Information on EC 3.2.1.25 - beta-mannosidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
3.2.1.25
-
RECOMMENDED NAME
GeneOntology No.
beta-mannosidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides
show the reaction diagram
-
-
-
-
hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides
show the reaction diagram
substrate adopts a B2,5 transition state
Q8AAK6
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
exohydrolysis
-
PATHWAY
KEGG Link
MetaCyc Link
Other glycan degradation
-
SYSTEMATIC NAME
IUBMB Comments
beta-D-mannoside mannohydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
beta-D-mannosidase
-
-
-
-
beta-D-mannosidase
-
-
beta-D-mannosidase
-
-
beta-MAN
-
-
beta-mannosidase
-
-
-
-
beta-mannosidase
-
-
beta-mannosidase 2A
-
-
beta-mannoside mannohydrolase
-
-
-
-
betaMANNOS1
-
previously identified as a beta-D-glucosidase
BglB
Pyrococcus horikoshii DSM 12428
O58237
-
-
exo beta-mannanase
-
-
exo-beta-D-mannanase
-
-
-
-
GH2 beta-mannosidase
-
-
GM-1
-
isozyme
GM-1
Phlebia radiata Fr. 79
-
isozyme
-
GM-2
-
isozyme
GM-2
Phlebia radiata Fr. 79
-
isozyme
-
HvBII
B5A496
-
ManB
Aspergillus aculeatus F-50
-
-
-
mannanase
-
-
-
-
mannase
-
-
-
-
mannosidase 5A
-
-
mannosidase, beta-
-
-
-
-
OT-1
-
isozyme
OT-1
Phlebia radiata Fr. 79
-
isozyme
-
PH0501
O58237
locus name
PH0501
Pyrococcus horikoshii DSM 12428
O58237
locus name
-
CAS REGISTRY NUMBER
COMMENTARY
9025-43-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Pekin-type drake
-
-
Manually annotated by BRENDA team
strain F-50
-
-
Manually annotated by BRENDA team
Aspergillus aculeatus F-50
strain F-50
-
-
Manually annotated by BRENDA team
strain K4
-
-
Manually annotated by BRENDA team
Aspergillus awamori K4
strain K4
-
-
Manually annotated by BRENDA team
AM-001
-
-
Manually annotated by BRENDA team
N16-5
UniProt
Manually annotated by BRENDA team
Bacillus sp. AM-001
AM-001
-
-
Manually annotated by BRENDA team
patient with beta-mannosodosis, an inborn lysosomal storage disorder
-
-
Manually annotated by BRENDA team
cultivar Clipper
-
-
Manually annotated by BRENDA team
var. distichum
UniProt
Manually annotated by BRENDA team
L. cv. Grand Rapids
-
-
Manually annotated by BRENDA team
subsp. sativa
-
-
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
Pyrococcus horikoshii DSM 12428
-
UniProt
Manually annotated by BRENDA team
Mill cv. Glamour
-
-
Manually annotated by BRENDA team
Solanum lycopersicum Mill.
Mill.
-
-
Manually annotated by BRENDA team
strain 5068
-
-
Manually annotated by BRENDA team
Thermotoga neapolitana 5068
5068
-
-
Manually annotated by BRENDA team
Thermotoga neapolitana 5068
strain 5068
-
-
Manually annotated by BRENDA team
Trichosporon cutaneum JCM 2947
JCM 2947
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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-methylumbelliferyl beta-D-mannoside + H2O
4-methylumbelliferone + beta-D-mannose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl beta-D-mannoside + H2O
4-methylumbelliferone + beta-D-mannose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl beta-D-mannoside + H2O
4-methylumbelliferone + beta-D-mannose
show the reaction diagram
-
4-methylumbelliferyl beta-D-mannopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
O58237, -
catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl beta-D-galactopyranoside is 20% compared to catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
Pyrococcus horikoshii DSM 12428
O58237
catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl beta-D-galactopyranoside is 20% compared to catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
4-nitrophenyl beta-D-glucopyranose + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranose + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
B5A496, -
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
O58237, -
catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl beta-D-glucopyranoside is 26% compared to catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl beta-D-mannopyranoside. The catalytic efficiency (kcat/Km) of the mutant enzymes Q77R, D206N and Q77R/D206N for 4-nitrophenyl beta-D-glucopyranoside is higher then that for 4-nitrophenyl beta-D-galactopyranoside and 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
Pyrococcus horikoshii DSM 12428
O58237
catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl beta-D-glucopyranoside is 26% compared to catalytic efficiency (kcat/Km) of the wild-type enzyme for 4-nitrophenyl beta-D-mannopyranoside. The catalytic efficiency (kcat/Km) of the mutant enzymes Q77R, D206N and Q77R/D206N for 4-nitrophenyl beta-D-glucopyranoside is higher then that for 4-nitrophenyl beta-D-galactopyranoside and 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O |
4-nitrophenol + beta-D-mannose
show the reaction diagram
O58237, -
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O |
4-nitrophenol + beta-D-mannose
show the reaction diagram
Pyrococcus horikoshii DSM 12428
O58237
-
-
-
?
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
B5A496, -
-
-
-
?
4-nitrophenyl-beta-D-mannopyranose + H2O
4-nitrophenol + beta-D-mannose
show the reaction diagram
-
238% of the activity with 4-nitrophenyl-beta-D-glucopyranose
-
-
?
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 + H2O
4-nitrophenol + D-mannopyranose
show the reaction diagram
A7LFP5
-
-
-
?
