Information on EC 3.2.1.25 - beta-mannosidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
3.2.1.25
-
RECOMMENDED NAME
GeneOntology No.
beta-mannosidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
exohydrolysis
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Other glycan degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-D-mannoside mannohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-43-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Pekin-type drake
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain F-50
-
-
Manually annotated by BRENDA team
strain F-50
-
-
Manually annotated by BRENDA team
strain K4
-
-
Manually annotated by BRENDA team
strain K4
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Bacillus sp. AM-001
AM-001
-
-
Manually annotated by BRENDA team
N16-5
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
L. cv. Grand Rapids
-
-
Manually annotated by BRENDA team
subsp. sativa
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain Fr. 79 (ATCC 64658)
-
-
Manually annotated by BRENDA team
Phlebia radiata Fr. 79
strain Fr. 79 (ATCC 64658)
-
-
Manually annotated by BRENDA team
desert and oasis flies studied, male and female, Neot Hakikar (oasis), Jordan Valley spring (wet), Kfar Adumim starved (arid), Jordan Valley autumn (arid)
-
-
Manually annotated by BRENDA team
Polyporus sulfureus
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Mill.
-
-
Manually annotated by BRENDA team
synthetic construct
-
-
-
Manually annotated by BRENDA team
JCM 2947
-
-
Manually annotated by BRENDA team
JCM 2947
-
-
Manually annotated by BRENDA team
-
-
-
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
1-galactosyl-mannotriose + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-beta-D-mannopyranoside + H2O
2,4-dinitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
2-acetamido-2-deoxymannopyranose + H2O
?
show the reaction diagram
-
-
-
-
?
2-amino-2-deoxymannopyranose + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl beta-D-mannoside + H2O
4-methylumbelliferone + beta-D-mannose
show the reaction diagram
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
4-nitrophenyl beta-D-glucopyranose + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannose
show the reaction diagram
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
show the reaction diagram
-
3.1% of the activity with 4-nitrophenyl-beta-D-glucopyranose
-
-
?
4-nitrophenyl-beta-D-fucopyranose + H2O
4-nitrophenol + beta-D-fucose
show the reaction diagram
-
129% of the activity with 4-nitrophenyl-beta-D-glucopyranose
-
-
?
4-nitrophenyl-beta-D-galactopyranose + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
-
17% of the activity with 4-nitrophenyl-beta-D-glucopyranose
-
-
?
4-nitrophenyl-beta-D-mannopyranose + H2O
4-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-beta-D-mannopyranose + H2O
4-nitrophenol + beta-D-mannose
show the reaction diagram
4-nitrophenyl-beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
show the reaction diagram
-
activity measured in whole fly homogenates, substrate concentration of 6 mM in citrate buffer
-
-
?
4-nitrophenyl-beta-D-mannopyranoside + H2O
4-nitrophenol + D-mannopyranose
show the reaction diagram
4-nitrophenyl-beta-D-mannopyranoside + methyl-alpha-D-mannopyranoside
4-nitrophenyl-alpha-D-mannopyranoside + methyl-beta-D-mannopyranoside
show the reaction diagram
-
the enzyme shows low transglycosylation activity at 50C and pH 5.0
-
-
-
4-nitrophenyl-beta-L-arabinopyranose + H2O
4-nitrophenol + beta-L-arabinopyranose
show the reaction diagram
-
16% of the activity with 4-nitrophenyl-beta-D-glucopyranose
-
-
?
