Information on EC 3.2.1.45 - glucosylceramidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.2.1.45
-
RECOMMENDED NAME
GeneOntology No.
glucosylceramidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a D-glucosyl-N-acylsphingosine + H2O = D-glucose + a ceramide
show the reaction diagram
-
-
-
-
a D-glucosyl-N-acylsphingosine + H2O = D-glucose + a ceramide
show the reaction diagram
the enzyme hydrolyses the beta-glucosidic linkage of glucosylceramide with retention of anomeric conformation via a two-step, double-displacement mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Other glycan degradation
-
Sphingolipid metabolism
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
D-glucosyl-N-acylsphingosine glucohydrolase
Also acts on glucosylsphingosine (cf. EC 3.2.1.62 glycosylceramidase).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acid beta-glucocerebrosidase
-
-
acid beta-glucosidase
-
-
-
-
acid beta-glucosidase
-
-
acid beta-glucosidase
-
-
acid beta-glycosidase
-
-
acid-beta-glucocerebrosidase
-
-
acid-beta-glucosidase
-
-
Alglucerase
-
-
-
-
beta-D-glucocerebrosidase
-
-
-
-
beta-GC
-
-
beta-glucocerebrosidase
-
-
-
-
beta-glucosidase
-
-
beta-glucosidase 2
-
-
beta-glucosidase 2
-
-
beta-glucosylceramidase
-
-
-
-
beta-glycosylceramidase
-
-
bile acid beta-glucosidase
-
-
bile acid beta-glucosidase
-
similar enzyme
ceramidase, glucosyl-
-
-
-
-
ceramide glucosidase
-
-
-
-
cerebroside beta-glucosidase
-
-
-
-
Ceredase
-
-
Ceredase
-
commercial preparation
Cerezyme
-
commercial preparation
Cerezyme
-
recombinant enzyme
D-glucosyl-N-acylsphingosine glucohydrolase
-
-
-
-
GBA
-
gene name
GBA
-
lysosomal glucocerebrosidase
GBA
P04062
-
GBA2
-
-
GBA2
-
non-lysosomal glucoceramidase
GBA2
Q9HCG7
-
GBA2
-
-
Gcase
-
-
gene-activated human GlcCerase
-
commercial preparation
Glc-Cerase
-
-
glcCer-beta-glucosidase
-
-
-
-
glucocerebrosidase
-
-
-
-
glucocerebrosidase
-
-
glucocerebrosidase
P04062
-
glucocerebroside beta-glucosidase
-
-
-
-
glucose cerebrosidase
-
-
-
-
glucosphingosine glucosylhydrolase
-
-
-
-
glucosylceramide beta-glucosidase
-
-
-
-
glucosylceramide beta-glucosidase
-
-
glucosylcerebrosidase
-
-
-
-
glucosylsphingosine beta-D-glucosidase
-
-
-
-
glucosylsphingosine beta-glucosidase
-
-
-
-
glycosylceramidase
-
-
glycosylceramide-beta-glucosidase
-
-
Imiglucerase
-
-
-
-
Imiglucerase
-
a recombinant formulation of human glucocerebrosidase
Klotho-related protein
-
-
KLrP
-
-
microsomal bile acid beta-glucosidase
-
-
N-acylsphingosyl-1-O-beta-D-glucoside:glucohydrolase
-
-
neutral beta-glycosylceramidase
-
-
NLGase
-
-
non-lysosomal glucosylceramidase
-
-
non-lysosomal glucosylceramidase
-
-
psychosine hydrolase
-
-
-
-
velaglucerase alfa
-
commercial preparation
CAS REGISTRY NUMBER
COMMENTARY
37228-64-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
methods of enzyme determination
-
-
Manually annotated by BRENDA team
children with chronic neuronopathic Gaucher disease
-
-
Manually annotated by BRENDA team
Gaucher disease-associated glucocerebroside variants N370S and G202R
-
-
Manually annotated by BRENDA team
Gaucher patients
-
-
Manually annotated by BRENDA team
methods of enzyme determination; overview
-
-
Manually annotated by BRENDA team
normal and Gaucher disease enzyme
-
-
Manually annotated by BRENDA team
normal and Gaucher disease enzyme
UniProt
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
patients with Gaucher disease
-
-
Manually annotated by BRENDA team
patients with Parkinson's disease and patients with demetia with Lewis bodies
-
-
Manually annotated by BRENDA team
patients with Psoriasis vulgaris
-
-
Manually annotated by BRENDA team
Turkish patients with Gaucher disease
-
-
Manually annotated by BRENDA team
methods of enzyme determination
-
-
Manually annotated by BRENDA team
methods of enzyme determination
-
-
Manually annotated by BRENDA team
methods of enzyme determination
-
-
Manually annotated by BRENDA team
putative lysosomal glucocerebrosidase precursor
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
Gaucher disease is caused by the dysfunction of glucocerebrosidase
malfunction
-
Gaucher disease is a progressive lysosomal storage disorder caused by the deficiency of glucocerebrosidase leading to the dysfunction in multiple organ systems
malfunction
-
mutations in the gene encoding for acid beta-glucosidase result in Gaucher disease
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(6-[N-(7-nitrobenz-2-oxa-1,3 diazol-4-yl)amino]hexanoyl)-beta-D-glucosylceramide + H2O
(6-[N-(7-nitrobenz-2-oxa-1,3 diazol-4-yl)amino]hexanoyl)sphingosine + D-glucose
show the reaction diagram
-
-
-
-
?
12(N-methyl-N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl))aminododecanoyl-2-N-sphingosyl 1-O-beta-D-glucoside + H2O
D-glucose + 12(N-methyl-N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl))aminododecanoyl-2-N-sphingosine
show the reaction diagram
-
-
-
-
?
12(N-methyl-N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl))aminododecanoyl-2-N-sphingosyl 1-O-beta-D-glucoside + H2O
D-glucose + 12(N-methyl-N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl))aminododecanoyl-2-N-sphingosine
show the reaction diagram
P04062
-
-
-
?
2,4-dinitrophenyl beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
-
?
3-O-benzoyl-N-stearylglucosphingosine + H2O
D-glucose + 3-O-benzoyl-N-stearylsphingosine
show the reaction diagram
-
not: galactocerebroside
-
-
?
4-methylumbelliferyl glucoside + H2O
4-methylumbelliferone + D-glucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-galactopyranoside + H2O
methylumbelliferone + beta-D-galactose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
methylumbelliferone + glucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
methylumbelliferone + glucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
methylumbelliferone + glucose
show the reaction diagram
P04062
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
methylumbelliferone + glucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
methylumbelliferone + glucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
methylumbelliferone + glucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
methylumbelliferone + glucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucose
show the reaction diagram
P04062
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
4-methylumbelliferone + beta-D-glucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucopyranoside + H2O
methylumbelliferone + beta-D-glucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
show the reaction diagram
-
-
-
-
?
6(N-methyl-N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl))aminohexyl-2-N-sphingosyl 1-O-beta-D-glucoside + H2O
D-glucose + 6(N-methyl-N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl))aminohexyl-2-N-sphingosine
show the reaction diagram
-
NBD-glucocerebroside
-
-
?
6(N-methyl-N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl))aminohexyl-2-N-sphingosyl 1-O-beta-D-glucoside + H2O
D-glucose + 6(N-methyl-N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl))aminohexyl-2-N-sphingosine
show the reaction diagram
-
complexed with bovine serum albumin
-
-
?
6-[N-(7-nitrobenz-2-oxa-1,3 diazol-4-yl)amino]hexanoyl)-beta-D-galactosylceramide + H2O
6-[N-(7-nitrobenz-2-oxa-1,3 diazol-4-yl)amino]hexanoyl)ceramide + D-galactose
show the reaction diagram
-
-
-
-
?
6-[N-methyl-N-(7-nitrobenz-2-oxa-1,3 diazol-4-yl)aminododecanoyl]sphingosyl-beta-D-glucoside + H2O
?
show the reaction diagram
-
-
-
-
?
C18-galactosylceramide + H2O
?
show the reaction diagram
-
-
-
-
?
C18-glucosylceramide + H2O
?
show the reaction diagram
-
-
-
-
?
D-glucocerebroside + H2O
D-glucose + ceramide
show the reaction diagram
-
-
-
-
?
D-glucosyl-beta-(1-1')-N-dodecanoyl-D-erythro-sphingosine + H2O
D-glucose + N-dodecanoyl-D-erythro-sphingosine
show the reaction diagram
-
product and internal standard are quantified using tandem mass spectrometry
-
-
?
