Information on EC 3.2.1.197 - beta-1,2-mannosidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.2.1.197
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RECOMMENDED NAME
GeneOntology No.
beta-1,2-mannosidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose + H2O = beta-D-mannopyranosyl-(1->2)-D-mannopyranose + alpha-D-mannopyranose
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
beta-1,2-D-mannoside mannohydrolase
The enzyme, characterized from multiple bacterial species, catalyses the hydrolysis of terminal, non-reducing D-mannose residues from beta-1,2-mannotriose and beta-1,2-mannobiose. The mechanism involves anomeric inversion, resulting in the release of alpha-D-mannopyranose. Activity with beta-1,2-mannotriose or higher oligosaccharides is higher than that with beta-1,2-mannobiose.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose + H2O
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose + alpha-D-mannopyranose
show the reaction diagram
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose + H2O
beta-D-mannopyranosyl-(1->2)-D-mannopyranose + alpha-D-mannopyranose
show the reaction diagram
beta-D-mannopyranosyl-(1->2)-D-mannopyranose + H2O
beta-D-mannopyranose + alpha-D-mannopyranose
show the reaction diagram
Candida mannan + H2O
? + alpha-D-mannopyranose
show the reaction diagram
additional information
?
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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-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose + H2O
beta-D-mannopyranosyl-(1->2)-D-mannopyranose + alpha-D-mannopyranose
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.56
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose
pH 5.5, 30C
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0.95
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose
pH 5.5, 30C
15
beta-D-mannopyranosyl-(1->2)-D-mannopyranose
pH 5.5, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose
Dyadobacter fermentans
C6W7B1
pH 5.5, 30C
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30
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose
Dyadobacter fermentans
C6W7B1
pH 5.5, 30C
30
beta-D-mannopyranosyl-(1->2)-D-mannopyranose
Dyadobacter fermentans
C6W7B1
pH 5.5, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.085 - 46
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose
214073
0.06 - 32
beta-D-mannopyranosyl-(1->2)-beta-D-mannopyranosyl-(1->2)-D-mannopyranose
212413
0.04 - 2
beta-D-mannopyranosyl-(1->2)-D-mannopyranose
210726
0.1 - 0.115
Candida mannan
214121
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.015
mutant E265A, pH 5.5, 30C
0.71
mutant E224A, pH 5.5, 30C
37
wild-type, pH 5.5, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with mannose bound in the -1 and +1 subsites. A pair of glutamate residues, Glu227 and Glu268, hydrogen bond to O1 of alpha-mannose, and either of these residues may function as the catalytic base. Conserved lysine residue, Lys199 is a key specificity determinant for beta-1,2-mannosidic linkages
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
stable up to for 15 min
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E227Q
32% of wild-type activity
E227Q/E268Q
no activity
E268A
5% of wild-type activity
E268Q
4% of wild-type activity
F344A
31% of wild-type activity
N74A
15% of wild-type activity
R89A
25% of wild-type activity
Y302A
6% of wild-type activity
E268A
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5% of wild-type activity
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E268Q
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4% of wild-type activity
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N74A
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15% of wild-type activity
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R89A
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25% of wild-type activity
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E224A
1.9% of wild-type activity. Glutamic acid residues E265 and E224 are critical for the hydrolysis of beta-1,2-mannotriose. The residues are not conserved among GH130 phosphorylases and are predicted to assist the nucleophilic attack of a water molecule in the hydrolysis of the beta-D-mannosidic bond
E265A
0.04% of wild-type activity. Glutamic acid residues E265 and E224 are critical for the hydrolysis of beta-1,2-mannotriose. The residues are not conserved among GH130 phosphorylases and are predicted to assist the nucleophilic attack of a water molecule in the hydrolysis of the beta-D-mannosidic bond
E224A
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1.9% of wild-type activity. Glutamic acid residues E265 and E224 are critical for the hydrolysis of beta-1,2-mannotriose. The residues are not conserved among GH130 phosphorylases and are predicted to assist the nucleophilic attack of a water molecule in the hydrolysis of the beta-D-mannosidic bond
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E265A
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0.04% of wild-type activity. Glutamic acid residues E265 and E224 are critical for the hydrolysis of beta-1,2-mannotriose. The residues are not conserved among GH130 phosphorylases and are predicted to assist the nucleophilic attack of a water molecule in the hydrolysis of the beta-D-mannosidic bond
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