Information on EC 2.4.1.340 - 1,2-beta-oligomannan phosphorylase

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The expected taxonomic range for this enzyme is: Thermoanaerobacter sp.

EC NUMBER
COMMENTARY hide
2.4.1.340
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RECOMMENDED NAME
GeneOntology No.
1,2-beta-oligomannan phosphorylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[(1->2)-beta-D-mannosyl]n + phosphate = [(1->2)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
(1->2)-beta-D-mannan:phosphate beta-D-mannosyl transferase (conformation-inverting)
The enzyme, originally characterized from the thermophilic anaerobic bacterium Thermoanaerobacter sp. X514, catalyses a reversible reaction. In the synthetic direction it produces oligosaccharides with a degree of polymerization (DP) of 3, 4 and 5. The phosphorolysis reaction proceeds to completion, although activity is highest when the substrate has at least three residues. cf. EC 2.4.1.339, beta-1,2-mannobiose phosphorylase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
involved in GDP-D-mannose biosynthesis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-mannose + alpha-D-mannose 1-phosphate
[(1->2)-beta-D-mannosyl]2 + phosphate
show the reaction diagram
in the synthetic direction it produces oligosaccharides with a degree of polymerization of 3, 4 and 5. The phosphorolysis reaction proceeds to completion, although activity is highest when the substrate has at least three residues
-
-
?
D-fructose + alpha-D-mannose 1-phosphate
? + phosphate
show the reaction diagram
-
-
-
?
[(1->2)-beta-D-mannosyl]2 + alpha-D-mannose 1-phosphate
[(1->2)-beta-D-mannosyl]3 + phosphate
show the reaction diagram
in the synthetic direction it produces oligosaccharides with a degree of polymerization of 3, 4 and 5. The phosphorolysis reaction proceeds to completion, although activity is highest when the substrate has at least three residues
-
-
?
[(1->2)-beta-D-mannosyl]2 + phosphate
alpha-D-mannose 1-phosphate
show the reaction diagram
in the synthetic direction it produces oligosaccharides with a degree of polymerization of 3, 4 and 5. The phosphorolysis reaction proceeds to completion, although activity is highest when the substrate has at least three residues
-
-
r
[(1->2)-beta-D-mannosyl]3 + alpha-D-mannose 1-phosphate
[(1->2)-beta-D-mannosyl]4 + phosphate
show the reaction diagram
in the synthetic direction it produces oligosaccharides with a degree of polymerization of 3, 4 and 5. The phosphorolysis reaction proceeds to completion, although activity is highest when the substrate has at least three residues
-
-
?
[(1->2)-beta-D-mannosyl]3 + phosphate
[(1->2)-beta-D-mannosyl]2 + alpha-D-mannose 1-phosphate
show the reaction diagram
in the synthetic direction it produces oligosaccharides with a degree of polymerization of 3, 4 and 5. The phosphorolysis reaction proceeds to completion, although activity is highest when the substrate has at least three residues
-
-
r
[(1->2)-beta-D-mannosyl]4 + alpha-D-mannose 1-phosphate
[(1->2)-beta-D-mannosyl]5 + phosphate
show the reaction diagram
in the synthetic direction it produces oligosaccharides with a degree of polymerization of 3, 4 and 5. The phosphorolysis reaction proceeds to completion, although activity is highest when the substrate has at least three residues
-
-
?
[(1->2)-beta-D-mannosyl]4 + phosphate
[(1->2)-beta-D-mannosyl]3 + alpha-D-mannose 1-phosphate
show the reaction diagram
in the synthetic direction it produces oligosaccharides with a degree of polymerization of 3, 4 and 5. The phosphorolysis reaction proceeds to completion, although activity is highest when the substrate has at least three residues
-
-
r
[(1->2)-beta-D-mannosyl]n + phosphate
[(1->2)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
show the reaction diagram
involved in GDP-D-mannose biosynthesis
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-
r
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
[(1->2)-beta-D-mannosyl]n + phosphate
[(1->2)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
show the reaction diagram
B0K2C2
involved in GDP-D-mannose biosynthesis
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r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41
alpha-D-mannose
pH 5.0, 30C, synthetic reaction
1.4
alpha-D-mannose 1-phosphate
pH 5.0, 30C, synthetic reaction
0.2
D-fructose
pH 5.0, 30C, synthetic reaction
0.63 - 0.74
phosphate
0.52 - 0.77
[(1->2)-beta-D-mannosyl]2
-
0.92 - 1.2
[(1->2)-beta-D-mannosyl]3
-
2.3
[(1->2)-beta-D-mannosyl]4
pH 5.0, 30C, phosphorolytic reaction
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.9
alpha-D-mannose
Thermoanaerobacter sp.
B0K2C2
pH 5.0, 30C, synthetic reaction
22
alpha-D-mannose 1-phosphate
Thermoanaerobacter sp.
B0K2C2
pH 5.0, 30C, synthetic reaction
2
D-fructose
Thermoanaerobacter sp.
B0K2C2
pH 5.0, 30C, synthetic reaction
1.9 - 25
[(1->2)-beta-D-mannosyl]2
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20 - 43
[(1->2)-beta-D-mannosyl]3
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49
[(1->2)-beta-D-mannosyl]4
Thermoanaerobacter sp.
B0K2C2
pH 5.0, 30C, phosphorolytic reaction
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.6
alpha-D-mannose
Thermoanaerobacter sp.
B0K2C2
pH 5.0, 30C, synthetic reaction
993
16
alpha-D-mannose 1-phosphate
Thermoanaerobacter sp.
B0K2C2
pH 5.0, 30C, synthetic reaction
638
10
D-fructose
Thermoanaerobacter sp.
B0K2C2
pH 5.0, 30C, synthetic reaction
117
3.7 - 32
[(1->2)-beta-D-mannosyl]2
210624
22 - 36
[(1->2)-beta-D-mannosyl]3
210625
21
[(1->2)-beta-D-mannosyl]4
Thermoanaerobacter sp.
B0K2C2
pH 5.0, 30C, phosphorolytic reaction
210626
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
synthetic reaction
6
phosphorolytic activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33997
2 * 33997, calculated from sequence
34000
2 * 34000, SDS-PAGE
50000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 33997, calculated from sequence; 2 * 34000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9.5
stable in pH-range 4.0-9.5 during a 30 min incubation
737136
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
stable up to 55C during a 30 min incubation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in in Escherichia coli Rosetta 2 (DE3)