4-O-beta-D-mannopyranosyl-D-mannopyranose + 1-propanol
?
show the reaction diagram
4-O-beta-D-mannopyranosyl-D-mannopyranose + D-fructose
?
show the reaction diagram
4-O-beta-D-mannopyranosyl-D-mannopyranose + D-galactose
?
show the reaction diagram
4-O-beta-D-mannopyranosyl-D-mannopyranose + D-xylose
?
show the reaction diagram
-
transglycosylation reaction, 18.4% transfer ratio
-
-
-
4-O-beta-D-mannopyranosyl-D-mannopyranose + ethanol
?
show the reaction diagram
4-O-beta-D-mannopyranosyl-D-mannopyranose + H2O
D-mannopyranose
show the reaction diagram
4-O-beta-D-mannopyranosyl-D-mannopyranose + L-arabinose
?
show the reaction diagram
4-O-beta-D-mannopyranosyl-D-mannopyranose + methanol
?
show the reaction diagram
-
transglycosylation reaction, 42.6% transfer ratio
-
-
-
4-O-beta-D-mannopyranosyl-D-mannopyranose + N-acetyl-D-glucosamine
?
show the reaction diagram
-
transglycosylation reaction, 1.4% transfer ratio
-
-
-
alpha-D-mannopyranose 1-phosphate + H2O
alpha-D-mannose + phosphate
show the reaction diagram
-
-
-
-
?
alpha-Man-(1-4)-beta-Man-(1-4)-Man + H2O
?
show the reaction diagram
-
-
-
-
?
beta-D-Man-(1-4)-beta-D-GlcNAc-(1-4)-beta-D-GlcNAc-Asn-Lys + H2O
?
show the reaction diagram
-
-
-
-
?
beta-D-Man-(1-4)-beta-D-GlcNAc-1-4-[alpha-L-Fuc(1-6)]-beta-D-GlcNAc-ASn-peptide + H2O
?
show the reaction diagram
-
-
-
-
?
beta-D-Man-(1-4)-beta-D-Man-(1-4)-D-Man + H2O
?
show the reaction diagram
-
-
-
-
?
beta-D-mannohexaitol + H2O
?
show the reaction diagram
beta-D-mannopentaitol + H2O
?
show the reaction diagram
beta-D-mannosyl-1,4-beta-D-glucoside + H2O
D-mannose + beta-D-glucose
show the reaction diagram
-
-
-
-
?
beta-D-mannotriitol + H2O
?
show the reaction diagram
beta-mannotetraitol + H2O
?
show the reaction diagram
beta1-4-mannobiose + H2O
?
show the reaction diagram
cellobiose + H2O
?
show the reaction diagram
-
33% of the activity with 4-nitrophenyl-beta-D-glucopyranose
-
-
?
cellohexaose + H2O
?
show the reaction diagram
-
303% of the activity with 4-nitrophenyl-beta-D-glucopyranose
-
-
?
cellopentaose + H2O
?
show the reaction diagram
-
225% of the activity with 4-nitrophenyl-beta-D-glucopyranose
-
-
?
cellotetraose + H2O
?
show the reaction diagram
-
52% of the activity with 4-nitrophenyl-beta-D-glucopyranose
-
-
?
cellotriose + H2O
?
show the reaction diagram
-
19% of the activity with 4-nitrophenyl-beta-D-glucopyranose
-
-
?
D-mannofuranurono-6,3-lactone + H2O
?
show the reaction diagram
-
-
-
-
?
D-mannoheptulose + H2O
?
show the reaction diagram
-
-
-
-
?
D-mannono-1,4-lactone + H2O
?
show the reaction diagram
-
-
-
-
?
L-mannono-1,4-lactone + H2O
?
show the reaction diagram
-
-
-
-
?
laminaribiose + H2O
?
show the reaction diagram
-
13% of the activity with 4-nitrophenyl-beta-D-glucopyranose
-
-
?
laminaritriose + H2O
?
show the reaction diagram
-
2.8% of the activity with 4-nitrophenyl-beta-D-glucopyranose
-
-
?
locust bean gum + H2O
?
show the reaction diagram
-
-
-
-
?
Man-(beta1-4)GlcNAc + H2O
mannose + GlcNAc
show the reaction diagram
Man-(beta1-4)ManNAc + H2O
mannose + ManNAc
show the reaction diagram
-
-
-
?
Man-GlcNAc-GlcNAc + H2O
mannose + GlcNAc-GlcNAc
show the reaction diagram
-
-
-
?
Manbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta-Asn + H2O
mannose + GlcNAcbeta(1-4)GlcNAcbeta-Asn
show the reaction diagram
Manbeta1-2Man + H2O
D-mannose
show the reaction diagram
Manbeta1-4GlcNAcbeta1-4Manbeta1-4GlcNAcbeta1-4GlcNAc + H2O
mannose + GlcNAcbeta1-4Manbeta1-4GlcNAcbeta1-4GlcNAc
show the reaction diagram
-
-
-
?
Manbeta1-4Man + H2O
D-mannose
show the reaction diagram
-
-
-
-
?
mannan + H2O
mannose + ?
show the reaction diagram
mannobiose + glucose + D-glucose
?
show the reaction diagram
-
transglycosylation reaction, 40.1% transfer ratio
-
-
-
mannopentaose + H2O
?
show the reaction diagram
mannopyranosylamine + H2O
?
show the reaction diagram
-
-
-
-
?
mannotetraose + H2O
?
show the reaction diagram
mannotriose + H2O
?
show the reaction diagram
methyl alpha-D-mannopyranoside + H2O
?
show the reaction diagram
-
-
-
-
?
naphthyl-beta-D-mannopyranoside + H2O
naphthol + beta-D-mannose
show the reaction diagram
-
-
-
-
?
o-nitrophenyl-beta-D-mannopyranoside + H2O
o-nitrophenol + alpha-D-mannose
show the reaction diagram
p-nitrophenyl beta-D-mannopyranoside + H2O
p-nitrophenol + beta-D-mannopyranose
show the reaction diagram
p-nitrophenyl beta-D-mannopyranoside + H2O
p-nitrophenol + beta-D-mannose
show the reaction diagram
p-nitrophenyl-beta-D-galactoside + H2O
p-nitrophenol + beta-D-galactose
show the reaction diagram
-
4.6% activity compared to p-nitrophenyl-beta-D-mannoside
-
-
?
p-nitrophenyl-beta-D-glucoside + H2O
p-nitrophenol + beta-D-glucose
show the reaction diagram
-
34.5% activity compared to p-nitrophenyl-beta-D-mannoside
-
-
?
p-nitrophenyl-beta-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
self-transfer of the mannosyl group is observed, and a 10-15% yield of a beta1,4-disaccharide is obtained
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
p-nitrophenyl-beta-galactoside + H2O
p-nitrophenol + beta-D-galactopyranose
show the reaction diagram
-
low activity
-
-
?
p-nitrophenyl-beta-mannoside + H2O
p-nitrophenol + beta-D-mannopyranose
show the reaction diagram
-
-
-
-
?
phenyl beta-D-mannoside + H2O
?
show the reaction diagram
sophorose + H2O
?
show the reaction diagram
-
15% of the activity with 4-nitrophenyl-beta-D-glucopyranose
-
-
?