D-glucosyl-N-butylsphingosine + H2O
D-glucose + N-butylsphingosine
show the reaction diagram
-
-
-
-
?
D-glucosyl-N-ethylsphingosine + H2O
D-glucose + N-ethylsphingosine
show the reaction diagram
-
-
-
-
?
D-glucosyl-N-methylsphingosine + H2O
D-glucose + N-methylsphingosine
show the reaction diagram
-
-
-
-
?
D-glucosyl-N-octylsphingosine + H2O
D-glucose + N-octylsphingosine
show the reaction diagram
-
-
-
-
?
D-glucosyl-N-propylsphingosine + H2O
D-glucose + N-propylsphingosine
show the reaction diagram
-
-
-
-
?
glucocerebroside + H2O
glucose + ceramide
show the reaction diagram
-
-
-
-
?
glucocerebroside + H2O
glucose + ceramide
show the reaction diagram
P04062
-
-
-
?
glucocerebroside + H2O
glucose + ceramide
show the reaction diagram
-
-
-
-
?
glucocerebroside + H2O
glucose + ceramide
show the reaction diagram
-
-
-
-
?
glucocerebroside + H2O
glucose + ceramide
show the reaction diagram
-
-
-
-
?
glucocerebroside + H2O
beta-D-glucose + ceramide
show the reaction diagram
-
-
-
-
?
glucosylceramide + H2O
beta-D-glucose + ceramide
show the reaction diagram
-
-
-
-
?
glucosylceramide + H2O
beta-D-glucose + ceramide
show the reaction diagram
-
-
-
-
?
glucosylceramide + H2O
beta-D-glucose + ceramide
show the reaction diagram
Q9HCG7
-
-
-
?
glucosylceramide + H2O
?
show the reaction diagram
-
-
-
-
?
N-(6-(7-nitrobenzo-2-oxa-1,3-diazol-4-yl)amino)hexanoyl-D-erythro-glucosylsphingosine + H2O
D-glucose + N-(6-(7-nitrobenzo-2-oxa-1,3-diazol-4-yl)amino)hexanoyl-sphingosine
show the reaction diagram
-
-
-
-
?
N-palmitoyl-dihydroglucocerebroside + H2O
D-glucose + N-palmitoyl-dihydrocerebroside
show the reaction diagram
-
-
-
-
?
N-stearoyl-dihydroglucocerebroside + H2O
D-glucose + N-stearoyl-dihydrocerebroside
show the reaction diagram
-
-
-
-
?
N-stearoylglucosyl ceramide + H2O
D-glucose + stearoylceramide
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
-
-
-
-
?
nonylumbelliferyl-beta-D-glucopyranoside + H2O
nonylumbelliferone + glucose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl beta-D-glucopyranoside + H2O
p-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
-
?
palmitylglucosyl ceramide + H2O
D-glucose + palmitylceramide
show the reaction diagram
-
-
-
-
?
undecylumbelliferyl-beta-D-glucopyranoside + H2O
undecylumbelliferone + glucose
show the reaction diagram
-
-
-
-
?
heptylumbelliferyl-beta-D-glucopyranoside + H2O
heptylumbelliferone + glucose
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme catalyses the penultimate step in the breakdown of membrane glycosphingolipids
-
-
-
additional information
?
-
-
not: galactosylceramide, GM1a and sphingomyelin
-
-
-
additional information
?
-
-
point mutations in glucocerebrosidase can cause Gaucher disease, a common lysosomal storage disease
-
-
-
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
glucocerebroside + H2O
glucose + ceramide
show the reaction diagram
-
-
-
-
?
glucocerebroside + H2O
glucose + ceramide
show the reaction diagram
P04062
-
-
-
?
glucocerebroside + H2O
glucose + ceramide
show the reaction diagram
-
-
-
-
?
glucocerebroside + H2O
glucose + ceramide
show the reaction diagram
-
-
-
-
?
glucocerebroside + H2O
glucose + ceramide
show the reaction diagram
-
-
-
-
?
glucosylceramide + H2O
beta-D-glucose + ceramide
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme catalyses the penultimate step in the breakdown of membrane glycosphingolipids
-
-
-
additional information
?
-
-
point mutations in glucocerebrosidase can cause Gaucher disease, a common lysosomal storage disease
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1R,2R,3S,4S,5R,6S)-7-oxabicyclo[4.1.0]heptane-2,3,4,5-tetrol
-
-
(1R,2R,3S,4S,5R,6S)-7-oxabicyclo[4.1.0]heptane-2,3,4,5-tetrol
-
-
(1R,2R,3S,4S,5R,6S)-7-oxabicyclo[4.1.0]heptane-2,3,4,5-tetrol
-
-
(3aR,4S,5R,6R,7S,7aS)-2-(3-phenylpropylimino)-octahydro-1H-benzo[d]imidazole-4,5,6,7-tetraol
-
-
-
(3aR,4S,5R,6R,7S,7aS)-2-(nonylimino)-octahydro-1H-benzo[d]imidazole-4,5,6,7-tetraol
-
-
-
(3aR,4S,5R,6S,7R,7aR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aR,4S,5R,6S,7R,7aR)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aR,4S,5R,6S,7R,7aS)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aR,4S,5R,6S,7R,7aS)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aR,4S,5S,6S,7R,7aR)-4-(benzyloxy)-2-(nonylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
-
-
(3aR,4S,5S,6S,7R,7aR)-4-(benzyloxy)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
-
-
(3aRS,4SR,5RS,6SR,7RS,7aRS)- 2-(hexylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aRS,4SR,5RS,6SR,7RS,7aRS)- 2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aRS,4SR,5RS,6SR,7RS,7aRS)- 2-(octylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aRS,4SR,5RS,6SR,7RS,7aSR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aRS,4SR,5SR,6SR,7RS,7aRS)-4-(benzyloxy)-2-(hexylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
-
-
(3aRS,4SR,5SR,6SR,7RS,7aRS)-4-(benzyloxy)-2-(nonylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
-
-
(3aRS,4SR,5SR,6SR,7RS,7aRS)-4-(benzyloxy)-2-(octylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
-
-
(3aS,4S,5R,6S,7R,7aR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aS,4S,5R,6S,7R,7aR)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aS,4S,5R,6S,7R,7aS)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aS,4S,5R,6S,7R,7aS)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aS,4S,5S,6S,7R,7aS)-4-(benzyloxy)-2-(nonylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
-
-
(3aSR,4SR,5RS,6SR,7RS,7aRS)-2-(hexylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aSR,4SR,5RS,6SR,7RS,7aRS)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aSR,4SR,5RS,6SR,7RS,7aRS)-2-(octylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aSR,4SR,5RS,6SR,7RS,7aSR)-2-(hexylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aSR,4SR,5RS,6SR,7RS,7aSR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aSR,4SR,5RS,6SR,7RS,7aSR)-2-(octylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
-
-
(3aSR,4SR,5SR,6SR,7RS,7aSR)-4-(benzyloxy)-2-(hexylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
-
-
(3aSR,4SR,5SR,6SR,7RS,7aSR)-4-(benzyloxy)-2-(nonylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
-
-
(3aSR,4SR,5SR,6SR,7RS,7aSR)-4-(benzyloxy)-2-(octylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
-
-
1,4-dideoxy-1,4-imino-D-arabinitol
-
-
1,5-dideoxy-1,5-iminoxylitol
-
potent inhibitor