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-xylopyranose + 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
-
-
?
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-mannohexaitol + H2O
?
show the reaction diagram
-
-
-
-
?
beta-D-mannopentaitol + 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-D-mannotriitol + H2O
?
show the reaction diagram
-
-
-
-
?
beta-D-mannotriitol + H2O
?
show the reaction diagram
-
-
-
-
?
beta-mannotetraitol + H2O
?
show the reaction diagram
-
-
-
-
?
beta-mannotetraitol + H2O
?
show the reaction diagram
-
-
-
-
?
beta1-4-mannobiose + H2O
?
show the reaction diagram
-
-
-
-
?
beta1-4-mannobiose + H2O
?
show the reaction diagram
Polyporus sulfureus
-
-
-
-
?
beta1-4-mannobiose + H2O
?
show the reaction diagram
Tremella fuciformis T-7
-
-
-
-
?
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)GlcNAc + H2O
mannose + GlcNAc
show the reaction diagram
-
-
-
-
?
Man-(beta1-4)GlcNAc + H2O
mannose + GlcNAc
show the reaction diagram
Polyporus sulfureus
-
-
-
?
Man-(beta1-4)GlcNAc + H2O
mannose + GlcNAc
show the reaction diagram
Tremella fuciformis T-7
-
-
-
-
?
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
-
-
-
?
Manbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta-Asn + H2O
mannose + GlcNAcbeta(1-4)GlcNAcbeta-Asn
show the reaction diagram
Polyporus sulfureus
-
-
-
-
?
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
-
glucomannans and galactomannans are completely hydrolyzed
-
-
?
mannan + H2O
mannose + ?
show the reaction diagram
-
galactomannan
-
?
mannobiose + 1-propanol
?
show the reaction diagram
Aspergillus awamori, Aspergillus awamori K4
-
transglycosylation reaction, 50% transfer ratio
-
-
-
mannobiose + arabinose
?
show the reaction diagram
Aspergillus awamori, Aspergillus awamori K4
-
transglycosylation reaction, 6.4% transfer ratio
-
-
-
mannobiose + ethanol
?
show the reaction diagram
Aspergillus awamori, Aspergillus awamori K4
-
transglycosylation reaction, 41.1% transfer ratio
-
-
-
mannobiose + fructose
?
show the reaction diagram
Aspergillus awamori, Aspergillus awamori K4
-
transglycosylation reaction, 72.3% transfer ratio
-
-
-
mannobiose + galactose
?
show the reaction diagram
Aspergillus awamori, Aspergillus awamori K4
-
transglycosylation reaction, 14.2% transfer ratio
-
-
-
mannobiose + glucose
?
show the reaction diagram
-
transglycosylation reaction, 40.1% transfer ratio
-
-
-
mannobiose + H2O
?
show the reaction diagram
-
-
-
-
?
mannobiose + H2O
?
show the reaction diagram
-
-
-
-
?
mannobiose + H2O
?
show the reaction diagram
Bacillus sp. AM-001
-
-
-
-
?
mannobiose + methanol
?
show the reaction diagram
-
transglycosylation reaction, 42.6% transfer ratio
-
-
-
mannobiose + N-acetylglucosamine
?
show the reaction diagram
-
transglycosylation reaction, 1.4% transfer ratio
-
-
-
mannobiose + xylose
?
show the reaction diagram
-
transglycosylation reaction, 18.4% transfer ratio
-
-
-
mannopentaose + H2O
?
show the reaction diagram
Bacillus sp., Bacillus sp. AM-001
-
-
-
-
?
mannopyranosylamine + H2O
?
show the reaction diagram
-
-
-
-
?
mannotetraose + H2O
?
show the reaction diagram
-
-
-
-
?
mannotetraose + H2O
?
show the reaction diagram
-
-
-
-
?
mannotetraose + H2O
?
show the reaction diagram
Bacillus sp. AM-001
-
-
-
-
?
mannotriose + H2O
?
show the reaction diagram
-
-
-
-
?
mannotriose + H2O
?
show the reaction diagram
Polyporus sulfureus
-
-
-
-
?
mannotriose + H2O
?
show the reaction diagram
-
-
-
-
?
mannotriose + H2O
?
show the reaction diagram
-
beta1-4-D-mannotriose
-
-
?
mannotriose + H2O
?
show the reaction diagram
Bacillus sp. AM-001
-
-
-
-
?
mannotriose + H2O
?
show the reaction diagram
Tremella fuciformis T-7
-
beta1-4-D-mannotriose
-
-
?
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
-
-
-
-
?
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
Solanum lycopersicum, Solanum lycopersicum Mill.
-
-
-
-
?
p-nitrophenyl beta-D-mannopyranoside + H2O
p-nitrophenol + beta-D-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl beta-D-mannopyranoside + H2O
p-nitrophenol + beta-D-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl beta-D-mannopyranoside + H2O
p-nitrophenol + beta-D-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl beta-D-mannopyranoside + H2O
p-nitrophenol + beta-D-mannose
show the reaction diagram
Thermotoga neapolitana 5068
-
-
-
-
?
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-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
-
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
Polyporus sulfureus
-
-
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
no activity with p-nitrophenyl-alpha-D-mannoside
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
p-nitrophenyl-beta-D-mannopyranoside
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
hydrolyses 4-nitrophenyl-beta-D-mannoside three times faster than p-nitrophenyl-beta-D-glucoside
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
Phlebia radiata Fr. 79
-
-
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
Thermotoga neapolitana 5068
-
-
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
Aspergillus aculeatus F-50
-
-
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
Trichosporon cutaneum JCM 2947
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
Bacillus sp. AM-001
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
Tremella fuciformis T-7
-
-
-
-
?