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
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MgSO4
-
26% stimulation at 10 mM
Mn2+
-
slight activation
ZnSO4
-
0.5 mM, 25% stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
-
(5S,6R,8R)-5-(hydroxymethyl)-2-(2-phenylethyl)-5,6,7,8-tetrahydroimidazo[1,2-a]pyridine-6,7,8-triol
persuasive transition state mimic
(5S,6R,8R)-5-(hydroxymethyl)-2-(phenoxymethyl)-5,6,7,8-tetrahydroimidazo[1,2-a]pyridine-6,7,8-triol
persuasive transition state mimic
(5S,6R,8R)-5-(hydroxymethyl)-2-[(phenylamino)methyl]-5,6,7,8-tetrahydroimidazo[1,2-a]pyridine-6,7,8-triol
persuasive transition state mimic
2-amino-2-deoxy-D-mannose
2-deoxy-2-fluoro-beta-D-mannosyl fluoride
-
time-dependent inactivation through accumulation of a covalent 2-deoxy-2-fluoro-alpha-D-mannosyl-beta-mannosidase 2A enzyme intermediate
2-deoxy-2-fluoro-beta-glycosyl fluorides
-
in vivo inhibition
-
4-nitrophenyl beta-D-thioglucoside
competitive, adopts 4NP-S-Glc 3S5 or 1S3 conformations upon binding according to STD NMR and trNOESY experiments. QM modeling and docking, based on GLIDE scores, predicts that 4-nitrophenyl beta-D-thioglucoside preferentially binds in 1S3 geometries
-
4-nitrophenyl beta-D-thiomannoside
competitive, adopts 4C1 geometry upon binding according to STD NMR and trNOESY experiments. QM modeling and docking, based on GLIDE scores, predicts that 4-nitrophenyl beta-D-thiomannoside preferentially binds in 1S3 geometries
-
beta-1,4-mannooligosaccharides
-
inhibit binding of the enzyme to galactomannans
-
Ca2+
-
5 mM Ca(NO3)2, 45% inhibition
Co2+
1.5 mM, 80% residual activity
D-mannono-1,4-lactone
-
-
D-mannosamine
-
-
D-mannose
dimethyl sulfoxide
5 mM, no residual activity
dimethylformamide
5 mM, no residual activity
ethanol
5 mM, no residual activity
Fe3+
Polyporus sulfureus
-
-
guanidine hydrochloride
-
0.6 M, 30% inhibition
iodoacetate
5 mM, no residual activity
isofagomine lactam
-
-
mannose
-
relative inhibition of 20%, three concentrations of 10, 50, and 100 mM tested
monoiodoacetate
-
-
N,N-(2-aminoethyl)-D-glucoamidine
-
-
N,N-(2-aminoethyl)-D-mannoamidine
-
-
N,N-(3-aminopropyl)-D-glucoamidine
-
-
N,N-(3-aminopropyl)-D-mannoamidine
-
-
N,N-(3-hydroxypropyl)-D-glucoamidine
-
-
N,N-(3-hydroxypropyl)-D-mannoamidine
-
-
N,N-(4-aminobutyl)-D-glucoamidine
-
-
N,N-(4-aminobutyl)-D-mannoamidine
-
-
N,N-propyl-D-mannoamidine
-
-
N-bromosuccinimide
-
-
n-Dodecylbenzene sulfonate
-
-
N-propyl-D-glucoamidine
-
-
N-[(2Z,3R,5R,6S)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]ethane-1,2-diaminium
-
N-[(2Z,3R,5R,6S)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]propan-1-aminium
-
p-nitrophenyl-alpha-D-mannopyranoside
p-nitrophenyl-beta-mannoside
-
above 0.4 mM
Sodium dodecyl sulfate
5 mM, no residual activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
0.05%, stabilizes
p-nitrophenyl-alpha-D-mannopyranoside
-
activates at low concentration, competitively inhibits at higher concentrations, 2-3 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0028 - 0.089
2,4-dinitrophenyl-beta-D-mannopyranoside
0.13 - 0.91
4-methylumbelliferyl beta-D-mannopyranoside
7.3 - 36.1
4-nitrophenyl beta-D-galactopyranoside
0.3 - 30.4
4-nitrophenyl beta-D-glucopyranoside
0.44 - 3.2
4-nitrophenyl beta-D-mannopyranoside
0.5
4-nitrophenyl-beta-D-glucopyranose
pH 4.0, 30C
0.25 - 1.6
4-nitrophenyl-beta-D-mannopyranose
2.5 - 3
4-nitrophenyl-beta-D-mannopyranoside
pH 5.0, 37C
0.000083
4-nitrophenyl-beta-mannopyranose
-
pH 7.0, 37C, mutant enzyme E215A
