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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

KM Value

KM Value on EC 2.4.1.20 - cellobiose phosphorylase

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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.5
1,5-anhydro-D-glucitol
-
pH 6.0, 37°C
8 - 9
1,5-anhydroglucitol
-
enzyme assay at 37°C in 50 mM Tris/HCl (pH 7.0)
17.2
2-deoxy-2-fluoro-D-glucose
-
-
24.3 - 250
2-deoxy-D-glucose
7.4
6-deoxy-6-fluoro-D-glucose
-
-
4.1 - 24
6-deoxy-D-glucose
1.46 - 30.7
alpha-D-glucose 1-phosphate
33.7
butyl beta-D-glucoside
-
mutant N156D/N163D/T508I/E649G/N667A, pH 6.6, 37°C
0.12 - 31.4
cellobiose
0.06
cellopentaose
at pH 7.5 and 75°C
0.062
cellotetraose
at pH 7.5 and 75°C
0.094
cellotriose
at pH 7.5 and 75°C
240
D-arabinose
-
-
2.6
D-cellobiose
-
-
10.8
D-gentobiose
-
pH 6.0, 37°C
5.7 - 58.1
D-glucosamine
0.69 - 28.9
D-glucose
10.8
D-glucoseamine
-
-
11.8 - 200
D-mannose
14 - 84
D-xylose
138 - 155
ethyl beta-D-glucoside
83
gentiobiose
-
enzyme assay at 37°C in 50 mM Tris/HCl (pH 7.0)
71
isomaltose
-
enzyme assay at 37°C in 50 mM Tris/HCl (pH 7.0)
160
L-fucose
-
-
228 - 330
lactose
93
melibiose
-
enzyme assay at 37°C in 50 mM Tris/HCl (pH 7.0)
1009
methyl alpha-D-glucoside
-
mutant N156D/N163D/T508I/E649G/N667A, pH 6.6, 37°C
56.6 - 79.8
methyl beta-D-glucoside
17.4
N-acetyl-D-glucosamine
-
mutant enzyme Y648V, at pH 6.0 and 37°C
31.2
phenyl beta-D-glucoside
-
mutant N156D/N163D/T508I/E649G/N667A, pH 6.6, 37°C
0.15 - 2.9
phosphate
additional information
additional information
-
simulation of molecular dynamics of the enzyme, the 1S3 pre-transition state conformer is highly stable compared with other conformers, and a conformational change from 4C1 to 1,4B occurs
-