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
-
-
-
-
?
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
-
-
?
methyl alpha-D-mannopyranoside + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-, Q95327
-
-
-
?
additional information
?
-
-
extensively hydrolyzes the carbohydrate portion of glycopeptides obtained from ovalbumin
-
-
?
additional information
?
-
-
hydrolyses D-galactose substituted manno-oligosaccharides up to, but not beyond, a side group
-
-
?
additional information
?
-
Polyporus sulfureus
-
the enzyme liberates mannose from core glycopeptide isolated from Taka-amylase A and alpha1-acid glycoprotein
-
-
?
additional information
?
-
-
the enzyme plays a key role in the hydrolysis of galactomannan in germinating guar seed
-
-
?
additional information
?
-
-
locust bean gum and guar flour are the best substrates for enzyme formation
-
-
?
additional information
?
-
-
goat liver contains both a lysosomal beta-mannosidase, acidic enzyme form, deficient in beta-mannosidosis, and a neutral nonlysosomal
-
-
-
additional information
?
-
-
deficiency of lysosomal beta-mannosidase activity results in a severe neurodegenerative disease in goats and cattle and a relatively milder phenotype in humans
-
-
?
additional information
?
-
-
in 4 cultures induced by locust bean gum
-
-
?
additional information
?
-
-
beta-mannosidase and endo-beta-mannanase are involved in the mobilization of the mannan-containing cell walls of the tomato seed endosperm. A lack of coordination of the activities of these two enzymes within individuals of a population
-
-
-
additional information
?
-
-
coincidental and substantial increase in activity of both beta-mannosidase and beta-mannanase after 48 h, following germination, suggests the cooperation of both enzymes in the degradation of endosperm cell wall galactomannan
-
-
-
additional information
?
-
-
Glu519 is the catalytic nucleophile in beta-mannosidase 2A
-
-
-
additional information
?
-
-
no hydrolysis of p-nitrophenyl derivatives of alpha-mannose, beta-N-acetylglucosamine, beta-glucose, beta-xylose, beta-cellobiose or beta-gentiobiose
-
-
-
additional information
?
-
-
CmMan5A releases beta-1,4-linked mannose substrates exclusively from the nonreducing end
-
-
-
additional information
?
-
-
4-nitrophenyl-N-acetyl-beta-D-glucosaminide, 4-nitrophenyl-beta-D-xyloside, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-gentiobioside, and 4-nitrophenyl-cellobioside are no substrates
-
-
-
additional information
?
-
-
in addition to hydrolysis, enzyme catalyzes transglycosylation with substrate 4-nitrophenyl-beta-D-mannopyranoside to yield 4-nitrophenyl-mannobiosides and 4-nitrophenyl mannotriosides containing beta-(1,4) and beta-(1,3) linkages. The rate of donor substrate hydrolysis increases in presence of acetonitrile and dimethylformamide
-
-
-
additional information
?
-
A7LFP5
no substrate: 4-nitrophenyl-alpha-D-mannose
-
-
-
additional information
?
-
-
comparison with the activities of rice family GH1 glycoside hydrolases
-
-
-
additional information
?
-
-
the Michaelis complex of the beta-mannosidase Man2A shows distortion to a 1S5 conformation supporting catalysis through a boat conformation
-
-
-
additional information
?
-
-
calculation of conformational free-energy surface of a beta-D-mannopyranose molecule associated with the ideal Stoddart conformational diagram. 1S5 is among the most stable conformers and simultaneously is the most preactivated conformation in terms of elongation/shortening of the C1-O1/C1-O5 bonds, C1-O1 orientation, and charge development at the anomeric carbon. Analysis of the computed free-energy surface gives support to the proposed 1S5-B2,5-OS2 catalytic itinerary. The degree of preactivation of the substrate in glycoside hydrolases is related to the properties of an isolated sugar ring. Introduction of a simple preactivation index integrating several structural, electronic, and energetic properties that can be used to predict the conformation of the substrate in the Michaelis complex of any glycoside hydrolase
-
-
-
additional information
?
-
B5A496, -
in glycoside recognition and substrate specificity of HvBII, a combination of the following determinants is likely to play key roles: the inherent conformational and spatial flexibilities of gluco- and manno-configured substrates in the enzymes' active sites, the subtle differences in the spatial disposition of active site residues and their capacities to form interactions with specific groups of substrates, and the small variations in the charge distributions and shapes of the catalytic sites
-
-
-
additional information
?
-
Solanum lycopersicum Mill.
-
coincidental and substantial increase in activity of both beta-mannosidase and beta-mannanase after 48 h, following germination, suggests the cooperation of both enzymes in the degradation of endosperm cell wall galactomannan
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-, Q95327
-
-
-
?
additional information
?
-
-
the enzyme plays a key role in the hydrolysis of galactomannan in germinating guar seed
-
-
?
additional information
?
-
-
locust bean gum and guar flour are the best substrates for enzyme formation
-
-
?
additional information
?
-
-
goat liver contains both a lysosomal beta-mannosidase, acidic enzyme form, deficient in beta-mannosidosis, and a neutral nonlysosomal
-
-
-
additional information
?
-
-
deficiency of lysosomal beta-mannosidase activity results in a severe neurodegenerative disease in goats and cattle and a relatively milder phenotype in humans
-
-
?
additional information
?
-
-
in 4 cultures induced by locust bean gum
-
-
?
additional information
?