16.9
Asn-(GlcNAc)2(Man)
-
-
-
2.8 - 12.5
Beta-D-mannohexaitol
12.5
beta-D-mannopentaitol
-
-
6.1
beta-D-mannosyl-1,4-beta-D-glucoside
-
pH 7.0, 37C, wild-type enzyme
12 - 12.5
beta-D-mannotetraitol
12.5 - 80
beta-D-mannotriitol
0.9
mannobiose
-
pH 7.0, 37C, wild-type enzyme
1.2 - 10
mannotriitol
0.1
Mannotriose
-
pH 7.0, 37C, wild-type enzyme
3.22
Naphthyl-beta-D-mannopyranoside
-
-
2.33 - 3
o-nitrophenyl-beta-D-mannopyranoside
0.55 - 9
p-nitrophenyl beta-D-mannopyranoside
0.017 - 11
p-nitrophenyl-beta-D-mannopyranoside
0.12 - 5
p-nitrophenyl-beta-D-mannoside
6.5 - 7.1
phenyl beta-D-mannoside
additional information
additional information
-
as the enzyme is inhibited by the substrate p-nitrophenyl-beta-mannoside at concentrations above 0.4 mM, the KM-value of 0.3 mM is only an estimate
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00183 - 214.4
2,4-dinitrophenyl-beta-D-mannopyranoside
13.5 - 571
4-nitrophenyl beta-D-galactopyranoside
25.5 - 439
4-nitrophenyl beta-D-glucopyranoside
1.6 - 45
4-nitrophenyl beta-D-mannopyranoside
0.5
4-nitrophenyl-beta-D-glucopyranose
Hordeum vulgare
B5A496
pH 4.0, 30C
0.033 - 3.1
4-nitrophenyl-beta-D-mannopyranose
0.1
4-nitrophenyl-beta-mannopyranose
Cellvibrio mixtus
-
pH 7.0, 37C, mutant enzyme E215A
2.17
4-O-beta-D-mannopyranosyl-D-mannopyranose
Cellvibrio mixtus
-
pH 7.0, 37C, wild-type enzyme
0.053
beta-D-mannosyl-1,4-beta-D-glucoside
Cellvibrio mixtus
-
pH 7.0, 37C, wild-type enzyme
166.7
Mannotriose
Cellvibrio mixtus
-
pH 7.0, 37C, wild-type enzyme
67.8
p-nitrophenyl beta-D-mannopyranoside
Thermotoga neapolitana
-
-
0.0097 - 157
p-nitrophenyl-beta-D-mannopyranoside
additional information
additional information
Cellulomonas fimi
-
as the enzyme is inhibited by the substrate p-nitrophenyl-beta-mannoside at concentrations above 0.4 mM, the turnover number of 167 per s is only an estimate
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.85 - 75.8
4-nitrophenyl beta-D-galactopyranoside
1.6 - 870
4-nitrophenyl beta-D-glucopyranoside
1.4 - 14.7
4-nitrophenyl beta-D-mannopyranoside
1
4-nitrophenyl-beta-D-glucopyranose
Hordeum vulgare
B5A496
pH 4.0, 30C
14384
12.7
4-nitrophenyl-beta-D-mannopyranose
Hordeum vulgare
B5A496
pH 4.0, 30C
13896
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000014 - 0.11
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
0.000057
(5S,6R,8R)-5-(hydroxymethyl)-2-(2-phenylethyl)-5,6,7,8-tetrahydroimidazo[1,2-a]pyridine-6,7,8-triol
pH 5.6
0.000401
(5S,6R,8R)-5-(hydroxymethyl)-2-(phenoxymethyl)-5,6,7,8-tetrahydroimidazo[1,2-a]pyridine-6,7,8-triol
pH 5.6
0.000072
(5S,6R,8R)-5-(hydroxymethyl)-2-[(phenylamino)methyl]-5,6,7,8-tetrahydroimidazo[1,2-a]pyridine-6,7,8-triol
pH 5.6
0.41
2-deoxy-2-fluoro-beta-D-mannosyl fluoride
-
-
0.095
4-nitrophenyl beta-D-thioglucoside
pH 4.0, 30C
-
0.266
4-nitrophenyl beta-D-thiomannoside
pH 4.0, 30C
-
0.05
Hg2+
-
-
0.00013
N,N-(2-aminoethyl)-D-glucoamidine
-
pH 6.8
0.000009
N,N-(2-aminoethyl)-D-mannoamidine
-
pH 6.8
0.00041
N,N-(3-aminopropyl)-D-glucoamidine
-
pH 6.8
0.00015
N,N-(3-aminopropyl)-D-mannoamidine
-
pH 6.8
0.00087
N,N-(3-hydroxypropyl)-D-glucoamidine
-
pH 6.8
0.00015
N,N-(3-hydroxypropyl)-D-mannoamidine
-
pH 6.8
0.00071
N,N-(4-aminobutyl)-D-glucoamidine
-
pH 6.8
0.00006
N,N-(4-aminobutyl)-D-mannoamidine
-
pH 6.8
0.00019
N,N-propyl-D-mannoamidine
-
pH 6.8
0.0033
N-propyl-D-glucoamidine
-
pH 6.8
0.001
N-[(2Z,3R,5R,6S)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]ethane-1,2-diaminium
pH 5.6
0.0019
