P2621
Phosphomannose Isomerase from Escherichia coli
recombinant, expressed in E. coli, ammonium sulfate suspension, ≥50 units/mg protein
Synonym(s):
D-Mannose-6-phosphate ketol-isomerase, Mannose Phosphate Isomerase, PMI
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About This Item
Specific activity:
≥50 units/mg protein
Recombinant:
expressed in E. coli
recombinant
expressed in E. coli
Quality Level
form
ammonium sulfate suspension
specific activity
≥50 units/mg protein
storage temp.
2-8°C
Application
PMI is used to study cell wall synthesis and energy production. PMI has been used to study how EDTA and metal ions, such as Zn++, Co++, Fe++, Mn++ and Cu++., can affect recovery and thermal stability. It may be used to study PMI′s effect on various alginate biosynthetic enzymes such as phosphomannomutase (PMM), GDP-mannose pyrophosphorylase (GMP), and GDP-mannose dehydrogenase (GMD).
Biochem/physiol Actions
Phosphomannose Isomerase (PMI) catalyses the interconversion of mannose 6-phosphate (Man-6-P) and fructose 6-phosphate (Fru-6-P), which provides a link between glucose metabolism and mannosylation.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Physical form
Supplied as a suspension in 3.2 M ammonium sulfate
Other Notes
One unit will convert 1.0 μmole of D-mannose 6-phosphate to D-fructose 6-phosphate per min at pH 7.6 at 25 °C, using a coupled enzyme system with phosphoglucose isomerase and glucose-6-phosphate dehydrogenase.
Storage Class
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Thangamani Rajesh et al.
Applied microbiology and biotechnology, 93(4), 1685-1693 (2011-09-29)
Phosphomannose isomerases (PMIs) in bacteria and fungi catalyze the reversible conversion of D-fructose-6-phosphate to D-mannose-6-phosphate during biosynthesis of GDP-mannose, which is the main intermediate in the mannosylation of important cell wall components, glycoproteins, and certain glycolipids. In the present study
Daisuke Tsuji et al.
Annals of neurology, 69(4), 691-701 (2011-04-27)
Novel recombinant human lysosomal β-hexosaminidase A (HexA) was developed for enzyme replacement therapy (ERT) for Tay-Sachs and Sandhoff diseases, ie, autosomal recessive GM2 gangliosidoses, caused by HexA deficiency. A recombinant human HexA (Om4HexA) with a high mannose 6-phosphate (M6P)-type-N-glycan content
Matthew R Amos et al.
Applied and environmental microbiology, 77(3), 776-785 (2010-12-15)
Extracellular polysaccharide (EPS) is produced by diverse bacterial pathogens and fulfills assorted roles, including providing a structural matrix for biofilm formation and more specific functions in virulence, such as protection against immune defenses. We report here the first investigation of