-
-
beta-mannosidase and endo-beta-mannanase are involved in the mobilization of the mannan-containing cell walls of the tomato seed endosperm. A lack of coordination of the activities of these two enzymes within individuals of a population
-
-
-
additional information
?
-
Solanum lycopersicum, Solanum lycopersicum Mill.
-
coincidental and substantial increase in activity of both beta-mannosidase and beta-mannanase after 48 h, following germination, suggests the cooperation of both enzymes in the degradation of endosperm cell wall galactomannan
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
Ca(NO3)2, 22% stimulation at 0.5 mM
Ca2+
-
slight activation
MgSO4
-
26% stimulation at 10 mM
Mn2+
-
slight activation
ZnSO4
-
0.5 mM, 25% stimulation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
O58237, -
-
(5S,6R,8R)-5-(hydroxymethyl)-2-(2-phenylethyl)-5,6,7,8-tetrahydroimidazo[1,2-a]pyridine-6,7,8-triol
Q8AAK6
persuasive transition state mimic
(5S,6R,8R)-5-(hydroxymethyl)-2-(phenoxymethyl)-5,6,7,8-tetrahydroimidazo[1,2-a]pyridine-6,7,8-triol
Q8AAK6
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
Q8AAK6
persuasive transition state mimic
2-amino-2-deoxy-D-mannose
-
-
2-amino-2-deoxy-D-mannose
-
competitive
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
B5A496, -
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
B5A496, -
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
-
Ag+
Polyporus sulfureus
-
2 mM, complete inhibition
Ag+
A7LFP5
1.5 mM, no residual activity
beta-1,4-mannooligosaccharides
-
inhibit binding of the enzyme to galactomannans
-
Ca2+
-
5 mM Ca(NO3)2, 45% inhibition
Co2+
A7LFP5
1.5 mM, 80% residual activity
Cu2+
-
0.2 mM, 76% inhibition
Cu2+
Polyporus sulfureus
-
-
Cu2+
A7LFP5
1.5 mM, no residual activity
D-mannono-1,4-lactone
-
-
D-mannosamine
-
-
D-mannose
-
with p-nitrophenyl-beta-D-mannopyranoside as substrate
D-mannose
Polyporus sulfureus
-
-
D-mannose
-
hydrolysis of p-nitrophenyl beta-D-mannoside, competitive
dimethyl sulfoxide
A7LFP5
5 mM, no residual activity
Dimethylformamide
A7LFP5
5 mM, no residual activity
ethanol
A7LFP5
5 mM, no residual activity
Fe3+
Polyporus sulfureus
-
-
-
guanidine hydrochloride
-
0.6 M, 30% inhibition
Hg2+
Polyporus sulfureus
-
-
Hg2+
-
0.05 mM, 50% inhibition
iodoacetate
A7LFP5
5 mM, no residual activity
isofagomine lactam
-
-
isoquinuclidine
Q8AAK6
-
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
Q8AAK6
-
N-[(2Z,3R,5R,6S)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]propan-1-aminium
Q8AAK6
-
p-nitrophenyl-alpha-D-mannopyranoside
-
activates at low concentration, competitively inhibits at higher concentrations, 2-3 mM
p-nitrophenyl-alpha-D-mannopyranoside
-
hydrolysis of p-nitrophenyl-beta-D-mannoside
p-nitrophenyl-beta-mannoside
-
above 0.4 mM
Pb2+
A7LFP5
1.5 mM, 78% residual activity
PMSF
Polyporus sulfureus
-
-
Sodium dodecyl sulfate
A7LFP5
5 mM, no residual activity
Zn2+
-
0.1 mM, 35% inhibition
Zn2+
-
10 mM ZnSO4, 30% inhibition
Zn2+
Polyporus sulfureus
-
-
Zn2+
A7LFP5
1.5 mM, no residual activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
0.05%, stabilizes
EDTA
-
activates
EDTA
-
11% stimulation at 5 mM
p-nitrophenyl-alpha-D-mannopyranoside
-
activates at low concentration, competitively inhibits at higher concentrations, 2-3 mM
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0028
-
2,4-dinitrophenyl-beta-D-mannopyranoside
-
mutant enzyme E462A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.015
-
2,4-dinitrophenyl-beta-D-mannopyranoside
-
mutant enzyme N461A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.088
-
2,4-dinitrophenyl-beta-D-mannopyranoside
-
wild type enzyme, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.089
-
2,4-dinitrophenyl-beta-D-mannopyranoside
-
mutant enzyme E555A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.13
-
4-methylumbelliferyl beta-D-mannopyranoside
-
beta-mannosidase B
0.35
-
4-methylumbelliferyl beta-D-mannopyranoside
-
beta-mannosidase A
0.5
-
4-methylumbelliferyl beta-D-mannopyranoside
-
-
0.56
-
4-methylumbelliferyl beta-D-mannopyranoside
-
-
0.8
-
4-methylumbelliferyl beta-D-mannopyranoside
-
-
0.91
-
4-methylumbelliferyl beta-D-mannopyranoside
-
-
7.3
-
4-nitrophenyl beta-D-galactopyranoside
O58237, -
pH 5.0, 90C, wild-type enzyme
7.8
-
4-nitrophenyl beta-D-galactopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme D206N
16.8
-
4-nitrophenyl beta-D-galactopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R
36.1
-
4-nitrophenyl beta-D-galactopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R/D206N
0.3
-
4-nitrophenyl beta-D-glucopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme D206N
13.5
-
4-nitrophenyl beta-D-glucopyranoside
O58237, -
pH 5.0, 90C, wild-type enzyme
16.2
-
4-nitrophenyl beta-D-glucopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R
30.4
-
4-nitrophenyl beta-D-glucopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R/D206N
0.44
-
4-nitrophenyl beta-D-mannopyranoside
O58237, -
pH 5.0, 90C, wild-type enzyme
-
0.68
-
4-nitrophenyl beta-D-mannopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R/D206N
-
1.1
-
4-nitrophenyl beta-D-mannopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R
-
3.2
-
4-nitrophenyl beta-D-mannopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme D206N
-
0.5
-
4-nitrophenyl-beta-D-glucopyranose
B5A496, -
pH 4.0, 30C
0.25
-
4-nitrophenyl-beta-D-mannopyranose
B5A496, -
pH 4.0, 30C
1.6
-
4-nitrophenyl-beta-D-mannopyranose
-
pH 7.0, 37C, wild-type enzyme
2.5
3
4-nitrophenyl-beta-D-mannopyranoside
A7LFP5
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
-
Beta-D-mannohexaitol
-
-
12.5
-
Beta-D-mannohexaitol
-
-
2.8
-
beta-D-mannopentaitol
-
-
12.5
-
beta-D-mannopentaitol
-
-
6.1
-
beta-D-mannosyl-1,4-beta-D-glucoside
-
pH 7.0, 37C, wild-type enzyme
12
-
beta-D-mannotetraitol
-
-
12.5
-
beta-D-mannotetraitol
-
-
12.5
-
beta-D-mannotriitol
-
-
80
-