1-([4-[(2-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)-3-phenylpropan-2-ol
-
-
1-([4-[(2-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)propan-2-ol
-
-
1-deoxynojirimycin
-
-
2,2'-([4-[(5-chloro-2-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]imino)diethanol
-
-
2-(4-(5-chloro-2-methoxyphenylamino)-6-(pyrrolidin-1-yl)-1,3,5-triazin-2-ylamino)ethanol
-
-
2-([4-(3,3-difluoropyrrolidin-1-yl)-6-[(2-methoxyphenyl)amino]-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-(benzylamino)-6-[(2-methoxyphenyl)amino]-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-(butylamino)-6-[(2-methoxyphenyl)amino]-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-azetidin-1-yl-6-[(2-methoxyphenyl)amino]-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(2,4-dimethoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(2,5-dimethoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(2-chlorophenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(2-ethoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(2-hydroxyethyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)benzamide
-
-
2-([4-[(2-hydroxyethyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)phenol
-
-
2-([4-[(2-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)acetamide
-
-
2-([4-[(2-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(2-methylphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(2-nitrophenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(2-phenoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(2-tert-butoxy-5-chlorophenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(2-tert-butoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(3-chlorophenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(3-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(3-methylphenyl)amino]-6-morpholin-4-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(3-methylphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(4-chlorophenyl)amino]-6-morpholin-4-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(4-chlorophenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(4-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(4-methylphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(5-benzyl-2-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(5-chloro-2-ethoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(5-chloro-2-methoxyphenyl)amino]-6-(diethylamino)-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(5-chloro-2-methoxyphenyl)amino]-6-azepan-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(5-chloro-2-methoxyphenyl)amino]-6-morpholin-4-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-([4-[(5-chloro-2-methoxyphenyl)amino]-6-piperidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
2-deoxy-2-fluoro-beta-D-glucopyranoside
-
-
2-[(4-pyrrolidin-1-yl-6-[[2-(trifluoromethoxy)phenyl]amino]-1,3,5-triazin-2-yl)amino]ethanol
-
-
2-[(4-[[2-(benzyloxy)phenyl]amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl)amino]ethanol
-
-
2-[(4-[[2-(methylsulfanyl)phenyl]amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl)amino]ethanol
-
-
2-[(4-[[2-methoxy-5-(trifluoromethyl)phenyl]amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl)amino]ethanol
-
-
2-[(4-[[5-chloro-2-(1-methylethoxy)phenyl]amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl)amino]ethanol
-
-
2-[[4-(phenylamino)-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino]ethanol
-
-
2-[[4-(prop-2-en-1-ylamino)-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino]ethanol
-
-
2R,5R-dihydroxymethyl-3R,4R-dihydroxypyrrolidine
-
-
4-([4-[(2-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)butan-1-ol
-
-
4-benzyl-2-([4-[(2-hydroxyethyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)phenol
-
-
4-chloro-2-([4-[(2-hydroxyethyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)phenol
-
-
4-eicosan-sphingenine
-
-
-
4-hexadecyl-sphingenine
-
-
-
4-methyl-N-(4-methyl-2-morpholin-4-ylquinolin-6-yl)cyclohexanecarboxamide
-
-
4-methyl-N-(4-methyl-2-piperidin-1-ylquinolin-6-yl)cyclohexanecarboxamide
-
-
4-methyl-N-[4-methyl-2-(4-methylpiperidin-1-yl)quinolin-6-yl]cyclohexanecarboxamide
-
-
4-methyl-N-[4-methyl-2-(4-pyrimidin-4-ylpiperazin-1-yl)-1,2-dihydroquinolin-6-yl]cyclohexanecarboxamide
-
-
4-O-(beta-D-glucopyranosyl)-N-butyl-2-O-butyl-1,5-dideoxy-1,5-imino-D-glucitol
-
-
4-octadecyl-sphingenine
-
-
-
4-octadecyl-threo-sphingenine
-
-
-
4-sphingenine
-
-
4-tetradecyl-sphingenine
-
-
-
4-undecyl-sphingenine
-
-
-
4-[4-(cyanomethoxy)phenyl]-4-oxo-N-{3-[(2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl]propyl}butanamide
-
-
4-[[(4-chlorophenyl)sulfonyl]amino]-N-(2,5-dihydro-1,3-thiazol-2-yl)benzamide
-
-
5-((4-methylphenyl)thio)-quinazoline 2,4-diamine
-
inhibition of wild-type enzyme and chaperone function on mutant enzyme. Treated fibroblasts from patients with Gaucher disease show decreased levels of enzyme in their endoplasmic reticulum and increased levels in lysosomes. Compound stabilizes a domain III active-site loop
5-(3,5-dichlorophenoxy)-N-(4-pyridinyl)-2-furamide
-
inhibition of wild-type enzyme and chaperone function on mutant enzyme. Treated fibroblasts from patients with Gaucher disease show decreased levels of enzyme in their endoplasmic reticulum and increased levels in lysosomes. Compound stabilizes a domain III active-site loop
5-N,6-O-[N'-(n-octyl)iminomethylidene]nojirimycin
-
potent inhibitor
-
5-N,6-S-[N'-(n-octyl)iminomethylidene]-6-thionojirimycin
-
potent inhibitor
-
6-amino-6-deoxy-5-N,6-N-[N'-(n-octyl)iminomethylidene]nojirimycin
-
-
-
6-bromo-6-deoxy-conduritol
-
-
6-bromo-6-deoxy-conduritol
-
-
6-bromo-6-deoxy-conduritol
-
-
6-bromo-conduritol-beta-epoxide
-
-
6-bromo-conduritol-beta-epoxide
-
-
6-bromo-conduritol-beta-epoxide
-
-
alkyl amines
-
-
Alkyl beta-glucosides
-
-
alpha-1-C-butyl-1-deoxynojirimycin
-
-
alpha-1-C-hexyl-1-deoxyimino-D-xylitol
-
-
alpha-1-C-hexyl-1-deoxynojirimycin
-
-
alpha-1-C-nonyl-1-deoxyimino-D-xylitol
-
strong inhibitor
alpha-1-C-propyl-1-deoxyimino-D-xylitol
-
-
alpha-1-C-propyl-1-deoxynojirimycin
-
-
beta-1-C-butyl-1,5-dideoxy-1,5-imino-L-iditol
-
-
beta-1-C-hexyl-1,5-dideoxy-1,5-imino-L-iditol
-
-
beta-1-C-propyl-1,5-dideoxy-1,5-imino-L-iditol
-
-
Ca2+
-
strong inhibition at 5 mM
calystegine A3
-
potent inhibitor
calystegine A5
-
-
calystegine B1
-
potent inhibitor
calystegine B2
-
potent inhibitor
calystegine B3
-
-
calystegine B4
-
-
calystegine C1
-
potent inhibitor
castanospermine
-
-
chondroitin sulfate
