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Literature summary for 2.4.1.8 extracted from

  • Zhang, Z.; Jaffrezic-Renault, N.; Bessueille, F.; Leonard, D.; Xia, S.; Wang, X.; Chen, L.; Zhao, J.
    Development of a conductometric phosphate biosensor based on tri-layer maltose phosphorylase composite films (2008), Anal. Chim. Acta, 615, 73-79.
    View publication on PubMed

Application

Application Comment Organism
analysis usage of the enzyme for a conductometric specific phosphate biosensor, method development and evaluation, overview Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression in Escherichia coli Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information development of a conductometric specific phosphate biosensor based on tri-layer maltose phosphorylase composite films, recombinant enzyme from Escherichia coli is immobilized on a planar interdigitated electrode by cross-linking with saturated glutaraldehyde vapour in the presence of bovine serum albumin, method development and evaluation, overview Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
maltose + phosphate Escherichia coli
-
D-glucose + beta-D-glucose 1-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
maltose + phosphate
-
Escherichia coli D-glucose + beta-D-glucose 1-phosphate
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
39
-
biosensor Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
the enzyme activity is strongly affected by the buffer solution pH, overview Escherichia coli
6
-
assay at, biosensor Escherichia coli