beta-D-mannotriitol
-
-
0.9
-
mannobiose
-
pH 7.0, 37C, wild-type enzyme
1.2
-
mannotriitol
-
enzyme from endosperm
10
-
mannotriitol
-
enzyme from cotyledons
3.22
-
Naphthyl-beta-D-mannopyranoside
-
-
2.33
-
o-nitrophenyl-beta-D-mannopyranoside
-
-
3
-
o-nitrophenyl-beta-D-mannopyranoside
-
-
0.55
-
p-nitrophenyl beta-D-mannopyranoside
-
-
3.1
-
p-nitrophenyl beta-D-mannopyranoside
-
-
9
-
p-nitrophenyl beta-D-mannopyranoside
-
-
0.017
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme W395A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.079
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme W198A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.18
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme E555A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.19
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme E462A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin; wild type enzyme, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.3
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
0.3
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
0.31
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme Q646A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin; mutant enzyme Y537A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.43
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme N461A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.46
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
0.5
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
1.3
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
1.43
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
2.2
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
10
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme W200A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin; mutant enzyme W645A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
11
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme D199A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.12
-
p-nitrophenyl-beta-D-mannoside
-
-
0.29
-
p-nitrophenyl-beta-D-mannoside
-
enzyme from cotyledons; enzyme from endosperm
0.29
-
p-nitrophenyl-beta-D-mannoside
-
enzyme from cotyledons
0.29
-
p-nitrophenyl-beta-D-mannoside
-
isozyme GM-1
0.32
-
p-nitrophenyl-beta-D-mannoside
-
-
0.34
-
p-nitrophenyl-beta-D-mannoside
-
isozyme OT-1
0.7
-
p-nitrophenyl-beta-D-mannoside
-
lysosomal, acidic enzyme
0.83
-
p-nitrophenyl-beta-D-mannoside
-
enzyme from endosperm
1.1
-
p-nitrophenyl-beta-D-mannoside
-
in sodium citrate buffer (100 mM, pH 3)
1.6
-
p-nitrophenyl-beta-D-mannoside
Polyporus sulfureus
-
-
1.78
-
p-nitrophenyl-beta-D-mannoside
-
isozyme GM-2
2
-
p-nitrophenyl-beta-D-mannoside
-
about
2.1
-
p-nitrophenyl-beta-D-mannoside
-
-
2.4
-
p-nitrophenyl-beta-D-mannoside
-
-
2.9
-
p-nitrophenyl-beta-D-mannoside
-
-
5
-
p-nitrophenyl-beta-D-mannoside
-
nonlysosomal, neutral enzyme
6.5
-
phenyl beta-D-mannoside
-
-
7.1
-
phenyl beta-D-mannoside
-
-
0.1
-
Mannotriose
-
pH 7.0, 37C, wild-type enzyme
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00183
-
2,4-dinitrophenyl-beta-D-mannopyranoside
-
mutant enzyme E555A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.008
-
2,4-dinitrophenyl-beta-D-mannopyranoside
-
mutant enzyme E462A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.85
-
2,4-dinitrophenyl-beta-D-mannopyranoside
-
mutant enzyme N461A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
214.4
-
2,4-dinitrophenyl-beta-D-mannopyranoside
-
wild type enzyme, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
13.5
-
4-nitrophenyl beta-D-galactopyranoside
O58237, -
pH 5.0, 90C, wild-type enzyme
14.2
-
4-nitrophenyl beta-D-galactopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R
66.5
-
4-nitrophenyl beta-D-galactopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R/D206N
571
-
4-nitrophenyl beta-D-galactopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme D206N
25.5
-
4-nitrophenyl beta-D-glucopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R
34.4
-
4-nitrophenyl beta-D-glucopyranoside
O58237, -
pH 5.0, 90C, wild-type enzyme
252
-
4-nitrophenyl beta-D-glucopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme D206N
439
-
4-nitrophenyl beta-D-glucopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R/D206N
1.6
-
4-nitrophenyl beta-D-mannopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R
-
4.2
-
4-nitrophenyl beta-D-mannopyranoside
O58237, -
pH 5.0, 90C, wild-type enzyme
-
6.8
-
4-nitrophenyl beta-D-mannopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R/D206N
-
45
-
4-nitrophenyl beta-D-mannopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme D206N
-
0.5
-
4-nitrophenyl-beta-D-glucopyranose
B5A496, -
pH 4.0, 30C
0.033
-
4-nitrophenyl-beta-D-mannopyranose
-
pH 7.0, 37C, wild-type enzyme
3.1
-
4-nitrophenyl-beta-D-mannopyranose
B5A496, -
pH 4.0, 30C
0.1
-
4-nitrophenyl-beta-mannopyranose
-
pH 7.0, 37C, mutant enzyme E215A
0.053
-
beta-D-mannosyl-1,4-beta-D-glucoside
-
pH 7.0, 37C, wild-type enzyme
2.17
-
mannobiose
-
pH 7.0, 37C, wild-type enzyme
67.8
-
p-nitrophenyl beta-D-mannopyranoside
-
-
0.0097
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme E555A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.045
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme D199A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.092
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme E462A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.25
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme N461A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.478
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme W645A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
0.886
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme W395A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
3.5
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme W198A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