N-[(2Z,3R,5R,6S)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]propan-1-aminium
pH 5.6
0.000975
noeuromycin
pH 5.6
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.3
-
culture filtrate
0.996
-
-
1.083
-
-
1.772
-
-
3.66
-
after 11.4fold puification
4.2
Polyporus sulfureus
-
-
17.6
-
-
30.7
-
supernatant
32.86
-
beta-mannanase II
45.61
-
beta-mannanase I
186.5
-
-
208
-
50C, pH 2.4
3732
-
after 121.55fold purification
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2
Polyporus sulfureus
-
hydrolysis of Manbeta1-4GlcNAcbeta1-4GlcNAcbeta-Asn
2.8
Polyporus sulfureus
-
hydrolysis of p-nitrophenyl-beta-D-mannoside or beta-1,3-mannobiose
3.5 - 4.5
-
-
5 - 5.5
-
lysosomal acidic enzyme
5 - 8
-
nonlysosomal neutral enzyme
5.1 - 5.6
-
-
5.7
-
assay at, pH-optimum estimated for
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 6
-
pH 3.0: about 20% of maximal activity, pH 6.0: about 40% of maximal activity
3.2 - 5.2
-
pH 3.2: about 70% of maximal activity, pH 5.2: about 80% of maximal activity
3.7 - 4.6
-
about 95% of maximal activity at pH 3.7 and pH 4.6
4.5 - 8.5
-
pH 4.5: about 15% of maximal activity, pH 8.5: about 45% of maximal activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
-
30C: about 35% of maximal activity, 60C: about 55% of maximal activity
40 - 60
-
40C: about 55% of maximal activity, 60C: about 65% of maximal activity
40 - 55
-
40C: optimum, at optimal pH active up to 55C
60
-
30 min, complete loss of activity
70 - 90
-
70C: about 40% of maximal activity, 90C: about 80% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8
-
isozyme GM-2, isoelectric focusing
4.65
-
isozyme OT-1, isoelectric focusing
5.77
-
chromatofocusing, enzyme from magnum region of oviduct and egg albumen, a second enzyme form of pI 6.3 exists in egg albumen, a second form of pI 6.37 exists in magnum region of hen oviduct
6.3
-
chromatofocusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
albumen
Manually annotated by BRENDA team
-
highest specific activities of both alpha-and beta-mannosidases
Manually annotated by BRENDA team
Polyporus sulfureus
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
from patients with rheumatoid arthritis and patients with pigmented villous nodular synovitis
Manually annotated by BRENDA team
-
whole fly homogenates
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Oryza sativa subsp. indica
Oryza sativa subsp. indica
Oryza sativa subsp. indica
Oryza sativa subsp. indica
Oryza sativa subsp. indica
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10000
-
gel filtration
38000
-
beta-mannanase II, disc gel electrophoresis
43000
-
beta-mannanase I, disc gel electrophoresis
59000
-
gel filtration
64000
Polyporus sulfureus
-
gel filtration
75000
-
gradient PAGE
79000
-
gel filtration
89500
-
isozyme GM-2, SDS-PAGE
94000
-
-
99900
-
SDS-PAGE
100000
100300
-
isozyme OT-1, SDS-PAGE
104200
-
calculated from amino acid sequence
104600
-
isozyme GM-1, SDS-PAGE
110000
-
gel filtration
120000
-
gel filtration
130000
135000
-
beta-mannosidase A, enzyme from urine, nondenaturing gradient PAGE
137000
-
beta-mannosidase A, enzyme from kidney, gradient gel electrophoresis
140000
155000
-
beta-mannosidase B, enzyme from kidney, gradient gel electrophoresis
160000
-
beta-mannosidase B, enzyme from urine, nondenaturing gradient PAGE
180000
-
gel filtration
193000
-
gel filtration
200000
250000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
x-ray crystallography
monomer
tetramer
trimer
-
