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2.4.1.64: alpha,alpha-trehalose phosphorylase

This is an abbreviated version!
For detailed information about alpha,alpha-trehalose phosphorylase, go to the full flat file.

Word Map on EC 2.4.1.64

Reaction

alpha,alpha-trehalose
+
phosphate
=
D-glucose
 +
beta-D-glucose 1-phosphate

Synonyms

Bsel_1207, inverting trehalose phosphorylase, phosphorylase, trehalose, TbTP, trehalose phosphorylase

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.64 alpha,alpha-trehalose phosphorylase

Engineering

Engineering on EC 2.4.1.64 - alpha,alpha-trehalose phosphorylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L649G
-
the mutant shows severely reduced production of beta-D-glucose 1-phosphate compared to the wild type enzyme
L649G/A693Q
-
the mutant shows severely reduced production of beta-D-glucose 1-phosphate compared to the wild type enzyme
L649G/A693Q/W371Y
-
the mutant shows severely reduced production of beta-D-glucose 1-phosphate compared to the wild type enzyme but displays a strict specificity (99%) for beta-D-galactose 1-phosphate as product
A431T
the mutant shows strongly decreased catalytic efficiency for D-glucose and decreased catalytic efficiency for D-galactose compared to the wild type enzyme
A440E
the mutant shows increased catalytic efficiency for D-glucose and wild type catalytic efficiency for D-galactose compared to the wild type enzyme
A440K
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440M
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440V
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440V/N657Y
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
A440V/R448S
the mutant shows increased catalytic efficiency for D-glucose and strongly increased catalytic efficiency for D-galactose compared to the wild type enzyme
N657D
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657G
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657I
the mutant shows approximate 2fold increase in affinity for D-galactose
N657L
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657R
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
N657Y
the mutant shows approximate 2fold increase in affinity for D-galactose
P588H
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448D
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448F
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448N
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448S
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
R448S/N657Y
the mutant shows about wild type catalytic efficiencies for D-glucose and D-galactose
R448V
the mutant shows increased catalytic efficiencies for D-glucose and D-galactose compared to the wild type enzyme
additional information
-
construction of chimeric phosphorylases of the kojibiose phosphorylase gene and the trehalose phosphorylase gene from Thermoanaerobacter brockii