6.08
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme W395A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
15.9
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme Y537A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
20.38
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme W198A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
26.85
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme Y537A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
34.43
-
p-nitrophenyl-beta-D-mannopyranoside
-
mutant enzyme Q646A, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
128.1
-
p-nitrophenyl-beta-D-mannopyranoside
-
wild type enzyme, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
157
-
p-nitrophenyl-beta-D-mannopyranoside
-
wild type enzyme, at 37C in 43.5 mM sodium phosphate, 10 mM citric acid buffer, pH 5.6, containing 1 mg/ml bovine serum albumin
166.7
-
Mannotriose
-
pH 7.0, 37C, wild-type enzyme
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]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.85
-
4-nitrophenyl beta-D-galactopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R
228467
1.8
-
4-nitrophenyl beta-D-galactopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R/D206N
228467
1.9
-
4-nitrophenyl beta-D-galactopyranoside
O58237, -
pH 5.0, 90C, wild-type enzyme
228467
75.8
-
4-nitrophenyl beta-D-galactopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme D206N
228467
1.6
-
4-nitrophenyl beta-D-glucopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R
80189
2.58
-
4-nitrophenyl beta-D-glucopyranoside
O58237, -
pH 5.0, 90C, wild-type enzyme
80189
14.4
-
4-nitrophenyl beta-D-glucopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R/D206N
80189
870
-
4-nitrophenyl beta-D-glucopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme D206N
80189
1.4
-
4-nitrophenyl beta-D-mannopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R
0
9.8
-
4-nitrophenyl beta-D-mannopyranoside
O58237, -
pH 5.0, 90C, wild-type enzyme
0
9.9
-
4-nitrophenyl beta-D-mannopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme Q77R/D206N
0
14.7
-
4-nitrophenyl beta-D-mannopyranoside
O58237, -
pH 5.0, 90C, mutant enzyme D206N
0
1
-
4-nitrophenyl-beta-D-glucopyranose
B5A496, -
pH 4.0, 30C
263541
12.7
-
4-nitrophenyl-beta-D-mannopyranose
B5A496, -
pH 4.0, 30C
227767
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000014
-
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
O58237, -
pH 5.0, 90C, mutant enzyme D206N
0.02
-
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
O58237, -
pH 5.0, 90C, mutant enzyme Q77R/D206N
0.1
-
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
O58237, -
pH 5.0, 90C, wild-type enzyme
0.11
-
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
O58237, -
pH 5.0, 90C, mutant enzyme Q77R
0.000057
-
(5S,6R,8R)-5-(hydroxymethyl)-2-(2-phenylethyl)-5,6,7,8-tetrahydroimidazo[1,2-a]pyridine-6,7,8-triol
Q8AAK6
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
Q8AAK6
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
Q8AAK6
pH 5.6
0.41
-
2-deoxy-2-fluoro-beta-D-mannosyl fluoride
-
-
0.095
-
4-nitrophenyl beta-D-thioglucoside
B5A496, -
pH 4.0, 30C
-
0.266
-
4-nitrophenyl beta-D-thiomannoside
B5A496, -
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
Q8AAK6
pH 5.6
0.0019
-
N-[(2Z,3R,5R,6S)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]propan-1-aminium
Q8AAK6
pH 5.6
0.000975
-
noeuromycin
Q8AAK6
pH 5.6
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.3
-
-
culture filtrate
0.506
-
-
-
0.996
-
-
-
1.083
-
-
-
1.772
-
-
-
3.66
-
-
after 11.4fold puification
4.2
-
Polyporus sulfureus
-
-
4.37
-
-
-
17.6
-
-
-
20.6
-
-
-
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
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
assay described, enzyme activity measured in homogenates of 10 to 15 male and female flies before and after sucrose meals, monitoring by spectroscopy, values of relative activity shown, reduced activity after feeding with sucrose observed
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
-
hydrolysis of p-nitrophenyl-beta-D-mannopyranoside, at 55C
4.2
-
-
-
4.3
-
-
-
4.5
-
-
-
4.75
-
O58237, -
-
5
5.5
-
lysosomal acidic enzyme
5
8
-
nonlysosomal neutral enzyme
5
-
A7LFP5
-
5.1
5.6
-
-
5.7
-
-
assay at, pH-optimum estimated for
6.5
-
-
at 40C
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
A7LFP5
-
50
-
-
-
55
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
60
-
30C: about 35% of maximal activity, 60C: about 55% of maximal activity
40
55
-
40C: optimum, at optimal pH active up to 55C
40
60
-
40C: about 55% of maximal activity, 60C: about 65% of maximal activity
60
-
-
30 min, complete loss of activity
70
90
-
70C: about 40% of maximal activity, 90C: about 80% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.8
-
-
isozyme GM-2, isoelectric focusing
4.65
-
-
isozyme OT-1, isoelectric focusing
4.8
-
-
isoelectric focusing
4.8
-
-
isozyme GM-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 ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
solid culture, with coffee waste and wheat bran
Manually annotated by BRENDA team
Aspergillus awamori K4
-
solid culture, with coffee waste and wheat bran
-
Manually annotated by BRENDA team
Trichosporon cutaneum JCM 2947
-
-
-
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
-
peripheral blood leukocyte
Manually annotated by BRENDA team
-
magnum region
Manually annotated by BRENDA team
-
cotyledon and endosperm tissue
Manually annotated by BRENDA team
-
cotyledons, in association with a cellulosic cell-wall fraction
Manually annotated by BRENDA team
-
activity increases in the micropylar and lateral endosperm during and following germination
Manually annotated by BRENDA team
-
increase in activity following germination
Manually annotated by BRENDA team
Solanum lycopersicum Mill.
