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Information on EC 3.2.1.24 - alpha-mannosidase and Organism(s) Mus musculus and UniProt Accession O09159
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EC Tree
3.2.1.24 alpha-mannosidaseIUBMB Comments
Also hydrolyses alpha-D-lyxosides and heptopyranosides with the same configuration at C-2, C-3 and C-4 as mannose.
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Word Map
- 3.2.1.24
- oligosaccharide
- mannose
- glycosidases
-
n-linked
- swainsonine
- hydrolases
- mannans
- n-glycans
-
concanavalin
- alpha-fucosidase
- xylanase
- beta-n-acetylglucosaminidase
- beta-d-galactosidase
- beta-hexosaminidase
- cellulase
-
endo-beta-n-acetylglucosaminidase
-
high-mannose
- beta-d-glucosidase
- galactomannans
- 1-deoxymannojirimycin
-
asparagine-linked
-
jack
- beta-mannosidase
-
exoglycosidase
-
mannosylated
- man9glcnac2
- n-acetyl-beta-glucosaminidase
-
locust
- beta-d-glucuronidase
-
complex-type
- glucomannans
-
konjac
-
mannose-type
-
hemicellulases
- glc3man9glcnac2
- castanospermine
-
oligomannosides
- alpha-d-galactosidase
- alpha-d-glucosidase
-
mannose-rich
- beta-xylosidase
-
lipid-linked
- hexosaminidase
- beta-n-acetylhexosaminidase
-
mannose-containing
-
hybrid-type
- i-cell
- mucolipidosis
-
oligomannose
- analysis
- cellulosome
- diagnostics
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
alpha-mannosidase, mannanase, alpha-d-mannosidase, lysosomal alpha-mannosidase, alpha-mannosidase ii, golgi alpha-mannosidase ii, alpha1,2-mannosidase, alpha-1,2-mannosidase, alpha-man, man2c1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,2-alpha-D-mannosidase
-
-
-
-
1,2-alpha-mannosidase
-
-
-
-
Alpha mannosidase 6A8B
-
-
-
-
alpha-D-mannopyranosidase
-
-
-
-
alpha-D-mannosidase
-
-
-
-
Alpha-D-mannoside mannohydrolase
-
-
-
-
AMAN
-
-
-
-
exo-alpha-mannosidase
-
-
-
-
Laman
-
-
-
-
Lysosomal acid alpha-mannosidase
-
-
-
-
p-nitrophenyl-alpha-mannosidase
-
-
-
-
additional information
-
the enzyme belongs to the class 1 alpha1,2-mannosidases of glycosylhydrolase family 47
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides
active site structure and catalytic residues, e.g. Asn515 involved in substrate binding, reaction mechanism and processing steps, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-mannoside mannohydrolase
Also hydrolyses alpha-D-lyxosides and heptopyranosides with the same configuration at C-2, C-3 and C-4 as mannose.
CAS REGISTRY NUMBER
COMMENTARY
9025-42-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl-alpha-D-mannopyranoside + H2O
4-methylumbelliferone + alpha-D-mannopyranose
-
-
?
6 pyridylamino-Man9GlcNAc2 + H2O
pyridylamino-Man8GlcNAc2 + pyridylamino-Man7GlcNAc2 + pyridylamino-Man6GlcNAc2 + pyridylamino-Man5GlcNAc2 + pyridylamino-Man4GlcNAc2 + pyridylamino-Man3GlcNAc2 + 21 alpha-D-mannopyranose
stepwise cleavage to Man2GlcNAc structures
-
?
alpha-D-mannosidosis fibroblasts + H2O
Manbeta(1-4)GlcNAc + ?
-
-
?
p-nitrophenyl-alpha-D-mannopyranoside + H2O
p-nitrophenol + alpha-D-mannopyranose
-
-
?
pyridylamino-Man5GlcNAc + H2O
pyridylamino-Man4GlcNAc + pyridylamino-Man3-2GlcNAc + alpha-D-mannose
-
lesser degree of pyridylamino-Man3-2GlcNAc, stepwise cleavage to Man2GlcNAc structures
?
Man6GlcNAc2 + H2O
Man5GlcNAc2 + mannose
-
slow reaction of the Golgi alpha-mannosidase in vitro
-
-
?
Man9GlcNAc2 + 3 H2O
Man6GlcNAc2 + 3 mannose
-
fast reaction of the Golgi alpha-mannosidase in vitro
-
-
?
Man9GlcNAc2 + H2O
Man5GlcNAc2 + Man6GlcNAc2 + Man7GlcNAc2 + Man8GlcNAc2 + alpha-D-mannopyranose
-
-
major product: Man5GlcNAc2, involved in Asn-linked oligosaccharide maturation
?
additional information
?
-
-
class 1 alpha1,2-mannosidases of glycosylhydrolase family 47 play critical roles in the maturation of Asn-linked glycoproteins in the endoplasmic reticulum and Golgi complex as well as in the recognition and timing of disposal of terminally unfolded proteins by ER-associated degradation, overview
-
-
?
