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Phosphomannose isomerase (Escherichia coli)

Product code: E-PMIEC

1,000 Units

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Content: 1,000 Units
Shipping Temperature: Ambient
Storage Temperature: 2-8oC
Formulation: In 3.2 M ammonium sulphate
Physical Form: Suspension
Stability: > 1 year under recommended storage conditions
Enzyme Activity: Isomerase
EC Number:
CAS Number: 9023-88-5
Synonyms: mannose-6-phosphate isomerase; D-mannose-6-phosphate aldose-ketose-isomerase
Source: Escherichia coli
Molecular Weight: 43,915
Concentration: Supplied at ~ 500 U/mL
Expression: Recombinant from Escherichia coli
Specificity: Catalyses the reaction:
D-Mannose 6-phosphate = D-fructose 6-phosphate
Specific Activity: ~ 100 U/mg (25oC, pH 7.6 on mannose 6-phosphate)
Unit Definition: One Unit of phosphomannose isomerase activity is defined as the amount of enzyme required to release one µmole of fructose 6-phosphate from mannose 6-phosphate (3.14 mM) per minute in the presence of NAD+ at pH 7.6 and 25oC.
Temperature Optima: 40oC
pH Optima: 7.6
Application examples: Applications for the measurement of D-mannose in carbohydrate research and in the food and feeds, fermentation, wine, beverage and dairy industries.

High purity recombinant Phosphomannose isomerase (Escherichia coli) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

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Enterococcus faecalis α1-2‐mannosidase (EfMan‐I): an efficient catalyst for glycoprotein N‐glycan modification.

Li, Y., Li, R., Yu, H., Sheng, X., Wang, J., Fisher, A. J. & Chen, X. (2020). FEBS Letters, 594(3), 439-451.

While multiple α 1-2‐mannosidases are necessary for glycoprotein N‐glycan maturation in vertebrates, a single bacterial α1-2‐mannosidase can be sufficient to cleave all α1-2‐linked mannose residues in host glycoprotein N‐glycans. We report here the characterization and crystal structure of a new α1-2‐mannosidase (EfMan‐I) from Enterococcus faecalis, a Gram‐positive opportunistic human pathogen. EfMan‐I catalyzes the cleavage of α1-2‐mannose from not only oligomannoses but also high‐mannose‐type N‐glycans on glycoproteins. Its 2.15 Å resolution crystal structure reveals a two‐domain enzyme fold similar to other CAZy GH92 mannosidases. An unexpected potassium ion was observed bridging two domains near the active site. These findings support EfMan‐I as an effective catalyst for in vitro N‐glycan modification of glycoproteins with high‐mannose‐type N‐glycans.

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