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
form
ammonium sulfate suspension
specific activity
≥50 units/mg protein
storage temp.
2-8°C
Quality Level
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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Studies on the phosphomannose isomerase of Amorphophallus konjac C. Koch II. Effect of divalent metal ions on the EDTA-treated enzyme
Takao Murata
Plant & Cell Physiology, 16, 963-970 (1975)
Michael Newcomb et al.
Applied microbiology and biotechnology, 90(2), 625-634 (2011-02-15)
Clostridium thermocellum, an anaerobic, thermophilic, and ethanogenic bacterium produces a large cellulase complex termed the cellulosome and many free glycosyl hydrolases. Most cellulase genes scatter around the genome. We mapped the transcripts of the six-gene cluster celC-glyR3-licA-orf4-manB-celT and determined their
Stéphanie Desvergnes et al.
Bioorganic & medicinal chemistry, 20(4), 1511-1520 (2012-01-25)
In the design of inhibitors of phosphosugar metabolizing enzymes and receptors with therapeutic interest, malonate has been reported in a number of cases as a good and hydrolytically-stable surrogate of the phosphate group, since both functions are dianionic at physiological
Russell Dahl et al.
Journal of medicinal chemistry, 54(10), 3661-3668 (2011-05-05)
We report the discovery and validation of a series of benzoisothiazolones as potent inhibitors of phosphomannose isomerase (PMI), an enzyme that converts mannose-6-phosphate (Man-6-P) into fructose-6-phosphate (Fru-6-P) and, more importantly, competes with phosphomannomutase 2 (PMM2) for Man-6-P, diverting this substrate
Craig T Narasaki et al.
PloS one, 6(10), e25514-e25514 (2011-11-09)
Coxiella burnetii, the etiologic agent of human Q fever, is a gram-negative and naturally obligate intracellular bacterium. The O-specific polysaccharide chain (O-PS) of the lipopolysaccharide (LPS) of C. burnetii is considered a heteropolymer of the two unusual sugars β-D-virenose and
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