-
-
Co2+
-
complete inhibition at 5 mM
conduritol B epoxide
-
-
conduritol B epoxide
-
irreversible inhibitor
conduritol B epoxide
Q9HCG7
-
conduritol B-epoxide
-
-
conduritol-B-epoxide
-
irreversible
Cu2+
-
complete inhibition at 5 mM
cyclophellitol
-
oral application induces Gaucher like disease
Dextran sulfate
-
-
-
gluconolactone
-
competitive inhibitor
gluconolactone
-
-
glucose
-
at 220 mM
glucosylsphingosine
-
-
glucosylsphingosine
-
-
glycosylamine
-
-
-
Hg2+
-
complete inhibition at 5 mM
iminoglycolipid
-
-
-
isofagomine
-
potent inhibitor
isofagomine
-
competitive inhibition and role as a pharmacological chaperone. A hydrogen bonding network is formed between isofagomine and active site residues resulting in greater global stability and a shift in the melting curve by 15 degrees. Isofagomine enhances mutant enzyme activity in pre-treated N370S/N370S and F213L/L444P patient fibroblasts with Gaucher disease
methyl ([4-[(2-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)acetate
-
-
Mg2+
-
strong inhibition at 5 mM
Mn2+
-
strong inhibition at 5 mM
N-(2,5-dihydro-1,3-thiazol-2-yl)-4-[methyl(phenylsulfonyl)amino]benzamide
-
-
N-(4-methyl-2-morpholin-4-ylquinolin-6-yl)-4-propylcyclohexanecarboxamide
-
-
N-(4-methyl-2-morpholin-4-ylquinolin-6-yl)cyclopropanecarboxamide
-
-
N-(4-methyl-2-morpholinoquinolin-6-yl)cyclohexanecarboxamide
-
-
N-(5-adamantane-1-yl-methoxy)pentyl-deoxynojirimycin
-
extremely potent inhibitor for GBA2
N-(5-chloro-2-methoxyphenyl)-6-pyrrolidin-1-yl-1,3,5-triazine-2,4-diamine
-
-
N-(5-chloro-2-methoxyphenyl)-N'-(2-methoxyethyl)-6-pyrrolidin-1-yl-1,3,5-triazine-2,4-diamine
-
-
N-(5-chloro-2-methoxyphenyl)-N'-(furan-2-ylmethyl)-6-pyrrolidin-1-yl-1,3,5-triazine-2,4-diamine
-
-
N-(5-ethyl-1,3,4-thiadiazol-2-yl)-4-(phenylsulfonamido)benzamide
-
-
N-(5-ethyl-1,3,4-thiadiazolidin-2-yl)-4-[methyl(phenylsulfonyl)amino]benzamide
-
-
N-(5-methylisoxazol-3-yl)-4-(phenylsulfonamido)benzamide
-
-
N-(5-methylisoxazol-3-yl)-4-[methyl(phenylsulfonyl)amino]benzamide
-
-
N-benzyl-4-[(phenylsulfonyl)amino]benzamide
-
-
N-benzyl-N'-(5-chloro-2-methoxyphenyl)-6-pyrrolidin-1-yl-1,3,5-triazine-2,4-diamine
-
-
N-butyl-1-deoxynojirimycin
-
-
N-butyl-1-deoxynojirimycin
-
-
N-butyl-4-[(phenylsulfonyl)amino]benzamide
-
-
N-butyl-deoxynojirimycin
-
Miglustat
N-butyl-deoxynojirimycin
-
Zavesca
N-butyl-N'-(5-chloro-2-methoxyphenyl)-6-pyrrolidin-1-yl-1,3,5-triazine-2,4-diamine
-
-
N-butyldeoxynojirimycin
-
extremely potent inhibitor for GBA2
N-butyldeoxynojirimycin
-
Zavesca
N-butyldeoxynojirimycin
-
-
N-butylisofagomine
-
-
N-carboxynonyldeoxynojirimycin
-
-
N-decyl-1-deoxynojirimycin
-
-
N-decyl-1-deoxynojirimycin
-
-
N-decylglycosylamine
-
-
N-dodecyl-1-deoxynojirimycin
-
-
N-dodecyl-1-deoxynojirimycin
-
-
N-dodecyl-1-deoxynojirimycin
-
potent inhibitor
N-dodecyldeoxynojirimycin
-
-
N-dodecylglycosylamine
-
-
N-hexadecylglycosylamine
-
-
N-hexyl-1-deoxynojirimycin
-
-
N-Hexyl-D-glucosylsphingosine
-
-
N-Hexyl-D-glucosylsphingosine
-
-
N-hexylglycosylamine
-
-
N-hydroxy-6-pyrrolidin-1-yl-1,3,5-triazine-2,4-diamine
-
-
N-methyl-1-deoxynojirimycin
-
-
N-methyl-1-deoxynojirimycin
-
-
N-methylcalystegine B2
-
-
N-nonyl-1-deoxynojirimycin
-
-
N-nonyl-deoxynojirimycin
-
-
N-nonyldeoxynojirimycin
-
-
N-octadecylglycosylamine
-
-
N-octylglycosylamine
-
-
N-phenyl-4-[(phenylsulfonyl)amino]benzamide
-
-
N-propyl-1-deoxynojirimycin
-
-
N-tetradecyl-1-deoxynojirimycin
-
-
N-tetradecylglycosylamine
-
-
N-[2-(diethylamino)-4-methyl-1,2-dihydroquinolin-6-yl]-4-methylcyclohexanecarboxamide
-
-
N-[2-([4-[(2-hydroxyethyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)phenyl]acetamide
-
-
N-[2-([4-[(2-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethyl]acetamide
-
-
N-[2-[(3-chlorophenyl)amino]-4-methyl-1,2-dihydroquinolin-6-yl]-4-methylcyclohexanecarboxamide
-
-
N-{3-[4-(cyanomethoxy)benzoyl]benzoyl}propylamido-1-deoxynojirimycin
-
-
Ni2+
-
complete inhibition at 5 mM
nojirimycin bisulfite
-
-
p-hydroxymercuribenzoate
-
weak
p-nitrophenyl beta-D-glucopyranoside
-
inhibits mutant D223G
saposin C
-
-
-
Triton X-100
Q9HCG7
-
Monoclonal antibodies
-
100% inhibition with F1 and F2, 60% inhibition with no. 61
-
additional information
-
not inhibited by 4-O-(beta-D-glucopyranosyl)-N-butyl-1,5-dideoxy-1,5-imino-D-glucitol
-
additional information
-
not inhibited by conduritol B epoxide
-
additional information
-
not inhibited by beta-1-C-(2,3-dihydroxypropyl)-1,5-dideoxy-1,5-imino-L-iditol
-
additional information
-
isofagomine is not specific for the enzyme
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(3aR,4S,5R,6R,7S,7aS)-2-(3-phenylpropylimino)-octahydro-1H-benzo[d]imidazole-4,5,6,7-tetraol
-
Gcase activity increase: 1.9fold and 1.4fold in N370S and L44P, respectively, lymphoblasts from Gaucher patients
-
(3aR,4S,5R,6R,7S,7aS)-2-(nonylimino)-octahydro-1H-benzo[d]imidazole-4,5,6,7-tetraol
-
Gcase activity increase: 1.8fold and 1.4fold in N370S and L44P, respectively, lymphoblasts from Gaucher patients
-
(3aR,4S,5R,6S,7R,7aR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
Gcase activity increase: 1.8fold and 1.4fold in N370S and L44P, respectively, lymphoblasts from Gaucher patients
-
(3aR,4S,5R,6S,7R,7aS)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
Gcase activity increase: 1.7fold and 1.3fold in N370S and L44P, respectively, lymphoblasts from Gaucher patients
-
(3aRS,4SR,5RS,6SR,7RS,7aRS)- 2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
Gcase activity increase: 1.7fold in N370S lymphoblasts from Gaucher patients
-
(3aS,4S,5R,6S,7R,7aR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
Gcase activity increase: 1.4fold and 1.1fold in N370S and L44P, respectively, lymphoblasts from Gaucher patients
-
(3aS,4S,5R,6S,7R,7aS)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
Gcase activity increase: 2.1fold and 1.5fold in N370S and L44P, respectively, lymphoblasts from Gaucher patients
-
(3aSR,4SR,5RS,6SR,7RS,7aSR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
Gcase activity increase: 1.7fold in N370S lymphoblasts from Gaucher patients
-
Activator protein
-
-
-
dexamethasone
-
the pretreatment with dexamethasone has the effect of selectively increasing the uptake of wild-type and recombinant enzymes by the macrophages but not by the liver sinusoidal endothelial cells or hepatocyte cells in vitro, the dexamethasone pre-treatment increases the uptake of enzyme by kupffer cells and by splenic macrophages in vivo.
