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Information on EC 2.4.1.340 - 1,2-beta-oligomannan phosphorylase
for references in articles please use BRENDA:EC2.4.1.340
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.340 1,2-beta-oligomannan phosphorylase
IUBMB Comments
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, β-1,2-mannobiose phosphorylase.
The expected taxonomic range for this enzyme is: unclassified Thermoanaerobacter
Reaction Schemes
showSynonyms
1,2-beta-oligomannan phosphorylase, 1,2-beta-oligomannan:phosphate alpha-D-mannosyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[(1->2)-beta-D-mannosyl]n + phosphate = [(1->2)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
-
-
-
-
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-D-mannose + alpha-D-mannose 1-phosphate
[(1->2)-beta-D-mannosyl]2 + phosphate
Substrates: 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
Products: -
Products: -
?
D-fructose + alpha-D-mannose 1-phosphate
? + phosphate
Substrates: -
Products: -
Products: -
?
[(1->2)-beta-D-mannosyl]2 + alpha-D-mannose 1-phosphate
[(1->2)-beta-D-mannosyl]3 + phosphate
Substrates: 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
Products: -
Products: -
?
[(1->2)-beta-D-mannosyl]2 + phosphate
alpha-D-mannose 1-phosphate
Substrates: 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
Products: -
Products: -
r
[(1->2)-beta-D-mannosyl]3 + alpha-D-mannose 1-phosphate
[(1->2)-beta-D-mannosyl]4 + phosphate
Substrates: 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
Products: -
Products: -
?
[(1->2)-beta-D-mannosyl]3 + phosphate
[(1->2)-beta-D-mannosyl]2 + alpha-D-mannose 1-phosphate
Substrates: 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
Products: -
Products: -
r
[(1->2)-beta-D-mannosyl]4 + alpha-D-mannose 1-phosphate
[(1->2)-beta-D-mannosyl]5 + phosphate
Substrates: 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
Products: -
Products: -
?
[(1->2)-beta-D-mannosyl]4 + phosphate
[(1->2)-beta-D-mannosyl]3 + alpha-D-mannose 1-phosphate
Substrates: 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
Products: -
Products: -
r
[(1->2)-beta-D-mannosyl]n + phosphate
[(1->2)-beta-D-mannosyl]n-1 + alpha-D-mannose 1-phosphate
Substrates: involved in GDP-D-mannose biosynthesis
Products: -
Products: -
r
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
Substrates: involved in GDP-D-mannose biosynthesis
Products: -
Products: -
r
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
alpha-D-mannose 1-phosphate
pH 5.0, 30°C, synthetic reaction
2.3
[(1->2)-beta-D-mannosyl]4
pH 5.0, 30°C, phosphorolytic reaction
0.63
phosphate
cosubstrate: [(1->2)-beta-D-mannosyl]4, pH 5.0, 30°C, phosphorolytic reaction
0.71
phosphate
cosubstrate: [(1->2)-beta-D-mannosyl]3, pH 5.0, 30°C, phosphorolytic reaction
0.74
phosphate
cosubstrate: [(1->2)-beta-D-mannosyl]2, pH 5.0, 30°C, phosphorolytic reaction
0.52
[(1->2)-beta-D-mannosyl]2
pH 5.0, 30°C, phosphorolytic reaction
0.77
[(1->2)-beta-D-mannosyl]2
pH 5.0, 30°C, synthetic reaction
0.92
[(1->2)-beta-D-mannosyl]3
pH 5.0, 30°C, phosphorolytic reaction
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
22
alpha-D-mannose 1-phosphate
pH 5.0, 30°C, synthetic reaction
49
[(1->2)-beta-D-mannosyl]4
pH 5.0, 30°C, phosphorolytic reaction
1.9
[(1->2)-beta-D-mannosyl]2
pH 5.0, 30°C, phosphorolytic reaction
20
[(1->2)-beta-D-mannosyl]3
pH 5.0, 30°C, phosphorolytic reaction
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16
alpha-D-mannose 1-phosphate
pH 5.0, 30°C, synthetic reaction
21
[(1->2)-beta-D-mannosyl]4
pH 5.0, 30°C, phosphorolytic reaction
3.7
[(1->2)-beta-D-mannosyl]2
pH 5.0, 30°C, phosphorolytic reaction
22
[(1->2)-beta-D-mannosyl]3
pH 5.0, 30°C, phosphorolytic reaction
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BOLMP_THEPX
Thermoanaerobacter sp. (strain X514)
296
0
33997
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chiku, K.; Nihira, T.; Suzuki, E.; Nishimoto, M.; Kitaoka, M.; Ohtsubo, K.; Nakai, H.
Discovery of two beta-1,2-mannoside phosphorylases showing different chain-length specificities from Thermoanaerobacter sp. X-514
PLoS One
9
e114882
2014
Thermoanaerobacter sp. (B0K2C2)
brenda
EXTERNAL LINKS (specific for EC-Number 2.4.1.340)
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Release 2026.1 (March 2026)
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