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Information on EC 3.2.1.25 - beta-mannosidase and Organism(s) Homo sapiens

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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
beta-mannosidase, beta-d-mannosidase, beta-man, man2a, mannase, hvbii, cmman5a, beta-d-mannoside mannohydrolase, beta-mannoside mannohydrolase, beta-mannosidase 2a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-D-mannosidase
-
-
-
-
beta-mannosidase
-
-
-
-
beta-mannoside mannohydrolase
-
-
-
-
exo-beta-D-mannanase
-
-
-
-
mannanase
-
-
-
-
mannase
-
-
-
-
mannosidase, beta-
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
beta-D-mannoside mannohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-43-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-acetamido-2-deoxymannopyranose + H2O
?
show the reaction diagram
-
-
-
-
?
2-amino-2-deoxymannopyranose + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl beta-D-mannoside + H2O
4-methylumbelliferone + beta-D-mannose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + D-mannopyranose
show the reaction diagram
-
-
-
?
alpha-D-mannopyranose 1-phosphate + H2O
alpha-D-mannose + phosphate
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
mannopyranosylamine + H2O
?
show the reaction diagram
-
-
-
-
?
methyl alpha-D-mannopyranoside + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-mannoside + H2O
p-nitrophenol + alpha-D-mannose
show the reaction diagram
-
p-nitrophenyl-beta-D-mannopyranoside
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
1.5 mM, no residual activity
Co2+
1.5 mM, 80% residual activity
Cu2+
1.5 mM, no residual activity
D-mannosamine
-
-
dimethyl sulfoxide
5 mM, no residual activity
dimethylformamide
5 mM, no residual activity
ethanol
5 mM, no residual activity
iodoacetate
5 mM, no residual activity
Pb2+
1.5 mM, 78% residual activity
Sodium dodecyl sulfate
5 mM, no residual activity
Zn2+
1.5 mM, no residual activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13 - 0.56
4-methylumbelliferyl beta-D-mannopyranoside
2.5 - 3
4-nitrophenyl-beta-D-mannopyranoside
pH 5.0, 37°C
2.2
p-nitrophenyl-beta-D-mannopyranoside
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.996
-
-
1.772
-
-
17.6
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
3.7 - 4.6
-
about 95% of maximal activity at pH 3.7 and pH 4.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
from patients with rheumatoid arthritis and patients with pigmented villous nodular synovitis
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MANBA_HUMAN
879
0
100895
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A2R8YEC9_HUMAN
925
0
106051
TrEMBL
Secretory Pathway (Reliability: 1)
B4DT18_HUMAN
822
0
94398
TrEMBL
Secretory Pathway (Reliability: 1)
A7LFP5_HUMAN
879
0
100873
TrEMBL
Secretory Pathway (Reliability: 1)
Q59EG5_HUMAN
457
0
52941
TrEMBL
Secretory Pathway (Reliability: 4)
E9PFW2_HUMAN
822
0
94412
TrEMBL
Secretory Pathway (Reliability: 1)
A8K6D3_HUMAN
879
0
100937
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
-
gel filtration
135000
-
beta-mannosidase A, enzyme from urine, nondenaturing gradient PAGE
137000
-
beta-mannosidase A, enzyme from kidney, gradient gel electrophoresis
155000
-
beta-mannosidase B, enzyme from kidney, gradient gel electrophoresis
160000
-
beta-mannosidase B, enzyme from urine, nondenaturing gradient PAGE
37000
-
1 * 37000 + 1 * 49000 + 1 * 75000, beta-mannosidase A, SDS-PAGE
49000
75000
79000
-
gel filtration
97000
x * 97000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 97000, SDS-PAGE
trimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
enzyme contains high mannose type oligosaccharide chains
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
-
20°C, 60 min, stable
136027
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
1 h, stable
45
-
1 h, complete inactivation
50
-
5 min, about 65% loss of activity
55
-
2 min, about 65% loss of activity
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
-
recombinant enzyme
two forms of enzyme: beta-mannosidase A and B
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in HEK-293T cell
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Iwasaki, Y.; Tsuji, A.; Omura, K.; Suzuki, Y.
Purification and characterization of beta-mannosidase from human placenta
J. Biochem.
106
331-335
1989
Homo sapiens
Manually annotated by BRENDA team
Noeske, C.; Mersmann, G.
beta-D-Mannosidase from human placenta: properties and partial purification
Hoppe-Seyler's Z. Physiol. Chem.
364
1645-1651
1983
Homo sapiens
Manually annotated by BRENDA team
Bartholomew, B.A.; Perry, A.L.
The properties of synovial fluid beta-mannosidase activity
Biochim. Biophys. Acta
315
123-127
1973
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Guadalupi, R.; Bernard, M.; Orlacchio, A.; Foglietti, M.J.; Emiliani, C.
Purification and properties of human urinary beta-D-mannosidase
Biochim. Biophys. Acta
1293
9-16
1996
Homo sapiens
Manually annotated by BRENDA team
Samra, Z.Q.; Athar, M.A.
Cloning, sequence, expression and characterization of human beta-mannosidase
Acta Biochim. Pol.
55
479-490
2008
Homo sapiens (A7LFP5), Homo sapiens
Manually annotated by BRENDA team
Sabourdy, F.; Labauge, P.; Stensland, H.; Nieto, M.; Garcés, V.; Renard, D.; Castelnovo, G.; de Champfleur, N.; Levade, T.
A MANBA mutation resulting in residual beta-mannosidase activity associated with severe leukoencephalopathy: A possible pseudodeficiency variant
BMC Med. Genet.
10
84
2009
Homo sapiens
Manually annotated by BRENDA team