-phosphate guanylyltransferase, a vital enzyme for the production of mannose-containing glycoconjugates, such as protein N- and C-glycans, glycosylphosphatidylinositol protein, and some glycolipid membrane anchors, is known to have multiple important biological functions. This enzyme catalyzes the synthesis of GDP-Man from mannose 1-phosphate (Man-1-P) and GTP. Note that most of the mannose-1-phosphate guanylyltransferases require a bivalent cation for catalysis.

Mannose-1-phosphate guanylyltransferase is a member of the nucleotidyl transfevitrase family of enzymes. This enzyme was partially purified and first characterized from Athrobacter sp. in 1964. Since then, the enzyme has been purified from a wide range of organisms and tissues such as Pseudomonas aeruginosa, Mycobacterium smegmatis, mammary gland and pig liver. Interestingly, mannose-1-phosphate guanylyltransferase from P. aeruginosa is a bifunctional enzyme that has both mannose-1-phosphate guanylyltransferase and phosphomannose isomerase activities.

Enzyme Activity Measurement for Mannose-1-Phosphate Guanylyltransferase Figure 1: The reaction catalyzed by mannose-1-phosphate guanylyltransferase.
Reference: Davis A J, et al. Journal of Biological Chemistry, 2004, 279(13): 12462-12468.

Importantly, mannose-1-phosphate guanylyltransferase serves as a potential target for the design of antimicrobial drugs. Besides, this enzyme can also be used as a target for inhibitor design for anti-leishmanial therapy. Therefore, it is quite important to detect the activity of mannose-1-phosphate guanylyltransferase.

Creative Enzymes, relying on its superb expert team and devoted to developing robust activity analysis, is committed to acting as a globally recognized leader in the field of enzyme activity assays. We are fully prepared to make the most accurate enzymatic assays availalble to customers. The enzyme activity is measured using a colorimetric assay coupled with inorganic pyrophosphatase. The inorganic pyrophosphate generated in the reaction is subsequently converted to inorganic phosphate by consumption of inorganic pyrophosphatase. The increase in the concentration of inorganic phosphate, showing the activity of mannose-1-phosphate guanylyltransferase, is determined by measuring the absorbance at 650 nm spectrophotometrically. Our test results are the most trusted and proven in the market, and have been welcomed by thousands of customers in the past several years. Overall, Creative Enzymes is your trustworthy partner and always looks forward to collaborating with you sincerely.

Enzyme Activity Measurement for Mannose-1-Phosphate Guanylyltransferase Figure 2: The crystal structure of mannose-1-phosphate guanylyltransferase from Thermotoga maritima.

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SourceE. coli
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