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
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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
JCM 2947
-
-
Manually annotated by BRENDA team
JCM 2947
-
-
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
-
-
-
Manually annotated by BRENDA team
Phlebia radiata 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
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-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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-nitrophenol beta-D-mannopyranoside + H2O
4-nitrophenol + D-mannose
show the reaction diagram
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
show the reaction diagram
-
129% of the activity with 4-nitrophenyl-beta-D-glucopyranose
-
-
?
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 + alpha-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 + beta-D-mannose
show the reaction diagram
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + D-mannopyranose
show the reaction diagram
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + D-mannose
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-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-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
2.8 - 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
pH 4.0, 30C
0.033 - 3.1
4-nitrophenyl-beta-D-mannopyranose
0.1
4-nitrophenyl-beta-mannopyranose
-
pH 7.0, 37C, mutant enzyme E215A
2.17
4-O-beta-D-mannopyranosyl-D-mannopyranose
-
pH 7.0, 37C, wild-type enzyme
-
0.053
beta-D-mannosyl-1,4-beta-D-glucoside
-
pH 7.0, 37C, wild-type enzyme
166.7
Mannotriose
-
pH 7.0, 37C, wild-type enzyme
67.8
p-nitrophenyl beta-D-mannopyranoside
-
-
0.0097 - 157
p-nitrophenyl-beta-D-mannopyranoside
additional information
additional information
-
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
pH 4.0, 30C
12.7
4-nitrophenyl-beta-D-mannopyranose
pH 4.0, 30C
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
4.17
-
isoform M4, pH 5.6, 50C
4.2
Polyporus sulfureus
-
-
17.6
-
-
28.2
-
isoform M1, pH 5.6, 50C
30.7
-
supernatant
32.86
-
beta-mannanase II
38.7
-
isoform M2, pH 5.6, 50C
45.61
-
beta-mannanase I
52.8
-
isoform M3, pH 5.6, 50C
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
5 - 6
-
more than 90% of maximum 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)
Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10000
-
gel filtration
36000
x * 36000, SDS-PAGE of catalytic domain
37000
-
1 * 37000 + 1 * 49000 + 1 * 75000, beta-mannosidase A, SDS-PAGE
38000
-
beta-mannanase II, disc gel electrophoresis
43000
-
beta-mannanase I, disc gel electrophoresis
49000
-
1 * 37000 + 1 * 49000 + 1 * 75000, beta-mannosidase A, SDS-PAGE; beta-mannosidase B, 2 * 49000 + 1 * 75000, SDS-PAGE
56000
-
x * 56000, SDS-PAGE
56457
4 * 56457, calculated from sequence
56500
4 * 56500, SDS-PAGE
57500
-
x * 57500, SDS-PAGE
59000
-
gel filtration
64000
Polyporus sulfureus
-
gel filtration
79000
-
gel filtration
88000
-
x * 88000, SDS-PAGE
89500
-
isozyme GM-2, SDS-PAGE
95000
-
2 * 95000, SDS-PAGE
97000
x * 97000, SDS-PAGE
99900
-
SDS-PAGE
100000
100300
-
isozyme OT-1, SDS-PAGE
104200
-
calculated from amino acid sequence
104600
-
isozyme GM-1, SDS-PAGE
105000
-
x * 105000, SDS-PAGE
110000
-
gel filtration
114000
-
x * 114000, SDS-PAGE
120000
-
gel filtration
130000
135000
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression upon culture on complex media containing locust bean gum
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
Show AA Sequence (356 entries)
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