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2.4.1.20: cellobiose phosphorylase

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

Word Map on EC 2.4.1.20

Reaction

cellobiose
+
phosphate
=
alpha-D-glucose 1-phosphate
 +
D-glucose

Synonyms

Cbp, CbpA, cellobiose phosphorylase A, cellobiose:orthophosphate alpha-D-glucosyltransferase, CPase, CuCbP, GH94 cellobiose phosphorylase, lactose phosphorylase, ra2122, THA_1941, Tm_1848

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.20 cellobiose phosphorylase

Engineering

Engineering on EC 2.4.1.20 - cellobiose phosphorylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A423S
-
mutation introduced to increase thermostability, mutant displays a half-life of 11.3 min at 70°C
A781K
-
mutation introduced to increase thermostability, mutant displays a half-life of 15.3 min at 70°C
Q130H/K131Y/S411G/A423S/A781K
-
mutations introduced to increase thermostability, mutant displays a half-life of 17.7 min at 70°C
R48R/Q130H/K131Y/K142R/S411G/A423S/V526A/A781K
-
mutations introduced to increase thermostability, mutant displays a half-life of 24.6 min at 70°C
S411G
-
mutation introduced to increase thermostability, mutant displays a half-life of 13.6 min at 70°C
A397V
random, site-saturation, and site-directed mutagenesis, the mutant enzyme shows reduced activity with lactose compared to the wild-type enzyme
A397V/T508A/A512T/D557N/N667T/G681S
random, site-saturation, and site-directed mutagenesis, the mutant enzyme shows 3fold increased activity with lactose and 6fold decreased activity with cellobiose compared to the wild-type enzyme
A512T
random, site-saturation, and site-directed mutagenesis, the mutant enzyme shows similar activity with lactose compared to the wild-type enzyme
D557N
random, site-saturation, and site-directed mutagenesis, the mutant enzyme shows similar activity with lactose compared to the wild-type enzyme
E649C
-
mutant accepts methyl beta-D-glucoside and ethyl beta-D-glucoside as substrates
G681S
random, site-saturation, and site-directed mutagenesis, the mutant enzyme shows reduced activity with lactose compared to the wild-type enzyme
N156D/N163D/T508I/E649G/N667A
-
mutant with very broad acceptor specificity
T508A/N667T
random, site-saturation, and site-directed mutagenesis, the mutant enzyme shows increased activity with lactose compared to the wild-type enzyme
T508I/E649C/N667A
-
triple mutation broadens acceptor specificity
T508I/N667A
C485A
-
the mutant shows 43% of wild type activity with cellobiose. The mutant shows higher preference for D-glucosamine than the wild type enzyme
E654A
-
inactive
E654D
-
inactive
Y648A
-
inactive
Y648F
-
The mutant shows 23% of wild type activity with cellobiose. Apparent kcat/Km values of the mutant for D-mannose and 2-deoxy-D-glucose are 8.2 and 4.0fold higher than those of the wild type enzyme, respectively
Y648V
-
the mutant shows 0.888% of wild type activity with cellobiose and has synthetic activity toward N-acetyl-D-glucosamine
Y47H
-
the mutation is responsible for improved cellobiose consumption in the presence of xylose. The mutation alters the conformation of the enzyme dimer complex to reduce xylose binding to the active site
Y47H/K256/E270D/I384L/N488D/N578S/Y631F
-
the mutant strain shows improved growth and cellobiose consumption in comparison to the strain expressing wild type enzyme
additional information