Dicetyl phosphate
-
-
glycoprotein
-
heat-stable
heat-stable factor
-
-
-
heat-stable factor
-
-
-
heat-stable factor
-
-
-
isofagomine
-
GlcCerase activity is enhanced in normal fibroblasts 1.3fold after treatment with 0.03 mM isofagomine for 5 days
Lubrol Px
-
activates when C12-4-nitrobenz-2-oxa-1,3-diazole labelled glucosylceramide is substrate at optimal concentration of 0.05-0.15%
N-(n-butyl)deoxynojirimycin
-
other names are miglustat and Zavesca, about 20% increase of wild type enzyme activity at 0.0025 and 0.005 mM
N-(n-nonyl) deoxynojirimycin
-
1.3-1.4fold increase in activity is observed for the wild type enzyme at 0.02 mM
N-nonyl-deoxynojirimycin
-
Gcase activity increase: 1.9fold in N370S lymphoblasts from Gaucher patients
phosphatidylglycerol
-
acidic phospholipids, fatty acid composition important, higher activation in combination with heat-stable factor
phosphatidylglycerol
-
required
phosphatidylglycerol
-
-
phosphatidylinositol
-
acidic, unsaturated phospholipid interfaces interact with acid beta-glucosidase to conform the enzyme into an active structure
phosphatidylserine
-
-
phosphatidylserine
-
-
phosphatidylserine
-
-
phosphatidylserine
-
acidic, unsaturated phospholipid interfaces interact with acid beta-glucosidase to conform the enzyme into an active structure
Phospholipid
-
the full catalytic activity requires phospholipid interfaces
saposin C
-
required for full activity reconstruction of pure enzyme, study of saposin C, acidic, unsaturated phospholipid and enzyme interaction
-
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
-
saposin C
-
-
-
saposin-A
-
sphingolipid activator protein, only in synergy with saposin-C
-
saposin-A
-
-
-
saposin-C
-
sphingolipid activator protein, SAP-2
-
saposin-C
-
activation varies depending on mutation
-
saposin-C
-
recombinant and mutant proteins
-
Sodium cholate
-
activates when C12-4-nitrobenz-2-oxa-1,3-diazole labelled glucosylceramide is substrate at concentration of optimal 0.5%
sodium taurocholate
-
required
sodium taurocholate
-
-
sodium taurocholate
-
-
sodium taurocholate
-
activation is pH-dependent
sodium taurodeoxycholate
-
-
Triton X-100
-
-
Triton X-100
-
activates when C12-4-nitrobenz-2-oxa-1,3-diazole labelled glucosylceramide is substrate at optimal concentration of 0.05-0.15%
Triton X-100
-
-
Tween 20
-
activates when C12-4-nitrobenz-2-oxa-1,3-diazole labelled glucosylceramide is substrate at optimal concentration of 0.05-0.15%
monoclonal antibody
-
no. 122 mimicking the effect of saposin C
-
additional information
-
The reconstruction of the activity of lysosomal enzyme requires phospholipids and a protein factor: saposin C. The hydrophobic properties of saposin C are regulated by the pH of the environment. The interaction of saposin C with membranes is affected by the content of anionic phospholipids
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00204
-
(6-[N-(7-nitrobenz-2-oxa-1,3 diazol-4-yl)amino]hexanoyl)-beta-D-galactosylceramide
-
in 50 mM MES buffer, pH 6.0, at 37C
0.00464
-
(6-[N-(7-nitrobenz-2-oxa-1,3 diazol-4-yl)amino]hexanoyl)-beta-D-glucosylceramide
-
in 50 mM MES buffer, pH 6.0, at 37C
0.05
-
12(N-methyl-N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl))aminohexyl-2-N-sphingosyl 1-O-beta-D-glucoside
-
-
0.0003
-
2,4-dinitrophenyl beta-D-glucopyranoside
-
pH 6.5, 37C, mutant E411A
0.15
-
2,4-dinitrophenyl beta-D-glucopyranoside
-
pH 6.5, 37C, mutant D223G
0.16
-
2,4-dinitrophenyl beta-D-glucopyranoside
-
pH 6.5, 37C, wild-type enzyme
0.1445
-
4-methylumbelliferyl-beta-D-galactopyranoside
-
in 50 mM MES buffer, pH 6.0, at 37C
0.04928
-
4-methylumbelliferyl-beta-D-glucopyranoside
-
in 50 mM MES buffer, pH 6.0, at 37C
0.636
-
4-methylumbelliferyl-beta-D-glucopyranoside
-
-
0.862
-
4-methylumbelliferyl-beta-D-glucopyranoside
-
in 50 mM citric acid, KH2PO4 (pH 5.9), 10 mM sodium taurocholate, and 0.01% Tween 20, at 21C
0.93
-
4-methylumbelliferyl-beta-D-glucopyranoside
-
-
1.5
-
4-methylumbelliferyl-beta-D-glucopyranoside
-
-
1.9
-
4-methylumbelliferyl-beta-D-glucopyranoside
-
-
2
-
4-methylumbelliferyl-beta-D-glucopyranoside
-
pH 5.9
2.1
3.7
4-methylumbelliferyl-beta-D-glucopyranoside
-
different patients
2.7
-
4-methylumbelliferyl-beta-D-glucopyranoside
-
in presence of phosphatidylserine and heat-stable factor
2.7
-
4-methylumbelliferyl-beta-D-glucopyranoside
-
-
3
-
4-methylumbelliferyl-beta-D-glucopyranoside
-
-
3.6
-
4-methylumbelliferyl-beta-D-glucopyranoside
-
-
4
-
4-methylumbelliferyl-beta-D-glucopyranoside
-
recombinant and mutant enzyme
24
-
4-methylumbelliferyl-beta-D-glucopyranoside
-
-
0.026
-
4-nonylumbelliferyl-beta-D-glucopyranoside
-
in presence of taurocholate
0.045
-
4-nonylumbelliferyl-beta-D-glucopyranoside
-
-
0.17
-
4-nonylumbelliferyl-beta-D-glucopyranoside
-
-
0.038
-
4-undecylumbelliferyl-beta-D-glucopyranoside
-
in presence of taurocholate
0.03
-
6(N-methyl-N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl))aminododecanoyl-2-N-sphingosyl 1-O-beta-D-glucoside
-
-
0.03
-
beta-D-glucocerebroside
-
-
-
0.055
-
beta-D-glucocerebroside
-
-
-
0.65
-
beta-D-glucocerebroside
-
-
-
0.00924
-
C18-galactosylceramide
-
in 50 mM MES buffer, pH 6.0, at 37C
0.01367
-
C18-glucosylceramide
-
in 50 mM MES buffer, pH 6.0, at 37C
0.042
-
D-glucosyl-N-butylsphingosine
-
-
0.032
-
D-glucosyl-N-ethylsphingosine
-
-
0.014
-
D-glucosyl-N-methylsphingosine
-
-
0.033
-
D-glucosyl-N-octylsphingosine
-
-
0.02
-
D-glucosyl-N-propylsphingosine
-
-
0.015
-
glucosylceramide
-
imiglucerase, in 50 mM sodium citrate, pH 6.0 with 0.75 mg/ml bovine serum albumin, at 37C
0.019
-
glucosylceramide
-
velaglucerase alfa, in 50 mM sodium citrate, pH 6.0 with 0.75 mg/ml bovine serum albumin, at 37C
0.08
-
glucosylceramide
-
-
0.223
-
glucosylceramide
-
pH 6.5, 37C
0.018
-
p-nitrophenyl beta-D-glucopyranoside
-
pH 6.5, 37C, mutant E411A
0.27
-
p-nitrophenyl beta-D-glucopyranoside
-
pH 6.5, 37C, wild-type enzyme
0.33
-
p-nitrophenyl beta-D-glucopyranoside
-
pH 6.5, 37C, mutant D223G
0.593
-
p-nitrophenyl-beta-glucopyranoside
-
pH 6.5, 37C, wild-type enzyme
1.35
-
p-nitrophenyl-beta-glucopyranoside
-
pH 6.5, 37C, mutant D223E
0.034
-
palmitylglucosyl ceramide
-
-
-
0.028
-
stearylglucosyl ceramide
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.03
-
(6-[N-(7-nitrobenz-2-oxa-1,3 diazol-4-yl)amino]hexanoyl)-beta-D-galactosylceramide
-
in 50 mM MES buffer, pH 6.0, at 37C
0.12
-
(6-[N-(7-nitrobenz-2-oxa-1,3 diazol-4-yl)amino]hexanoyl)-beta-D-glucosylceramide
-
in 50 mM MES buffer, pH 6.0, at 37C
0.012
-
2,4-dinitrophenyl beta-D-glucopyranoside
-
pH 6.5, 37C, mutant D223G
470
-
2,4-dinitrophenyl beta-D-glucopyranoside
-
pH 6.5, 37C, wild-type enzyme
1.57
-
4-methylumbelliferyl-beta-D-galactopyranoside
-
in 50 mM MES buffer, pH 6.0, at 37C
1.23
-
4-methylumbelliferyl-beta-D-glucopyranoside
-
in 50 mM MES buffer, pH 6.0, at 37C
0.007
-
C18-glucosylceramide
-
in 50 mM MES buffer, pH 6.0, at 37C
31.67
-
glucosylceramide
-
imiglucerase alfa, in 50 mM sodium citrate, pH 6.0 with 0.75 mg/ml bovine serum albumin, at 37C
35
-
glucosylceramide
-
velaglucerase alfa, in 50 mM sodium citrate, pH 6.0 with 0.75 mg/ml bovine serum albumin, at 37C
0.012
-
p-nitrophenyl beta-D-glucopyranoside
-
pH 6.5, 37C, mutant D223G
560
-
p-nitrophenyl beta-D-glucopyranoside
-
pH 6.5, 37C, wild-type enzyme
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00001
-
(3aR,4S,5R,6R,7S,7aS)-2-(3-phenylpropylimino)-octahydro-1H-benzo[d]imidazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.000003
-
(3aR,4S,5R,6R,7S,7aS)-2-(nonylimino)-octahydro-1H-benzo[d]imidazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0018
