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Literature summary for 2.4.1.7 extracted from

  • De Winter, K.; Soetaert, W.; Desmet, T.
    An imprinted cross-linked enzyme aggregate (iCLEA) of sucrose phosphorylase: combining improved stability with altered specificity (2012), Int. J. Mol. Sci., 13, 11333-11342.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.7

Cloned(Commentary)

Cloned (Comment) Organism
recombinnat expression in Escherichia coli Bifidobacterium adolescentis

Protein Variants

Protein Variants Comment Organism
additional information formation of a glutaraldehyde cross-linked enzyme aggregate for high improvement of the enzyme's stability at 60°C, molecular imprinting of the cross-linked enzyme aggregate with a suitable substrate, i.e. glycerol, involving enzyme precipitation by tert-butyl alcohol can 2fold increase the transglucosylation activity, stability and specificity of the modified enzyme, method, overview. The modified enzyme is more useful as industrial biocatalyst than the native enzyme 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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme partially from Escherichia coli via heat treatment removing the contaminating phosphatase activity Bifidobacterium adolescentis

Substrates and Products (Substrate)

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