M8284
Maltose Phosphorylase from Enterococcus sp.
recombinant, expressed in E. coli, lyophilized powder
Synonym(s):
Maltose:orthophosphate 1-β-D-Glucosyltransferase
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About This Item
Recommended Products
recombinant
expressed in E. coli
Quality Level
form
lyophilized powder
specific activity
≥9 units/mg solid
mol wt
90 kDa by SDS-PAGE
storage temp.
−20°C
Related Categories
General description
Maltose phosphorylase (MP) is a dimeric enzyme. This enzyme is classified under family 65 of the glycoside hydrolases. It is a member of the disaccharide phosphorylase family.
Application
Maltose Phosphorylase from Enterococcus sp. has been used as a component in coupled assay and ATPase activity assay to study its effects on ATPase activity, on the 90 kDa heat shock proteins (Hsp90) ATPase reaction and on background absorbance on the production of resorufin.
Maltose phosphorylase from Enterococcus has been used in a study to describe a new pathway for maltose utilization in lactic acid bacteria. It has also been used in a study to describe the transfer of glucosyl moiety of maltose to acceptors with alcoholic OH groups.
Biochem/physiol Actions
Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes maltose and inorganic phosphate into β-D-glucose-1-phosphate and glucose.
Maltose phosphorylase not only transfers glucosyl moieties from maltose to other sugars but has been shown to also use phenolic compounds such as salicyl alcohol as acceptors.
Enzymatically converts maltose to D-Glucose.
Unit Definition
One unit will produce 1.0 μmole of D-Glucose from maltose per minute at pH 7.0 at 30°C.
Other Notes
Contains lactose.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Yasushi Inoue et al.
Bioscience, biotechnology, and biochemistry, 66(12), 2594-2599 (2003-02-25)
The maltose phosphorylase (MPase) gene of Bacillus sp. strain RK-1 was cloned by PCR with oligonucleotide primers designed on the basis of a partial N-terminal amino acid sequence of the purified enzyme. The MPase gene consisted of 2,655 bp encoding
Christopher Avila et al.
Bioorganic & medicinal chemistry, 14(4), 1134-1142 (2005-10-11)
The Hsp90 molecular chaperone is responsible for the conformational maturation of nascent polypeptides and the rematuration of denatured proteins. Inhibition of Hsp90 represents a promising approach towards the treatment of cancer because numerous signaling cascades can be simultaneously targeted by
Stefan de Kok et al.
Metabolic engineering, 13(5), 518-526 (2011-06-21)
Increasing free-energy conservation from the conversion of substrate into product is crucial for further development of many biotechnological processes. In theory, replacing the hydrolysis of disaccharides by a phosphorolytic cleavage reaction provides an opportunity to increase the ATP yield on
Ulrika Andersson et al.
Environmental microbiology, 4(2), 81-88 (2002-04-26)
Maltose and trehalose catabolic pathways are linked through their common enzyme, beta-phosphoglucomutase, and metabolite, beta-glucose 1-phosphate, in Lactococcus lactis. Maltose is degraded by the concerted action of maltose phosphorylase and beta-phosphoglucomutase, whereas trehalose is assimilated by a novel pathway, including
Ana D Simonović et al.
Analytical biochemistry, 334(2), 312-317 (2004-10-21)
The phosphate precipitation reaction using ammonium molybdate and triethylamine under low pH has been applied to gel-based assays for detecting phosphate-releasing enzymes. The sensitivity of the assay is 10 pmol Pi/mm2 of 1.5-mm-thick gel. The assay is applicable to enzymes
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