Product Name
Maltose Phosphorylase from Enterococcus sp., recombinant, expressed in E. coli, lyophilized powder
SMILES string
OC(=O)CCCCCCCCCCCCC
InChI key
TUNFSRHWOTWDNC-UHFFFAOYSA-N
InChI
1S/C14H28O2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14(15)16/h2-13H2,1H3,(H,15,16)
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
Related Categories
Biochem/physiol Actions
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.
Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes maltose and inorganic phosphate into β-D-glucose-1-phosphate and glucose.
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.
Other Notes
Contains lactose.
One unit will produce 1.0 μmole of D-Glucose from maltose per minute at pH 7.0 at 30°C.
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.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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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.
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
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
Hiroyuki Nakai et al.
Carbohydrate research, 345(8), 1061-1064 (2010-04-16)
Lactobacillus acidophilus NCFM maltose phosphorylase (LaMalP) of glycoside hydrolase family 65 catalysed enzymatic synthesis of alpha-(1-->4)-glucosidic disaccharides from maltose and five monosaccharides in a coupled phosphorolysis/reverse phosphorolysis one-pot reaction. Thus phosphorolysis of maltose to beta-glucose 1-phosphate circumvented addition of costly
M Tangney et al.
FEMS microbiology letters, 76(1-2), 191-196 (1992-10-01)
Extracts prepared from cultures of Bacillus subtilis, grown on maltose as the sole carbon source, lacked maltose phosphotransferase system activity. There was, however, evidence for a maltose phosphorylase activity, and such extracts also possessed both glucokinase and glucose phosphotransferase system
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