-
(3aR,4S,5R,6S,7R,7aR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0048
-
(3aR,4S,5R,6S,7R,7aR)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0015
-
(3aR,4S,5R,6S,7R,7aS)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0088
-
(3aR,4S,5S,6S,7R,7aR)-4-(benzyloxy)-2-(nonylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.0111
-
(3aRS,4SR,5RS,6SR,7RS,7aRS)- 2-(hexylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.00044
-
(3aRS,4SR,5RS,6SR,7RS,7aRS)- 2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0017
-
(3aRS,4SR,5RS,6SR,7RS,7aRS)- 2-(octylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0024
-
(3aRS,4SR,5RS,6SR,7RS,7aSR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0259
-
(3aRS,4SR,5SR,6SR,7RS,7aRS)-4-(benzyloxy)-2-(hexylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.00053
-
(3aRS,4SR,5SR,6SR,7RS,7aRS)-4-(benzyloxy)-2-(nonylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.0036
-
(3aRS,4SR,5SR,6SR,7RS,7aRS)-4-(benzyloxy)-2-(octylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.00004
-
(3aS,4S,5R,6S,7R,7aR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0125
-
(3aS,4S,5R,6S,7R,7aR)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.000002
-
(3aS,4S,5R,6S,7R,7aS)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0028
-
(3aS,4S,5R,6S,7R,7aS)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.00018
-
(3aS,4S,5S,6S,7R,7aS)-4-(benzyloxy)-2-(nonylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.0034
-
(3aSR,4SR,5RS,6SR,7RS,7aRS)-2-(hexylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.00007
-
(3aSR,4SR,5RS,6SR,7RS,7aRS)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.00023
-
(3aSR,4SR,5RS,6SR,7RS,7aRS)-2-(octylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.00004
-
(3aSR,4SR,5RS,6SR,7RS,7aSR)-2-(hexylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.000002
-
(3aSR,4SR,5RS,6SR,7RS,7aSR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.000007
-
(3aSR,4SR,5RS,6SR,7RS,7aSR)-2-(octylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0013
-
(3aSR,4SR,5SR,6SR,7RS,7aSR)-4-(benzyloxy)-2-(hexylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.00047
-
(3aSR,4SR,5SR,6SR,7RS,7aSR)-4-(benzyloxy)-2-(nonylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.00013
-
(3aSR,4SR,5SR,6SR,7RS,7aSR)-4-(benzyloxy)-2-(octylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
2.4
-
2-deoxy-2-fluoro-beta-D-glucopyranoside
-
pH 6.5, 37C
2.2
-
alpha-1-C-nonyl-1-deoxyimino-D-xylitol
-
in 0.15 M citrate-phosphate buffer (pH 5.5), 1% sodium taurocholate/Triton X-100, at 37C
0.0005
-
calystegine B1
-
pH 4.5, 37C
0.0015
-
calystegine B1
-
pH 4.5, 37C
0.0009
-
calystegine C1
-
pH 4.5, 37C
0.0003
-
N-nonyl-deoxynojirimycin
-
pH 5.2, 37C
1.7
-
p-nitrophenyl beta-D-glucopyranoside
-
pH 6.5, 37C, mutant D223G
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0167
-
(1R,2R,3S,4S,5R,6S)-7-oxabicyclo[4.1.0]heptane-2,3,4,5-tetrol
-
-
0.00001
-
(3aR,4S,5R,6R,7S,7aS)-2-(3-phenylpropylimino)-octahydro-1H-benzo[d]imidazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.00004
-
(3aR,4S,5R,6R,7S,7aS)-2-(3-phenylpropylimino)-octahydro-1H-benzo[d]imidazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.000004
-
(3aR,4S,5R,6R,7S,7aS)-2-(nonylimino)-octahydro-1H-benzo[d]imidazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.00001
-
(3aR,4S,5R,6R,7S,7aS)-2-(nonylimino)-octahydro-1H-benzo[d]imidazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0017
-
(3aR,4S,5R,6S,7R,7aR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.006
-
(3aR,4S,5R,6S,7R,7aR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0012
-
(3aR,4S,5R,6S,7R,7aR)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.0104
-
(3aR,4S,5R,6S,7R,7aR)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.00032
-
(3aR,4S,5R,6S,7R,7aS)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.0019
-
(3aR,4S,5R,6S,7R,7aS)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0567
-
(3aR,4S,5R,6S,7R,7aS)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.16
-
(3aR,4S,5R,6S,7R,7aS)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0173
-
(3aR,4S,5S,6S,7R,7aR)-4-(benzyloxy)-2-(nonylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.157
-
(3aR,4S,5S,6S,7R,7aR)-4-(benzyloxy)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.0044
-
(3aRS,4SR,5RS,6SR,7RS,7aRS)- 2-(hexylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.0129
-
(3aRS,4SR,5RS,6SR,7RS,7aRS)- 2-(hexylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.00019
-
(3aRS,4SR,5RS,6SR,7RS,7aRS)- 2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.00071
-
(3aRS,4SR,5RS,6SR,7RS,7aRS)- 2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.00054
-
(3aRS,4SR,5RS,6SR,7RS,7aRS)- 2-(octylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.0025
-
(3aRS,4SR,5RS,6SR,7RS,7aRS)- 2-(octylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0006
-
(3aRS,4SR,5RS,6SR,7RS,7aSR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.0029
-
(3aRS,4SR,5RS,6SR,7RS,7aSR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0644
-
(3aRS,4SR,5SR,6SR,7RS,7aRS)-4-(benzyloxy)-2-(hexylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.0013
-
(3aRS,4SR,5SR,6SR,7RS,7aRS)-4-(benzyloxy)-2-(nonylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.0064
-
(3aRS,4SR,5SR,6SR,7RS,7aRS)-4-(benzyloxy)-2-(octylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.00002
-
(3aS,4S,5R,6S,7R,7aR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.00012
-
(3aS,4S,5R,6S,7R,7aR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0056
-
(3aS,4S,5R,6S,7R,7aR)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.0111
-
(3aS,4S,5R,6S,7R,7aR)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.000005
-
(3aS,4S,5R,6S,7R,7aS)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.000008
-
(3aS,4S,5R,6S,7R,7aS)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0024
-
(3aS,4S,5R,6S,7R,7aS)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.0068
-
(3aS,4S,5R,6S,7R,7aS)-3-nonyl-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.00035
-
(3aS,4S,5S,6S,7R,7aS)-4-(benzyloxy)-2-(nonylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.0016
-
(3aSR,4SR,5RS,6SR,7RS,7aRS)-2-(hexylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.0064
-
(3aSR,4SR,5RS,6SR,7RS,7aRS)-2-(hexylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.00004
-
(3aSR,4SR,5RS,6SR,7RS,7aRS)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.00022
-
(3aSR,4SR,5RS,6SR,7RS,7aRS)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.00008
-
(3aSR,4SR,5RS,6SR,7RS,7aRS)-2-(octylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.0006
-
(3aSR,4SR,5RS,6SR,7RS,7aRS)-2-(octylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.00004
-
(3aSR,4SR,5RS,6SR,7RS,7aSR)-2-(hexylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.0001
-
(3aSR,4SR,5RS,6SR,7RS,7aSR)-2-(hexylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.000008
-
(3aSR,4SR,5RS,6SR,7RS,7aSR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.000009
-
(3aSR,4SR,5RS,6SR,7RS,7aSR)-2-(nonylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.00001
-
(3aSR,4SR,5RS,6SR,7RS,7aSR)-2-(octylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 7.0, 37C
-
0.0002
-
(3aSR,4SR,5RS,6SR,7RS,7aSR)-2-(octylimino)-octahydrobenzo[d]oxazole-4,5,6,7-tetraol
-
pH 5.2, 37C
-
0.0039
-
(3aSR,4SR,5SR,6SR,7RS,7aSR)-4-(benzyloxy)-2-(hexylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.0017
-
(3aSR,4SR,5SR,6SR,7RS,7aSR)-4-(benzyloxy)-2-(nonylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.00074
-
