P2621
Phosphomannose Isomerase from Escherichia coli
recombinant, expressed in E. coli, ammonium sulfate suspension, ≥50 units/mg protein
Sinónimos:
D-Mannose-6-phosphate ketol-isomerase, Mannose Phosphate Isomerase, PMI
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Specific activity:
≥50 units/mg protein
Recombinant:
expressed in E. coli
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Permítanos ayudarlerecombinant
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.
Clase de almacenamiento
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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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
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
Shanna Sichwart et al.
Applied and environmental microbiology, 77(4), 1325-1334 (2010-12-21)
The gram-negative facultative chemolithoautotrophic bacterium Ralstonia eutropha strain H16 is known for its narrow carbohydrate utilization range, which limits its use for biotechnological production of polyhydroxyalkanoates and possibly other products from renewable resources. To broaden its substrate utilization range, which
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
I Sá-Correia et al.
Journal of bacteriology, 169(7), 3224-3231 (1987-07-01)
The specific activities of phosphomannose isomerase (PMI), phosphomannomutase (PMM), GDP-mannose pyrophosphorylase (GMP), and GDP-mannose dehydrogenase (GMD) were compared in a mucoid cystic fibrosis isolate of Pseudomonas aeruginosa and in two spontaneous nonmucoid revertants. In both revertants some or all of
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