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Information on EC 2.4.1.339 - beta-1,2-mannobiose phosphorylase
for references in articles please use BRENDA:EC2.4.1.339
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.339 beta-1,2-mannobiose phosphorylase
IUBMB Comments
The enzyme, originally characterized from the thermophilic anaerobic bacterium Thermoanaerobacter sp. X514, catalyses a reversible reaction. cf. EC 2.4.1.340, 1,2-β-oligomannan phosphorylase.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
lin0857, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-D-mannopyranosyl-(1->2)-D-mannopyranose + phosphate = D-mannopyranose + alpha-D-mannose 1-phosphate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
beta-D-mannopyranosyl-(1->2)-D-mannopyranose:phosphate alpha-D-mannosyltransferase
The enzyme, originally characterized from the thermophilic anaerobic bacterium Thermoanaerobacter sp. X514, catalyses a reversible reaction. cf. EC 2.4.1.340, 1,2-beta-oligomannan 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
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose + phosphate
beta-D-mannopyranosyl-(1->2)-D-mannopyranose + alpha-D-mannose 1-phosphate
Substrates: the enzyme preferentially phosphorolyzes beta-1,2-Man2 over beta-1,2-Man3
Products: -
Products: -
r
beta-D-mannopyranosyl-(1->2)-D-mannopyranose + alpha-D-mannose 1-phosphate
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose + phosphate
Substrates: no production of tetrasaccharide is detected
Products: -
Products: -
r
beta-D-mannopyranosyl-(1->2)-D-mannopyranose + phosphate
D-mannopyranose + alpha-D-mannose 1-phosphate
D-fructose + alpha-D-mannose 1-phosphate
? + phosphate
Substrates: -
Products: -
Products: -
r
D-mannopyranose + alpha-D-mannose 1-phosphate
beta-D-mannopyranosyl-(1->2)-D-mannopyranose + phosphate
Substrates: -
Products: -
Products: -
r
beta-D-mannopyranosyl-(1->2)-D-mannopyranose + phosphate
D-mannopyranose + alpha-D-mannose 1-phosphate
Substrates: the enzyme preferentially phosphorolyzes beta-1,2-Man2 over beta-1,2-Man3
Products: -
Products: -
r
beta-D-mannopyranosyl-(1->2)-D-mannopyranose + phosphate
D-mannopyranose + alpha-D-mannose 1-phosphate
-
Substrates: -
Products: -
Products: -
r
beta-D-mannopyranosyl-(1->2)-D-mannopyranose + phosphate
D-mannopyranose + alpha-D-mannose 1-phosphate
-
Substrates: -
Products: -
Products: -
r
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.1
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose
30°C, pH 7
0.13
phosphate
30°C, pH 7, cosubstrate: beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose
0.19
phosphate
30°C, pH 7, cosubstrate: beta-D-mannopyranosyl-(1->2)-D-mannopyranose
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose
30°C, pH 7
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose
30°C, pH 7
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7.5
pH 4.5: about 60% of maximal activity, pH 7.5: about 60% of maximal activity, synthetic reaction
5.5 - 8
pH 5.5: about 75% of maximal activity, pH 8.0: about 60% of maximal activity, phosphorolytic reaction
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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.
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). BMBP_THEPX
Thermoanaerobacter sp. (strain X514)
302
0
35111
Swiss-Prot
-
BMBP_LISIN
Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
355
0
39995
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method at 20°C, crystals complexed with beta-1,2-Man2 and beta-1,2-Man3 are prepared by soaking in the cryoprotectant solution supplemented with 50 mM beta-1,2-Man2 or 10 mM beta-1,2-Man3. beta-1,2-Mannotriose is bound in a U-shape, interacting with a phosphate analog at both ends. Lin0857 has a unique dimer structure connected by a loop, and a significant openclose loop displacement iss observed for substrate entry. A long loop, which is exclusively present in Lin0857, covers the active site to limit the pocket size. A structural basis for substrate recognition and phosphorolysis is provided
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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
expression in Escherichia coli as a C-terminally (His)6-tagged protein
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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., Thermoanaerobacter sp. X-514
brenda
Tsuda, T.; Nihira, T.; Chiku, K.; Suzuki, E.; Arakawa, T.; Nishimoto, M.; Kitaoka, M.; Nakai, H.; Fushinobu, S.
Characterization and crystal structure determination of beta-1,2-mannobiose phosphorylase from Listeria innocua
FEBS Lett.
589
3816-3821
2015
Listeria innocua (Q92DF6), Listeria innocua
brenda
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