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Information on EC 3.2.1.45 - glucosylceramidase and Organism(s) Mus musculus and UniProt Accession Q69ZF3

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EC Tree
IUBMB Comments
Also acts on glucosylsphingosine (cf. EC 3.2.1.62 glycosylceramidase).
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This record set is specific for:
Mus musculus
UNIPROT: Q69ZF3
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
glucocerebrosidase, imiglucerase, acid beta-glucosidase, beta-glucocerebrosidase, glucosylceramidase, alglucerase, velaglucerase alfa, taliglucerase alfa, cerezyme, glccerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nonlysosomal beta-glucosidase
-
nonlysosomal glucosylceramidase
-
acid beta-glucosidase
Alglucerase
-
-
-
-
beta-D-glucocerebrosidase
-
-
-
-
beta-glucocerebrosidase
-
-
-
-
beta-glucosidase 2
-
-
beta-glucosylceramidase
-
-
-
-
ceramidase, glucosyl-
-
-
-
-
ceramide glucosidase
-
-
-
-
cerebroside beta-glucosidase
-
-
-
-
D-glucosyl-N-acylsphingosine glucohydrolase
-
-
-
-
GBA2
-
-
Gcase
-
-
glcCer-beta-glucosidase
-
-
-
-
glucocerebrosidase
-
-
-
-
glucocerebroside beta-glucosidase
-
-
-
-
glucose cerebrosidase
-
-
-
-
glucosphingosine glucosylhydrolase
-
-
-
-
glucosylceramide beta-glucosidase
-
-
-
-
glucosylcerebrosidase
-
-
-
-
glucosylsphingosine beta-D-glucosidase
-
-
-
-
glucosylsphingosine beta-glucosidase
-
-
-
-
Imiglucerase
-
-
-
-
microsomal bile acid beta-glucosidase
-
-
non-lysosomal glucosylceramidase
-
-
psychosine hydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
D-glucosyl-N-acylsphingosine glucohydrolase
Also acts on glucosylsphingosine (cf. EC 3.2.1.62 glycosylceramidase).
CAS REGISTRY NUMBER
COMMENTARY hide
37228-64-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucopyranose
show the reaction diagram
-
-
-
?
D-glucosylceramide + H2O
D-glucose + ceramide
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
methylumbelliferone + glucose
show the reaction diagram
-
-
-
-
?
glucocerebroside + H2O
glucose + ceramide
show the reaction diagram
-
-
-
-
?
glucosylceramide + H2O
beta-D-glucose + ceramide
show the reaction diagram
-
-
-
-
?
N-stearoylglucosyl ceramide + H2O
D-glucose + stearoylceramide
show the reaction diagram
-
-
-
-
?
nonylumbelliferyl-beta-D-glucopyranoside + H2O
nonylumbelliferone + glucose
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glucosylceramide + H2O
D-glucose + ceramide
show the reaction diagram
-
-
-
?
glucocerebroside + H2O
glucose + ceramide
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-(5-adamantane-1-yl-methoxypentyl)-deoxynojirimycin
-
N-butyldeoxynojirimycin
-
6-bromo-6-deoxy-conduritol
-
-
6-bromo-conduritol-beta-epoxide
-
-
conduritol B epoxide
-
-
cyclophellitol
-
oral application induces Gaucher like disease
N-carboxynonyldeoxynojirimycin
-
-
N-dodecyldeoxynojirimycin
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heat-stable factor
-
-
-
phosphatidylserine
-
-
saposin C
-
optimal in vitro enzyme activity requires saposin C. Reduced saposin levels increase the instability of V394L or D409H GCases, the decreases leads to large accumulations of glucosylceramide in all tissues
-
sodium taurocholate
Triton X-100
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.636 - 0.93
4-methylumbelliferyl-beta-D-glucopyranoside
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00014
N-carboxy-nonyldeoxynojirimycin
Mus musculus
-
-
0.0229
N-dodecyl-deoxynojirimycin
Mus musculus
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 5.8
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
highest activity in stratum corneum
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
some enzyme-knockout mice display a strong locomotor defect, others displayed only mild alterations of the gait pattern and no signs of cerebellar defects. Enzyme knockout results in a severe sperm morphological defect called globozoospermia. Loss of GBA2 enzyme activity diminishes neurite outgrowth
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GBA2_MOUSE
918
0
103294
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57000
-
2 * 57000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 57000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D585H
the mutation causes 99% decrease of activity and is associated with autosomal-recessive cerebellar ataxia
F410V
the mutation causes 98% decrease of activity and is associated with hereditary spastic paraplegia
G674R
the mutation causes 99% decrease of activity and is associated with hereditary spastic paraplegia
M501V
the mutation is associated with Marinesco-Sjoegren-like syndrome
R621W
the mutation causes 99% decrease of activity and is associated with hereditary spastic paraplegia
R725H
the mutation causes 70% decrease of activity is associated with autosomal-recessive cerebellar ataxia
R864H
the mutation causes 99% decrease of activity and is associated with autosomal-recessive cerebellar ataxia
D409H
-
homozygous, mice expressing low levels of prosaposin and saposins are backcrossed into mice with the point mutation D409H. In contrast to the mice with low levels of prosaposin and saposins the mutant mice with low levels of prosaposin and saposins display large numbers of engorged macrophages and nearly exclusive glucosylceramide accumulation in the liver, lung, spleen, thymus and brain
V394L
-
homozygous, mice expressing low levels of prosaposin and saposins are backcrossed into mice with the point mutation V394L. In contrast to the mice with low levels of prosaposin and saposins the mutant mice with low levels of prosaposin and saposins display large numbers of engorged macrophages and nearly exclusive glucosylceramide accumulation in the liver, lung, spleen, thymus and brain
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing destroys activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anti-FLAG magnetic bead chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in CHO cells
expression in NIH 3T3 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Imai, K.