Man8GlcNAc2 + 3 H2O
Man5GlcNAc2 + 3 D-mannose
-
Golgi alpha-mannosidase in vivo
-
-
?
Man8GlcNAc2 + 3 H2O
Man5GlcNAc2 + 3 D-mannose
-
slow reaction of the endoplasmic reticulum alpha-mannosidase in vitro
-
-
?
Man9GlcNAc2 + H2O
Man8GlcNAc2 + mannose
-
endoplasmic reticulum alpha-mannosidase in vivo
-
-
?
Man9GlcNAc2 + H2O
Man8GlcNAc2 + mannose
-
fast reaction of the endoplasmic reticulum alpha-mannosidase in vitro
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-D-mannosidosis fibroblasts + H2O
Manbeta(1-4)GlcNAc + ?
-
-
?
Man8GlcNAc2 + 3 H2O
Man5GlcNAc2 + 3 D-mannose
-
Golgi alpha-mannosidase in vivo
-
-
?
Man9GlcNAc2 + H2O
Man5GlcNAc2 + Man6GlcNAc2 + Man7GlcNAc2 + Man8GlcNAc2 + alpha-D-mannopyranose
-
-
major product: Man5GlcNAc2, involved in Asn-linked oligosaccharide maturation
?
Man9GlcNAc2 + H2O
Man8GlcNAc2 + mannose
-
endoplasmic reticulum alpha-mannosidase in vivo
-
-
?
additional information
?
-
-
class 1 alpha1,2-mannosidases of glycosylhydrolase family 47 play critical roles in the maturation of Asn-linked glycoproteins in the endoplasmic reticulum and Golgi complex as well as in the recognition and timing of disposal of terminally unfolded proteins by ER-associated degradation, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
is critical in coordination of the enzyme's (alphaalpha)7 barrel structure, located at the base of the barrel
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-deoxymannojirimycin
-
pretreatment with 1-deoxymannojirimycin protectes primary cultured mouse cortical neurons from Amyloid beta1-42 toxicity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MA2B1_MOUSE
1013
0
114648
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
structure analysis, the enzyme has an (alphaalpha)7 barrel structure with a coordinating Ca2+ ion, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
30 mg/ml purified recombinant Golgi alpha-mannosidase IA in 20 mM MES, pH 6.5, 150 mM NaCl, 5 mM CaCl2, and 0.75 M NDSB-201, crystallization of free enzyme by microbatch method using a precipitation solution containing 15-20% PEG 4000 at pH 4.5-6.5, cocrystallization of 1-deoxymannojirimycin bound to the enzyme by hanging drop vapour diffusion method at 37°C, 0.001 ml of a solution containing 200 mM 1-deoxymannojirimycin is mixed with an equal volume of crystallization solution containing 100 mM MES and 100 mM Tris-HCl, pH 6.0, and 25-35% PEG 4000, 2 days at 18°C, X-ray diffraction structure determination and analysis at 1.5 A resolution, structure modelling
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant yeast alpha-factor signal sequence-fusion enzyme from Pichia pastoris strain GS115 by ion exchange and hydrophobic interaction chromatography, eluent is ammonium sulfate, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of Golgi alpha-mannosidase IA in fusion with the yeast alpha-factor signal sequence in Pichia pastoris strain GS115
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
inhibition of N-glycan processing in the endoplasmic reticulum attenuates endoplasmic reticulum stressinduced cell death by increasing high-mannose type oligosaccharides that reduce protein aggregation, such as amyloidogenesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vallee, F.; Lal, A.; Moremen, K.W.; Howell, P.L.
Purification, crystallization and preliminary X-ray crystallographic analysis of recombinant murine Golgi mannosidase IA, a class I alpha-mannosidase involved in Asn-linked oligosaccharide maturation
Acta Crystallogr. Sect. D
55
571-573
1999
Mus musculus
Beccari, T.; Appolloni, M.G.; Costanzi, E.; Stinchi, S.; Stirling, J.L.; Della Fazia, M.A.; Servillo, G.; Viola, M.P.; Orlacchio, A.
Lysosomal alpha-mannosidases of mouse tissues: characteristics of the isoenzymes, and cloning and expression of a full-length cDNA
Biochem. J.
327
45-49
1997
Mus musculus (O09159), Mus musculus
Merkle, R.K.; Zhang, Y.; Ruest, P.J.; Lal, A.; Liao, Y.F.; Moremen, K.W.
Cloning, expression, purification, and characterization of the murine lysosomal acid alpha-mannosidase
Biochim. Biophys. Acta
1336
132-146
1997
Mus musculus (O09159), Mus musculus
Schneikert, J.; Herscovics, A.
Characterization of a novel mouse recombinant processing alpha-mannosidase
Glycobiology
4
445-450
1994
Mus musculus
Tempel, W.; Karaveg, K.; Liu, Z.J.; Rose, J.; Wang, B.C.; Moremen, K.W.
Structure of mouse Golgi alpha-mannosidase IA reveals the molecular basis for substrate specificity among class 1 (family 47 glycosylhydrolase) alpha1,2-mannosidases
J. Biol. Chem.
279
29774-29786
2004
Mus musculus
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