S0937
Sucrose Phosphorylase
recombinant, expressed in E. coli, lyophilized powder, ≥45 units/mg solid
Synonym(s):
SPase, disaccharide glucosyltransferase, sucrose glucosyltransferase, Sucrose:orthophosphate α-D-glucosytransferase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
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recombinant
expressed in E. coli
Quality Level
form
lyophilized powder
specific activity
≥45 units/mg solid
mol wt
56 kDa by SDS-PAGE
shipped in
wet ice
storage temp.
−20°C
General description
Research area: Cell signaling
Sucrose Phosphorylase belongs to glycoside hydrolase, GH13 family. It comprises of four domains with the glucose anomeric carbon-binding site and a glucoside-binding site. The active site residues include Asp192 and Glu232. It is majorly produced by bifidobacteria and lactic acid bacteria. The cross-linked sucrose phosphorylase aggregates is thermostable and could be exploited for industrial catalysis of glycosylation.
Sucrose Phosphorylase belongs to glycoside hydrolase, GH13 family. It comprises of four domains with the glucose anomeric carbon-binding site and a glucoside-binding site. The active site residues include Asp192 and Glu232. It is majorly produced by bifidobacteria and lactic acid bacteria. The cross-linked sucrose phosphorylase aggregates is thermostable and could be exploited for industrial catalysis of glycosylation.
Application
Sucrose Phosphorylase has been used in sucrose determination in wheat plant and in sucrose hydrogen production.
Sucrose phosphorylase has been used:
- To assess the enzymatic synthesis of stable, odorless, and powdered furanone glucosides.
- To investigate the novel transglucosylating reaction with carboxylic compounds.
- In sucrose determination in wheat plant and in sucrose hydrogen production.
Biochem/physiol Actions
Sucrose phosphorylase catalyzes the reversible conversion of sucrose (α-D-glucopyranosyl-1,2-β-D-fructofuranoside) and phosphate into D-fructose and α-D-glucose 1-phosphate. This reaction plays a crucial role in generating the vital glucose component through sucrose metabolism.(1)
Unit Definition
One unit will produce 1.0 μmole of D-fructose from sucrose per min with the corresponding reduction of NADP to NADPH at pH 7.6, at 25 °C.
Physical form
Contains sucrose as stabilizer.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
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Koji Nomura et al.
Bioscience, biotechnology, and biochemistry, 72(1), 82-87 (2008-01-08)
Transglucosylation from sucrose to acetic acid by sucrose phosphorylase (EC 2.4.1.7) was studied. 1-O-Acetyl-alpha-D-glucopyranose was isolated as the main product of the enzyme reaction. We also compared the pH-dependence of transglycosylation catalyzed by sucrose phosphorylase toward carboxyl and hydroxyl groups.
Alexandra Schwarz et al.
The Biochemical journal, 403(3), 441-449 (2007-01-20)
The role of acid-base catalysis in the two-step enzymatic mechanism of alpha-retaining glucosyl transfer by Leuconostoc mesenteroides sucrose phosphorylase has been examined through site-directed replacement of the putative catalytic Glu237 and detailed comparison of purified wild-type and Glu237-->Gln mutant enzymes
Kazuhisa Sugimoto et al.
Journal of bioscience and bioengineering, 104(1), 22-29 (2007-08-19)
We examined the synthesis of benzoyl glucoside using the transglucosylation reaction of sucrose phosphorylase. Sucrose phosphorylase from Streptococcus mutans showed marked transglucosylating activity, particularly under acidic conditions. On the other hand, sucrose phosphorylase from Leuconostoc mesenteroides showed very weak transglucosylating
Structural rearrangements of sucrose phosphorylase from Bifidobacterium adolescentis during sucrose conversion
Mirza O, et al.
The Journal of Biological Chemistry, 281(46), 35576-35584 (2006)
Mamoru Nishimoto et al.
Carbohydrate research, 344(18), 2573-2576 (2009-10-24)
Beta-D-Galactopyranosyl-(1-->3)-2-acetamido-2-deoxy-D-galactose (galacto-N-biose, GNB) is an important core structure in functional sugar chains such as T-antigen disaccharide and the core 1 sugar chain in mucin glycoproteins. We successfully developed a one-pot enzymatic production of GNB from sucrose and GalNAc by the
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