Information on EC 2.4.1.247 - beta-D-galactosyl-(1->4)-L-rhamnose phosphorylase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.247
-
RECOMMENDED NAME
GeneOntology No.
beta-D-galactosyl-(1->4)-L-rhamnose phosphorylase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
beta-D-galactosyl-(1->4)-L-rhamnose + phosphate = L-rhamnose + alpha-D-galactose 1-phosphate
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-D-galactosyl-(1->4)-L-rhamnose:phosphate 1-alpha-D-galactosyltransferase
The enzyme from Clostridium phytofermentans is also active towards towards beta-D-galactosyl derivatives of L-mannose, L-lyxose, D-glucose, 2-deoxy-D-glucose, and D-galactose in this order. Differs from 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase (EC 2.4.1.211) in being active towards L-rhamnose and inactive towards N-acetyl hexosamine derivatives.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bacterium possesses three GalHexNAcP homologous genes, cphy1920 gene; anaerobic cellulolytic bacterium
UniProt
Manually annotated by BRENDA team
gene oter 1377
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme belongs to the glycoside hydrolase family 112
physiological function
-
GalRhaPOt may be involved in rhamnogalacturonan I, in pectin, metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-glucose + alpha-D-galactose 1-phosphate
beta-D-galactosyl-(1->4)-2-deoxy-D-glucose + phosphate
show the reaction diagram
-
reverse (synthetic) reaction
-
-
r
2-deoxy-D-glucose + alpha-D-galactose 1-phosphate
D-galactosyl-beta-1,3-2-deoxy-D-glucose + phosphate
show the reaction diagram
when D-glucose derivatives are used as acceptors, reaction products are beta-1,3-galactosides
-
-
r
alpha-D-galactose 1-phosphate + L-rhamnose
D-galactosyl-beta-1,4-L-rhamnose + phosphate
show the reaction diagram
highest activity
-
-
r
beta-D-galactosyl-(1->3)-D-glucose + phosphate
D-glucose + alpha-D-galactose 1-phosphate
show the reaction diagram
-
lower activity
-
-
r
beta-D-galactosyl-(1->4)-L-rhamnose + phosphate
L-rhamnose + alpha-D-galactose 1-phosphate
show the reaction diagram
D-galactose + alpha-D-galactose 1-phosphate
beta-D-galactosyl-(1->4)-D-galactose + phosphate
show the reaction diagram
-
reverse (synthetic) reaction
-
-
r
D-galactose + alpha-D-galactose 1-phosphate
D-galactosyl-beta-1,3-D-galactose + phosphate
show the reaction diagram
-
-
-
r
D-glucose + alpha-D-galactose 1-phosphate
beta-D-galactosyl-(1->4)-D-glucose + phosphate
show the reaction diagram
-
reverse (synthetic) reaction
-
-
r
D-glucose + alpha-D-galactose 1-phosphate
D-galactosyl-beta-1,3-D-glucose + phosphate
show the reaction diagram
when D-glucose derivatives are used as acceptors, reaction products are beta-1,3-galactosides
-
-
r
D-xylose + alpha-D-galactose 1-phosphate
beta-D-galactosyl-(1->4)-D-xylose + phosphate
show the reaction diagram
-
reverse (synthetic) reaction
-
-
r
L-lyxose + alpha-D-galactose 1-phosphate
beta-D-galactosyl-(1->4)-L-rhamnose + phosphate
show the reaction diagram
-
reverse (synthetic) reaction
-
-
r
L-lyxose + alpha-D-galactose 1-phosphate
D-galactosyl-beta-1,4-L-lyxose + phosphate
show the reaction diagram
-
-
-
r
L-mannose + alpha-D-galactose 1-phosphate
beta-D-galactosyl-(1->4)-L-mannose + phosphate
show the reaction diagram
-
reverse (synthetic) reaction
-
-
r
L-mannose + alpha-D-galactose 1-phosphate
D-galactosyl-beta-1,4-L-mannose + phosphate
show the reaction diagram
-
-
-
r
L-rhamnose + alpha-D-galactose 1-phosphate
beta-D-galactosyl-(1->4)-L-rhamnose + phosphate
show the reaction diagram
-
reverse (synthetic) reaction
-
-
r
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-D-galactosyl-(1->4)-L-rhamnose + phosphate
