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Literature summary for 2.4.1.7 extracted from

  • De Winter, K.; Verlinden, K.; Kren, V.; Weignerova¡, L.; Soetaert, W.; Desmet, T.
    Ionic liquids as cosolvents for glycosylation by sucrose phosphorylase: balancing acceptor solubility and enzyme stability (2013), Green Chem., 15, 1949-1955.
No PubMed abstract available
Search for more literature for 2.4.1.7

Protein Variants

Protein Variants Comment Organism
additional information construction of s stabilized enzyme mutant LNFI through 6 point mutations Bifidobacterium adolescentis

General Stability

General Stability Organism
half-lives of the enzyme at pH 6.5 and 60°C, in the presence of 20% of different cosolvents and 1 M sucrose, overview Bifidobacterium adolescentis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sucrose + phosphate Bifidobacterium adolescentis
-
 D-fructose + alpha-D-glucose 1-phosphate
-
 r

Organism

Organism UniProt Comment Textmining
Bifidobacterium adolescentis Q84HQ2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
resveratrol + alpha-D-glucose 1-phosphate establishing of a resveratrol glycosylation method using the enzyme and IL AMMOENG 101 as the most effective cosolvent, solubility at pH 6.5 and 60°C, in the presence of 20% of different cosolvents and 1 M sucrose, overview Bifidobacterium adolescentis 3-O-alpha-D-glucopyranosyl-(E)-resveratrol + phosphate
-
 r
sucrose + phosphate
-
 Bifidobacterium adolescentis D-fructose + alpha-D-glucose 1-phosphate
-
 r

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Bifidobacterium adolescentis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
 Bifidobacterium adolescentis