(3aSR,4SR,5SR,6SR,7RS,7aSR)-4-(benzyloxy)-2-(octylimino)-octahydrobenzo[d]oxazole-5,6,7-triol
-
pH 5.2, 37C
-
0.16
-
1,4-dideoxy-1,4-imino-D-arabinitol
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.0023
-
1,5-dideoxy-1,5-iminoxylitol
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.0068
-
1-([4-[(2-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)-3-phenylpropan-2-ol
-
-
0.0207
-
1-([4-[(2-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)propan-2-ol
-
-
0.0288
-
1-deoxynojirimycin
-
non-lysosomal GBA2
0.24
-
1-deoxynojirimycin
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.506
-
1-deoxynojirimycin
-
lysosomal GBA
0.00043
-
2-(4-(5-chloro-2-methoxyphenylamino)-6-(pyrrolidin-1-yl)-1,3,5-triazin-2-ylamino)ethanol
-
-
0.0007
-
2-(4-(5-chloro-2-methoxyphenylamino)-6-(pyrrolidin-1-yl)-1,3,5-triazin-2-ylamino)ethanol
-
-
0.0075
-
2-([4-(3,3-difluoropyrrolidin-1-yl)-6-[(2-methoxyphenyl)amino]-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.0188
-
2-([4-(benzylamino)-6-[(2-methoxyphenyl)amino]-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.0061
-
2-([4-(butylamino)-6-[(2-methoxyphenyl)amino]-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00231
-
2-([4-azetidin-1-yl-6-[(2-methoxyphenyl)amino]-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.0049
-
2-([4-[(2,4-dimethoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00153
-
2-([4-[(2,5-dimethoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.02897
-
2-([4-[(2-chlorophenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00077
-
2-([4-[(2-ethoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.002
-
2-([4-[(2-hydroxyethyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)phenol
-
-
0.00108
-
2-([4-[(2-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00394
-
2-([4-[(2-methylphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.0314
-
2-([4-[(2-phenoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00104
-
2-([4-[(2-tert-butoxy-5-chlorophenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00033
-
2-([4-[(2-tert-butoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00669
-
2-([4-[(3-chlorophenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00825
-
2-([4-[(3-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.0477
-
2-([4-[(3-methylphenyl)amino]-6-morpholin-4-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00431
-
2-([4-[(3-methylphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00619
-
2-([4-[(3-methylphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.0465
-
2-([4-[(4-chlorophenyl)amino]-6-morpholin-4-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00634
-
2-([4-[(4-chlorophenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00773
-
2-([4-[(4-chlorophenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.0088
-
2-([4-[(4-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.01004
-
2-([4-[(4-methylphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00222
-
2-([4-[(5-benzyl-2-methoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00096
-
2-([4-[(5-chloro-2-ethoxyphenyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.01213
-
2-([4-[(5-chloro-2-methoxyphenyl)amino]-6-morpholin-4-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.0311
-
2-([4-[(5-chloro-2-methoxyphenyl)amino]-6-piperidin-1-yl-1,3,5-triazin-2-yl]amino)ethanol
-
-
0.00334
-
2-[(4-pyrrolidin-1-yl-6-[[2-(trifluoromethoxy)phenyl]amino]-1,3,5-triazin-2-yl)amino]ethanol
-
-
0.02167
-
2-[(4-[[2-(benzyloxy)phenyl]amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl)amino]ethanol
-
-
0.00239
-
2-[(4-[[2-(methylsulfanyl)phenyl]amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl)amino]ethanol
-
-
0.00265
-
2-[(4-[[2-methoxy-5-(trifluoromethyl)phenyl]amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl)amino]ethanol
-
-
0.00344
-
2-[(4-[[5-chloro-2-(1-methylethoxy)phenyl]amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl)amino]ethanol
-
-
0.01647
-
2-[[4-(phenylamino)-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino]ethanol
-
-
0.28
-
2R,5R-dihydroxymethyl-3R,4R-dihydroxypyrrolidine
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.00037
-
4-benzyl-2-([4-[(2-hydroxyethyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)phenol
-
-
0.00073
-
4-chloro-2-([4-[(2-hydroxyethyl)amino]-6-pyrrolidin-1-yl-1,3,5-triazin-2-yl]amino)phenol
-
-
0.000063
-
4-methyl-N-(4-methyl-2-morpholin-4-ylquinolin-6-yl)cyclohexanecarboxamide
-
-
0.000452
-
4-methyl-N-(4-methyl-2-piperidin-1-ylquinolin-6-yl)cyclohexanecarboxamide
-
-
0.000268
-
4-methyl-N-[4-methyl-2-(4-methylpiperidin-1-yl)quinolin-6-yl]cyclohexanecarboxamide
-
-
0.00245
-
4-methyl-N-[4-methyl-2-(4-pyrimidin-4-ylpiperazin-1-yl)-1,2-dihydroquinolin-6-yl]cyclohexanecarboxamide
-
-
0.000075
-
4-[4-(cyanomethoxy)phenyl]-4-oxo-N-{3-[(2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl]propyl}butanamide
-
non-lysosomal GBA2
0.00165
-
4-[4-(cyanomethoxy)phenyl]-4-oxo-N-{3-[(2R,3R,4R,5S)-3,4,5-trihydroxy-2-(hydroxymethyl)piperidin-1-yl]propyl}butanamide
-
lysosomal GBA
0.00129
-
4-[[(4-chlorophenyl)sulfonyl]amino]-N-(2,5-dihydro-1,3-thiazol-2-yl)benzamide
-
-
0.0078
-
5-((4-methylphenyl)thio)-quinazoline 2,4-diamine
-
pH 5.5, 37C
0.0047
-
5-(3,5-dichlorophenoxy)-N-(4-pyridinyl)-2-furamide
-
pH 5.5, 37C
0.1
-
alpha-1-C-butyl-1-deoxynojirimycin
-
in 0.15 M citrate-phosphate buffer (pH 5.5), 1% sodium taurocholate/Triton X-100, at 37C
0.000019
-
alpha-1-C-hexyl-1-deoxyimino-D-xylitol
-
in 0.15 M citrate-phosphate buffer (pH 5.5), 1% sodium taurocholate/Triton X-100, at 37C
0.0042
-
alpha-1-C-hexyl-1-deoxynojirimycin
-
in 0.15 M citrate-phosphate buffer (pH 5.5), 1% sodium taurocholate/Triton X-100, at 37C
0.00056
-
alpha-1-C-propyl-1-deoxyimino-D-xylitol
-
in 0.15 M citrate-phosphate buffer (pH 5.5), 1% sodium taurocholate/Triton X-100, at 37C
0.4
-
alpha-1-C-propyl-1-deoxynojirimycin
-
in 0.15 M citrate-phosphate buffer (pH 5.5), 1% sodium taurocholate/Triton X-100, at 37C
0.147
-
beta-1-C-butyl-1,5-dideoxy-1,5-imino-L-iditol
-
in 0.15 M citrate-phosphate buffer (pH 5.5), 1% sodium taurocholate/Triton X-100, at 37C
0.043
-
beta-1-C-hexyl-1,5-dideoxy-1,5-imino-L-iditol
-
in 0.15 M citrate-phosphate buffer (pH 5.5), 1% sodium taurocholate/Triton X-100, at 37C
0.487
-
beta-1-C-propyl-1,5-dideoxy-1,5-imino-L-iditol
-
in 0.15 M citrate-phosphate buffer (pH 5.5), 1% sodium taurocholate/Triton X-100, at 37C
0.0031
-
calystegine A3
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.031
-
calystegine A5
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.0025
-
calystegine B1
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.001
-
calystegine B2
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.076
-
calystegine B3
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.082
-
calystegine B4
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.0025
-
calystegine C1
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.019
-
castanospermine
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.000005
-
isofagomine
-
wild type enzyme, at pH 7.2
0.000009
-
isofagomine
-
wild type enzyme, at pH 6.4
0.000018
-
isofagomine
-
mutant enzyme N370S, at pH 5.2
0.000026
-
isofagomine
-
mutant enzyme N370S, at pH 6.4
0.00003
-
isofagomine
-
wild type enzyme, at pH 5.2
0.00004
-
isofagomine
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.000128
-
isofagomine
-
mutant enzyme N370S, at pH 7.2
0.2
-
isofagomine
-
in 50 mM citrate buffer with 0.25% (v/v) Triton X-100 (pH 4.5)
0.0344
-
N-(2,5-dihydro-1,3-thiazol-2-yl)-4-[methyl(phenylsulfonyl)amino]benzamide
-
-
0.000133
-
N-(4-methyl-2-morpholin-4-ylquinolin-6-yl)-4-propylcyclohexanecarboxamide
-