L-rhamnose + alpha-D-galactose 1-phosphate
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
51 - 290
2-deoxy-D-glucose
2.1
beta-D-galactosyl-(1->4)-L-rhamnose
-
pH 7.0, 37C
610 - 1500
D-galactose
7.9
D-galactosyl-beta-1,4-L-rhamnose
-
330 - 460
D-glucose
370
D-xylose
-
recombinant enzyme, pH 7.0, 37C, reverse reaction
58 - 220
L-Lyxose
55 - 78
L-Mannose
2.3 - 2.4
L-rhamnose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 8
2-deoxy-D-glucose
60
beta-D-galactosyl-(1->4)-L-rhamnose
Opitutus terrae
-
recombinant enzyme, pH 7.0, 37C, forward reaction
24 - 37
D-galactose
45
D-galactosyl-beta-1,4-L-rhamnose
Lachnoclostridium phytofermentans
A9KHK4
-
33 - 85
D-glucose
19
D-xylose
Opitutus terrae
-
recombinant enzyme, pH 7.0, 37C, reverse reaction
14 - 120
L-Lyxose
75 - 170
L-Mannose
50 - 74
L-rhamnose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.073
2-deoxy-D-glucose
Opitutus terrae
-
recombinant enzyme, pH 7.0, 37C, reverse reaction
531
0.024
D-galactose
Opitutus terrae
-
recombinant enzyme, pH 7.0, 37C, reverse reaction
71
0.099
D-glucose
Opitutus terrae
-
recombinant enzyme, pH 7.0, 37C, reverse reaction
35
0.051
D-xylose
Opitutus terrae
-
recombinant enzyme, pH 7.0, 37C, reverse reaction
115
0.25
L-Lyxose
Opitutus terrae
-
recombinant enzyme, pH 7.0, 37C, reverse reaction
1647
1.4
L-Mannose
Opitutus terrae
-
recombinant enzyme, pH 7.0, 37C, reverse reaction
2102
22
L-rhamnose
Opitutus terrae
-
recombinant enzyme, pH 7.0, 37C, reverse reaction
703
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.17
-
recombinant enzyme, substrate D-galactose, reverse reaction, pH 7.0, 37C
0.37
-
recombinant enzyme, substrate D-xylose, reverse reaction, pH 7.0, 37C
0.41
-
recombinant enzyme, substrate 2-deoxy-D-glucose, reverse reaction, pH 7.0, 37C
0.62
-
recombinant enzyme, substrate D-glucose, reverse reaction, pH 7.0, 37C
1.4
-
recombinant enzyme, substrate L-lyxose, reverse reaction, pH 7.0, 37C
8.4
-
recombinant enzyme, substrate L-mannose, reverse reaction, pH 7.0, 37C
27
-
purified recombinant enzyme, substrate beta-D-galactosyl-(1->4)-L-rhamnose, forward reaction, pH 7.0, 37C
29
-
recombinant enzyme, substrate L-rhamnose, reverse reaction, pH 7.0, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
activity range, profile, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 55
-
activity range, profile, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
proteins are predicted not to possess N-terminal signal peptides
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
84847
-
x * 80000, recombinant C-terminally His6-tagged Oter 1377 protein, SDS-PAGE, x * 84847, recombinant C-terminally His6-tagged Oter 1377 protein, sequence calculation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 80000, recombinant C-terminally His6-tagged Oter 1377 protein, SDS-PAGE, x * 84847, recombinant C-terminally His6-tagged Oter 1377 protein, sequence calculation
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
recombinant C-terminally His6-tagged Oter 1377 protein, stable at
722132
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
protein is thermostable up to 37C
45
-
recombinant C-terminally His6-tagged Oter 1377 protein, 30 min, 90% activity remaining
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged Oter 1377 protein from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic tree, cloning of the modified oter 1377 gene from plasmid pUC57 to pET-30a(+) and expression as C-terminally His6-tagged protein in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
suitable catalyst for practical syntheses of oligosaccharides