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Literature summary for 2.4.1.7 extracted from

  • Wildberger, P.; Todea, A.; Nidetzky, B.
    Probing enzyme substrate interactions at the catalytic subsite of Leuconostoc mesenteroides sucrose phosphorylase with site-directed mutagenesis: The roles of Asp (2012), Biocatal. Biotransform., 30, 326-337.
No PubMed abstract available

Protein Variants

Protein Variants Comment Organism
D49A site-directed mutagenesis, the mutant enzyme shows 10000000fold reduced enzyme glycosylation and 500fold reduced enzyme deglycosylation compared to the wild-type enzyme. The mutant also shows a loss in selectivity for phosphate against water and substrate inhibition by phosphate Leuconostoc mesenteroides
D49A/R395L site-directed mutagenesis, inactive mutant Leuconostoc mesenteroides
R395L site-directed mutagenesis, the mutant enzyme shows 100000fold reduced enzyme glycosylation and 500fold reduced enzyme deglycosylation compared to the wild-type enzyme. The mutant also shows a loss in selectivity for phosphate against water and substrate inhibition by phosphate Leuconostoc mesenteroides

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sucrose + phosphate Leuconostoc mesenteroides
-
D-fructose + alpha-D-glucose 1-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Leuconostoc mesenteroides
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + phosphate
-
Leuconostoc mesenteroides D-fructose + alpha-D-glucose 1-phosphate
-
?
sucrose + phosphate the transferred glucosyl moiety of sucrose is accomodated at the catalytic subsite of the phosphorylase through a network of charged hydrogen bonds, conserved residues Asp49 and Arg395 are pointing towards the equatorial hydroxyl at C4 which is essential for catalytic efficiency, overview Leuconostoc mesenteroides D-fructose + alpha-D-glucose 1-phosphate
-
?

General Information

General Information Comment Organism
physiological function sucrose phosphorylase is a bacterial alpha-transglucosidase that catalyses glucosyl transfer from sucrose to phosphate, releasing D-fructose and alpha-glucose 1-phosphate as product of the first enzyme glycosylation step and second enzyme deglycosylation step of the enzymatic reaction, respectively Leuconostoc mesenteroides