M8284
Maltose Phosphorylase from Enterococcus sp.
recombinant, expressed in E. coli, lyophilized powder
Synonyma:
Maltose:orthophosphate 1-β-D-Glucosyltransferase
Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
About This Item
Doporučené produkty
recombinant
expressed in E. coli
form
lyophilized powder
specific activity
≥9 units/mg solid
mol wt
90 kDa by SDS-PAGE
storage temp.
−20°C
Související kategorie
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
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Zákazníci si také prohlíželi
Ulrika Andersson et al.
BMC microbiology, 2, 28-28 (2002-09-26)
Maltose metabolism is initiated by an ATP-dependent permease system in Lactococcus lactis. The subsequent degradation of intracellular maltose is performed by the concerted action of Pi-dependent maltose phosphorylase and beta-phosphoglucomutase. In some Gram-positive bacteria, maltose metabolism is regulated by a
Vladimir Privman et al.
The journal of physical chemistry. B, 113(15), 5301-5310 (2009-04-10)
We develop an approach aimed at optimizing the parameters of a network of biochemical logic gates for reduction of the "analog" noise buildup. Experiments for three coupled enzymatic AND gates are reported, illustrating our procedure. Specifically, starch, one of the
M P Egloff et al.
Structure (London, England : 1993), 9(8), 689-697 (2001-10-06)
Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose without requiring any cofactors, such as pyridoxal phosphate. The enzyme is part of operons that are involved in maltose/malto-oligosaccharide metabolism.
Y Inoue et al.
Bioscience, biotechnology, and biochemistry, 65(12), 2644-2649 (2002-02-06)
Bacillus sp. RK-1 was isolated as a bacterium that produced maltose phosphorylase (MPase) in the culture supernatant. Screening was done from among about 400 isolates that could grow at 55 degrees C in a medium containing maltose as the sole
Zhiqiang Zhang et al.
Analytica chimica acta, 615(1), 73-79 (2008-04-29)
A conductometric biosensor for phosphate detection was developed using maltose phosphorylase (MP) from recombinant Escherichia coli immobilized on a planar interdigitated electrode by cross-linking with saturated glutaraldehyde (GA) vapour in the presence of bovine serum albumin (BSA). The process parameters
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