-
increase in activity following germination
-
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
A7LFP5
transcription in all cells and tissues tested
Manually annotated by BRENDA team
additional information
-
enzymic activities decrease significantly during the postbreeding resting season compared to the breeding season
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
ionically associated with a matrix fraction, most likely the cell wall
Manually annotated by BRENDA team
Solanum lycopersicum Mill.
-
ionically associated with a matrix fraction, most likely the cell wall
-
Manually annotated by BRENDA team
Thermotoga neapolitana 5068
-
-
-
Manually annotated by BRENDA team
-
goat liver contains both an acid lysosomal beta-mannosidase, deficient in beta-mannosidosis, and a neutral nonlysosomal beta-mannosidase
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
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
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10000
-
-
gel filtration
38000
-
-
beta-mannanase II, disc gel electrophoresis
43000
-
-
beta-mannanase I, disc gel electrophoresis
54000
-
-
enzyme from cotyledons, gel filtration
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
-
-
enzyme from endosperm, gel filtration
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
-
-
equilibrium sedimentation
130000
-
-
gel filtration
130000
-
-
SDS-PAGE
135000
-
-
beta-mannosidase A, enzyme from urine, nondenaturing gradient PAGE
137000
-
-
beta-mannosidase A, enzyme from kidney, gradient gel electrophoresis
140000
-
-
gel filtration
140000
-
-
gel filtration
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
-
-
gel filtration
250000
-
O58237, -
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 94000, SDS-PAGE
?
-
x * 94000, SDS-PAGE
?
-
x * 88000, SDS-PAGE
?
-
x * 114000, SDS-PAGE
?
-
x * 105000, SDS-PAGE
?
-
x * 57500, SDS-PAGE
?
-
x * 200000-220000, SDS-PAGE
?
-
x * 56000, SDS-PAGE
?
A7LFP5
x * 97000, SDS-PAGE
?
Q5YEX6
x * 36000, SDS-PAGE of catalytic domain
?
Bacillus sp. AM-001
-
x * 94000, SDS-PAGE
-
?
-
x * 36000, SDS-PAGE of catalytic domain
-
?
Solanum lycopersicum Mill.
-
x * 56000, SDS-PAGE
-
?
Thermotoga neapolitana 5068
-
x * 200000-220000, SDS-PAGE
-
?
Trichosporon cutaneum JCM 2947
-
x * 114000, SDS-PAGE
-
dimer
-
2 * 135000, SDS-PAGE
dimer
-
2 * 95000, SDS-PAGE
dimer
-
2 * 130000
dimer
Thermotoga neapolitana 5068
-
2 * 95000, SDS-PAGE
-
homodimer
-
x-ray crystallography
monomer
-
1 * 59000, SDS-PAGE
tetramer
O58237, -
4 * 56457, calculated from sequence; 4 * 56500, SDS-PAGE
tetramer
Pyrococcus horikoshii DSM 12428
-
4 * 56457, calculated from sequence; 4 * 56500, SDS-PAGE
-
trimer
-
1 * 37000 + 1 * 49000 + 1 * 75000, beta-mannosidase A, SDS-PAGE; beta-mannosidase B, 2 * 49000 + 1 * 75000, SDS-PAGE
monomer
-
1 * 38000, beta-mannanase II, SDS-PAGE; 1 * 43000, beta-mannanase I, SDS-PAGE
additional information
-
a 90000 Da peptide and a 100000 Da peptide is detected by SDS-PAGE
additional information
-
peptides of 100000 Da and 110000 Da and a minor peptide of 84000 Da detected by SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
-
glycoprotein
Aspergillus aculeatus F-50
-
-
-
glycoprotein
-
neutral sugar content: 17.8%. Presence of galactose, mannose and N-acetylglucosamine in a molar ratio of 1.3:7:1
glycoprotein
-
oligosaccharide is attached to the protein in a GlcNAc-Asn linkage, mannose and glucosamine in the ratio of 2.5 or 3:1
glycoprotein
-
contains 17% N-linked carbohydrate
glycoprotein
-
N-linked carbohydrate
glycoprotein
-
the 90000 Da peptide is glycosylated mainly by mannose, the 100000 Da peptide contains complex oligosaccharides
glycoprotein
-
contains 7% carbohydrate
glycoprotein
-
contains 3.1% carbohydrate
glycoprotein
-
enzyme contains high mannose type oligosaccharide chains
glycoprotein
-
0.01% carbohydrate covalently bound to the partially purified enzyme
glycoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
catalytic domain, to 1.6 A resolution. Space group P212121
Q5YEX6
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
Q8AAK6
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
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.5
7.5
-
37C, 2 h, stable
2.8
9
Polyporus sulfureus
-
25C, 1 h, stable
3.5
6
-
stable
3.5
-
-
rapid loss of activity
4
6
-
high stability at
4.5
7
-
stable
4.5
-
-
stable to extended incubation at 45C
4.5
-
-
55C, 5 min, 40% loss of activity, at pH-values lower than pH 4.5, 80% loss of activity
4.5
-
-
most stable at
5
5.5
-
37C, 1 h, stable
5
7
-
55C, 5 min, pH 5-7, 10-20% loss of activity
5
8
-
40C, 30 min, stable up to
5.9
-
-