Characterization of beta-glucosidase as a peripheral enzyme of lysosomal membranes from mouse liver and purification
J. Biochem.
98
1405-1416
1985
Mus musculus
Manually annotated by BRENDA team
Schliemann, W.; Schliemann, B.
beta-D-Glucosidasen (EC 3.2.1.21) und glucosylceramidasen (EC 3.2.1.45) des Menschen
Pharmazie
4
243-250
1982
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Daniels, L.B.; Glew, R.H.
beta-D-Glucosidases in tissue
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
4
217-226
1984
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
-
Manually annotated by BRENDA team
Legler, G.
beta-Glucocerebrosidase: mechanistic studies with covalent and non-covalent inhibitors
NATO ASI Ser. A, Life Sci.
150
63-72
1988
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
-
Manually annotated by BRENDA team
Atsumi, S.; Nosaka, C.; Iinuma, H.; Umezawa, K.
Inhibition of glucocerebrosidase and induction of neural abnormality by cyclophellitol in mice
Arch. Biochem. Biophys.
297
362-367
1992
Mus musculus
Manually annotated by BRENDA team
Holleran, W.M.; Takagi, Y.; Imokawa, G.; Jackson, S.; Lee, J.M.; Elias, P.M.
beta-Glucocerebrosidase activity in murine epidermis: characterization and localization in relation to differentiation
J. Lipid Res.
33
1201-1209
1992
Mus musculus
Manually annotated by BRENDA team
Carstea, E.D.; Murray, G.J.; O'Neill, R.R.
Molecular and functional characterization of the murine glucocerebrosidase gene
Biochem. Biophys. Res. Commun.
184
1477-1483
1992
Mus musculus (P17439), Mus musculus
Manually annotated by BRENDA team
Watt Chan, K.; Waire, J.; Simons, B.; Karey, K.; Fung, J.; Copelans, D.; Andrews, L.
Measurement of lysosomal glucocerebrosidase activity in mouse liver using a fluorescence-activated cell sorter assay
Anal. Biochem.
334
227-233
2004
Mus musculus
Manually annotated by BRENDA team
Sun, Y.; Quinn, B.; Witte, D.P.; Grabowski, G.A.
Gaucher disease mouse models: point mutations at the acid beta-glucosidase locus combined with low-level prosaposin expression lead to disease variants
J. Lipid Res.
46
2102-2113
2005
Mus musculus
Manually annotated by BRENDA team
Walden, C.M.; Sandhoff, R.; Chuang, C.C.; Yildiz, Y.; Butters, T.D.; Dwek, R.A.; Platt, F.M.; van der Spoel, A.C.
Accumulation of glucosylceramide in murine testis, caused by inhibition of beta-glucosidase 2: implications for spermatogenesis
J. Biol. Chem.
282
32655-32664
2007
Mus musculus
Manually annotated by BRENDA team
Woeste, M.A.; Stern, S.; Raju, D.N.; Grahn, E.; Dittmann, D.; Gutbrod, K.; Doermann, P.; Hansen, J.N.; Schonauer, S.; Marx, C.E.; Hamzeh, H.; Koerschen, H.G.; Aerts, J.M.F.G.; Boenigk, W.; Endepols, H.; Sandhoff, R.; Geyer, M.; Berger, T.K.; Bradke, F.; Wachten, D.
Species-specific differences in nonlysosomal glucosylceramidase GBA2 function underlie locomotor dysfunction arising from loss-of-function mutations
J. Biol. Chem.
294
3853-3871
2019
Mus musculus (Q69ZF3), Mus musculus
Manually annotated by BRENDA team