1 * 37000 + 1 * 49000 + 1 * 75000, beta-mannosidase A, SDS-PAGE; beta-mannosidase B, 2 * 49000 + 1 * 75000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalytic domain, to 1.6 A resolution. Space group P212121
molecular modeling and electron densitiy studies of wild-type and mutant E555Q
-
sitting drop vapour diffusion method with either 0.15-0.35 M NaBr and 6-12% PEG 3350, 0.1 M bis-Tris propane, pH 7, or 0.08-0.2 M KSCN, and 8-15% PEG 3350, 0.1 M bis-Tris propane, pH 7
-
wild-type in complex with inhibitors (5S,6R,8R)-5-(hydroxymethyl)-2-[(phenylamino)methyl]-5,6,7,8-tetrahydroimidazo[1,2-a]pyridine-6,7,8-triol, N-[(2Z,3R,5R,6S)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]ethane-1,2-diaminium, noeuromycin, isoquinuclidine, mutants Q646A, Y537A, N461A, W198G, W345A and W645A in complex with (5S,6R,8R)-5-(hydroxymethyl)-2-[(phenylamino)methyl]-5,6,7,8-tetrahydroimidazo[1,2-a]pyridine-6,7,8-triol
hanging drop vapour diffusion method
-
three-dimensional structure of CmMan5 in complex with isofagomine lactam is determined by X-ray crystallography to resolution 1.7 A
-
synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 7.5
-
37C, 2 h, stable
136039
2.8 - 9
Polyporus sulfureus
-
25C, 1 h, stable
136041
3.5
-
rapid loss of activity
136038
3.5 - 6
-
stable
136058
4 - 6
-
high stability at
136059
4.5 - 7
-
stable
136034
5 - 7
-
55C, 5 min, pH 5-7, 10-20% loss of activity
136047
5 - 8
-
40C, 30 min, stable up to
136030
5 - 5.5
-
37C, 1 h, stable
136038
5.9
-
exhibits highest pH stability at pH 5.9 after 5 h incubation at 50C
679572
6 - 10
-
unstable below pH 6.0 and above pH 10.0
136034
6.5 - 8
-
40C, 30 min, stable. Unstable below pH 6.5 and above pH 8.0
136031
6.5 - 9
-
pH 6.5: about 35% of maximal activity, pH 9.0: about 40% of maximal activity
136061
7
-
unstable above pH 7
136029
7.5 - 9
-
20C, 60 min, stable
136027
10
-
4C, 1 h, little loss of activity
136045
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
stable up to
76
-
half-life of 10 min at 76C
85
-
half-life: 18 h
90
-
half-life: 42 min
98
-
half-life: 2 min
101
melting temperature is 100.7C
102
half-life: 27 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
albumin, 1 mg/ml, stabilizes against high temperatures and low pH values
-
both forms of enzyme are partially stabilized by human albumin
-
EDTA, 1 mM, stabilizes
-
no inactivation by freezing and thawing
-
stable to dialysis between pH 4.5 and pH 7.5 with or without zinc in the medium
-
Stable to freeze-drying
-
stable to freezing, -20C, and thawing
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetonitrile
-
increases the rate of donor substrate hydrolysis to transglycosylation
dimethylformamide
-
increases the rate of donor substrate hydrolysis to transglycosylation
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
tends to be inactived by oxygen, dithiothreitol reactivates
-
136038
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, lyophilized enzyme, stable for over a year
-
-20C, freeze-dried enzyme, stable
-
-20C, stable
-
-20C, stable for 2 or 3 months
-
-80C, pH 5.0, chromatofocusing elution buffer, loss of activity within 1 month
-
4C, in aqueous solution, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-mannanase I and II
-
Mono S HR 5/5 column chromatography and Superdex 200 gel filtration
-
partial
Q-Sepharose column chromatography, SP-Sepharose column chromatography, and chromatofocusing on Polybuffer Exchanger PBE-94
-
recombinant
-
recombinant enzyme
TALON immobilized metal ion affinity chromatography, Q12 column chromatography, and S200 gel filtration