exhibits highest pH stability at pH 5.9 after 5 h incubation at 50C
6
10
-
unstable below pH 6.0 and above pH 10.0
6.5
8
-
40C, 30 min, stable. Unstable below pH 6.5 and above pH 8.0
6.5
9
-
pH 6.5: about 35% of maximal activity, pH 9.0: about 40% of maximal activity
7
-
-
unstable above pH 7
7.5
9
-
20C, 60 min, stable
10
-
-
4C, 1 h, little loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
stable up to
37
-
-
1 h, 50% inactivation
37
-
-
60 min, beta-mannanase I and II, stable
37
-
-
1 h, stable
37
-
-
half-life: 27 h
40
-
-
stable up to
40
-
-
15 min, stable up to
40
-
-
1 h, stable
45
-
-
1 h, complete inactivation
45
-
-
stable to extended incubation at pH 4.5
45
-
-
15 min, pH 5.5, stable up to
50
-
-
rapid loss of activity above
50
-
-
2 h, more than 70% loss of activity
50
-
-
5 min, about 65% loss of activity
50
-
-
24 h, 30% loss of activity
50
-
-
pH 4.5, half-life: 710 min
55
-
-
2 h, stable
55
-
-
2 min, about 65% loss of activity
55
-
-
5 min, pH 5-7, 10-20% loss of activity
55
-
-
unstable at
60
-
-
complete inactivation of beta-mannanase I after 60 min, complete inactivation of beta-mannanase II after 40 min
60
-
-
pH 5, 30 min, relatively stable below
65
-
-
1 h, 30-40% loss of activity
65
-
-
1 h, pH 4.5, about 50% loss of activity
76
-
-
half-life of 10 min at 76C
85
-
-
half-life: 18 h
90
-
-
half-life: 42 min
98
-
-
half-life: 2 min
101
-
O58237, -
melting temperature is 100.7C
102
-
O58237, -
half-life: 27 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
LITERATURE
tends to be inactived by oxygen, dithiothreitol reactivates
-
136038
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable
-
-10C, lyophilized enzyme, stable for over a year
-
4C, in aqueous solution, stable for several months
-
-80C, pH 5.0, chromatofocusing elution buffer, loss of activity within 1 month
-
-20C, freeze-dried enzyme, stable
-
-20C, stable for 2 or 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
TALON immobilized metal ion affinity chromatography, Q12 column chromatography, and S200 gel filtration
-
partial
-
recombinant
-
partial
-
recombinant enzyme
A7LFP5
two forms of enzyme: beta-mannosidase A and B
-
Q-Sepharose column chromatography, SP-Sepharose column chromatography, and chromatofocusing on Polybuffer Exchanger PBE-94
-
-
Polyporus sulfureus
-
Mono S HR 5/5 column chromatography and Superdex 200 gel filtration
-
beta-mannanase I and II
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Aspergillus aculeatus strain PyrG
-
expression in Escherichia coli
-
expression of catalytic domain in Escherichia coli
Q5YEX6
expressed in Escherichia coli strain BL21
-
the gene encoding beta-mannosidase is localized to human chromosome 4
-
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
-
expression in Escherichia coli
-
-
A7LFP5
expression in HEK-293T cell
-
expression in Escherichia coli
-
expression in Escherichia coli
O58237, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
N461A
-
low activity
N461A
Q8AAK6
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand
Q646A
-
low activity
Q646A
Q8AAK6
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand
W198A
-
low activity
W198G
Q8AAK6
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
Q8AAK6
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand
W395A
-
low activity
W645A
-
low activity
W645A
Q8AAK6
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand
Y537A
-
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
O58237, -
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
O58237, -
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
O58237, -
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
Pyrococcus horikoshii DSM 12428
-
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
Pyrococcus horikoshii DSM 12428
-
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
Pyrococcus horikoshii DSM 12428
-
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
-
Y537A
Q8AAK6
crystallization data. Involved either in hydrogen bonding to the ligands or in the maintenance of the hydrophilic sheath around the ligand
additional information
Q95327
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 ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
the enzyme together with alpha-galactosidase and endo-beta-D-mannanase, can be used to characterize the structures of more complex oligosacharides
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
analysis
-
comparison of glycolytic and chitinolytic enzyme activities between desert and oasis flies of Phlebotomus papatasi to evaluate potential differences in susceptibility to infection with Leishmania major
analysis
-
application in carbohydrate research