-
two forms of enzyme: beta-mannosidase A and B
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Aspergillus aculeatus strain PyrG
-
expressed in Escherichia coli strain BL21
-
expression in Escherichia coli
expression in HEK-293T cell
-
expression of catalytic domain in Escherichia coli
man2A gene is subcloned into the expression vector pET28A(+), yielding the plasmid pET28Man. The protein encoded by this plasmid carries a C-terminal His6 tag for purification, expression in Escherichia coli BL21
-
the gene encoding beta-mannosidase is localized to human chromosome 4
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E206G
-
complete loss of activity
E314G
-
complete loss of activity
D199A
-
low activity
E462A
-
low activity
E555A
-
low activity
E555Q
-
molecular modeling and electron densitiy studies of the Michaelis complex
W198A
-
low activity
W198G
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand
W200A
-
low activity
W345A
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand
W395A
-
low activity
E330A
-
mutant enzyme displays no activity against mannan or 4-nitrophenyl-beta-mannopyranoside
R641H
-
natural mutant identified in a patient with beta-mannosidisis. Patient is homozygous for the mutation, which leads to a residual activity of about 7% in the patient's leukocytes, 11% in lymphoblasts and 14% in plasma. Expression in transfected cells also results in 7% residual activity
D206N
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 11fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 60fold higher than that for 4-nitrophenyl beta-D-mannopyranoside
Q77R
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 2fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 1.1fold higher than that for 4-nitrophenyl beta-D-mannopyranoside
Q77R/D206N
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 8fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 1.4fold higher than that for 4-nitrophenyl beta-D-mannopyranoside
D206N
-
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 11fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 60fold higher than that for 4-nitrophenyl beta-D-mannopyranoside
-
Q77R
-
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 2fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 1.1fold higher than that for 4-nitrophenyl beta-D-mannopyranoside
-
Q77R/D206N
-
in contrast to the wild-type enzyme which shows a catalytic efficiency for 4-nitrophenyl beta-D-mannopyranoside that is 5fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 4fold higher than that for 4-nitrophenyl beta-D-glucopyranoside, the mutant enzyme shows highest catalytic efficiency towards 4-nitrophenyl beta-D-glucopyranoside, 8fold higher than that for 4-nitrophenyl beta-D-galactopyranoside and 1.4fold higher than that for 4-nitrophenyl beta-D-mannopyranoside
-
additional information
mutation associated with caprine beta-mannosidosis: single-base deletion at position 1398 of the coding sequence results in a shift in the reading frame, yielding a deduced peptide of 481 amino acids
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
-
mutation c.1922G>A, i.e. R641H, natural mutant identified in a patient with beta-mannosidisis. Patient is homozygous for the mutation, which leads to a residual activity of about 7% in the patient's leukocytes, 11% in lymphoblasts and 14% in plasma. Expression in transfected cells also results in 7% residual activity
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