-
0.000183
-
N-(4-methyl-2-morpholin-4-ylquinolin-6-yl)cyclopropanecarboxamide
-
-
0.000031
-
N-(4-methyl-2-morpholinoquinolin-6-yl)cyclohexanecarboxamide
-
-
0.00007
-
N-(5-ethyl-1,3,4-thiadiazol-2-yl)-4-(phenylsulfonamido)benzamide
-
-
0.000103
-
N-(5-ethyl-1,3,4-thiadiazol-2-yl)-4-(phenylsulfonamido)benzamide
-
-
0.00296
-
N-(5-ethyl-1,3,4-thiadiazolidin-2-yl)-4-[methyl(phenylsulfonyl)amino]benzamide
-
-
0.000168
-
N-(5-methylisoxazol-3-yl)-4-(phenylsulfonamido)benzamide
-
-
0.0252
-
N-(5-methylisoxazol-3-yl)-4-[methyl(phenylsulfonyl)amino]benzamide
-
-
0.1
-
N-benzyl-4-[(phenylsulfonyl)amino]benzamide
-
IC50 above 0.1 mM
0.27
-
N-butyl-1-deoxynojirimycin
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-glucopyranoside as substrate
0.0246
-
N-butyl-4-[(phenylsulfonyl)amino]benzamide
-
-
0.044
-
N-butyl-isofagomine
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.00777
-
N-butyl-N'-(5-chloro-2-methoxyphenyl)-6-pyrrolidin-1-yl-1,3,5-triazine-2,4-diamine
-
-
0.002
-
N-butyldeoxynojirimycin
-
in 50 mM citrate buffer with 0.25% (v/v) Triton X-100 (pH 4.5)
0.00014
-
N-carboxy-nonyldeoxynojirimycin
-
-
0.00005
-
N-dodecyl-1-deoxynojirimycin
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.0229
-
N-dodecyl-deoxynojirimycin
-
-
0.32
-
N-methyl-calystegine B2
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
0.0003
-
N-nonyl-deoxynojirimycin
-
pH 7.0, 37C
0.00066
-
N-nonyl-deoxynojirimycin
-
pH 5.2, 37C
0.00646
-
N-phenyl-4-[(phenylsulfonyl)amino]benzamide
-
-
0.00106
-
N-[2-(diethylamino)-4-methyl-1,2-dihydroquinolin-6-yl]-4-methylcyclohexanecarboxamide
-
-
0.00002
-
N-{3-[4-(cyanomethoxy)benzoyl]benzoyl}propylamido-1-deoxynojirimycin
-
non-lysosomal GBA2
0.00035
-
N-{3-[4-(cyanomethoxy)benzoyl]benzoyl}propylamido-1-deoxynojirimycin
-
lysosomal GBA
0.028
-
nojirimycin bisulfite
-
in 0.1 M citrate buffer (pH 5.2), using 4-methylumbelliferyl-beta-D-glucopyranoside as substrate
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00007
-
-
mutant E235A
0.00008
-
-
mutant E340A
0.0046
-
-
wild-type enzyme
0.02
-
-
expressed activity of wild-type enzyme
0.075
0.1
-
enzyme in cell lines from two patients with Niemann-Pick disease type C
0.4
-
-
enzyme in normal fibroblasts
2.5
-
-
-
3.57
-
-
-
16.6
-
-
-
26.7
-
-
-
additional information
-
-
Cells transfected with wild-type enzyme diplays significant levels of enzyme activity, about 90% increase with respect to non-transfected cells
additional information
-
-
the difference in activity between the control and the mutated cells correlates well with difference in the enzyme mass
additional information
-
-
comparison of activity of probands with Parkinson`s disease and enzyme gene alteration
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
5
-
-
4.8
5.8
-
taurocholate shifts pH-optimum for hydrolysis of nonylumbelliferyl-beta-D-glucose from 5.8 to 4.9, activator protein shifts pH-optimum for hydrolysis of methylumbelliferyl-beta-D-glucose from 5.8 to 4.3
5
-
-
addition of heat-stable factor shifts pH-optimum for hydrolysis of methylumbelliferyl-beta-D-glucose from 6.5 to 5.0
5.2
-
-
assay at
5.5
-
-
-
5.6
-
-
-
5.6
-
-
-
6
6.6
-
-
6.2
-
-
-
7
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
6
-
pH 3.5: about 40% of maximum activity, pH 6.0: about 20% of maximum activity
4.5
7.5
-
-
4.8
5.8
-
-
5
6.5
-
-
5
8
-
pH 5.0: about 70% of maximum activity, pH 8.0: about 30% of maximum activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
37
-
-
assay at
37
-
-
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
highest activity in stratum corneum
Manually annotated by BRENDA team
-
mainly present in the upper epidermis, decreased in psoriatic skin compared to normal control, increased in lesional compared to non-lesional psoriatic skin
Manually annotated by BRENDA team
-
normal fibroblasts and fibroblasts of patients with Gaucher disease
Manually annotated by BRENDA team
-
derived from Gaucher patients homozygous for N370S (non-neuronophatic form) or L444P (neuronophatic form)
Manually annotated by BRENDA team
-
recombinant glucocerebrosidase uptake by Gaucher disease human osteoblast culture model
Manually annotated by BRENDA team
-
Gaucher disease
Manually annotated by BRENDA team
-
non-lysosomal GBA2
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
endolysosomal enzyme
Manually annotated by BRENDA team
-
LIMP-2 is the receptor for the mannose-6-phosphate independent transport of beta-glucocerebrosidase to the lysosome
Manually annotated by BRENDA team
-
bound; bound to acidic lipids in membranes
Manually annotated by BRENDA team
-
similar enzyme
-
Manually annotated by BRENDA team
Q9HCG7
GBA2 is in part associated with the outer layer of plasma membranes
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
52000
-
-
after deglycosylation, SDS-PAGE
56000
-
-
gel filtration, SDS-PAGE
56000
-
-
gel filtration, SDS-PAGE
57000
-
-
after deglycosylation, SDS-PAGE
59000
-
-
gel filtration, SDS-PAGE
59000
-
-
3 forms, 66000 Da and 62500 Da, absent in Gaucher disease patients, gel filtration, SDS-PAGE
59000
-
-
-
60000
-
-
gel filtration, SDS-PAGE
62500
-
-
3 forms, 66000 Da and 59000 Da, gel filtration, SDS-PAGE
63000
-
-
SDS-PAGE, Gaucher disease enzyme
63000
-
-
-
63000
-
-
SDS-PAGE
63000
-
-
SDS-PAGE
64000
-
-
gel filtration, SDS-PAGE
64000
-
-
gel filtration, SDS-PAGE
64000
-
-
endo-H-sensitive form, expressed in CHO cell
66000
-
-
3 forms, 62500 Da and 59000 Da, gel filtration, SDS-PAGE
67000
-
-
SDS-PAGE
67000
-
-
radiation inactivation, normal enzyme
67000
-
-
-
68000
-
-
gel filtration, SDS-PAGE
69000
-
-
endo-H-resistant form, expressed in CHO cell
70000
-
-
gel filtration, SDS-PAGE
75000
-
-
gel filtration, SDS-PAGE
92020
-
-
electrospray ionisation mass spectrometry
125000
-
-
radiation inactivation, Gaucher disease enzyme
138000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 90700, SDS-PAGE
dimer
-
2 * 57000, SDS-PAGE
dimer
-
2 * 70000, SDS-PAGE
monomer
-
1 * 67000, subunit coupling in Gaucher disease enzyme
monomer
-
in tissues: monomer or aggregate, interconvertible
tetramer
-
4 * 60000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
contains mannose residues
glycoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cocrystallization with inhibitors using the micro-batch technique, with 0.2 M (NH4)2SO4/0.1 M Tris, pH 6.5, 25% (w/v) polyethylene glycol 3350 or 0.2 M NH4COOCH3/0.1 M HEPES, pH 7.5, 25% (w/v) polyethyleneglycol 3350
-
crystallization and X-ray analysis of recombinant enzyme
-
hanging drop vapour diffusion method with 0.1 M Tris-HCl buffer, pH 8.5, containing 0.2 M magnesium chloride, 27.5% PEG 3350, 5% glycerol, 0.5 M glucose or 0.5 M galactose
-
in complex beta-cyclodextrin and either 5-N,6-O-[N'-(n-octyl)iminomethylidene]nojirimycin or 5-N,6-S-[N'-(n-octyl)iminomethylidene]-6-thionojirimycin, microbatch under oil method, using 0.2 M (NH4)2SO4, 0.1 M Tris pH 6.5, and 25% (w/v) PEG3350
-
microbatch crystallization, the crystallization solution contains a 1:1 ratio of the concentrated enzyme solution and 2 M (NH4)2SO4, 0.1 M Bis-Tris pH 5.5
-
velaglucerase alfa, micro-batch crystallization under oil, using 1 M (NH4)2SO4/0.1 M HEPES, pH 7.0, containing 0.5% (w/v) PEG8000
-
X-ray structure of enzyme at 2.0 A resolution
-
X-ray structure of human acid-beta-glucosidase covalently bound to conduritol-B-epoxide
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
30 min, 10% loss of activity
5.5
-
-
rapid loss
6
8
-
stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42
-
-
60 min, 10% loss of activity
50
-
-
60 min, 60% loss of activity
50
-
-
60 min, no loss of activity
52
-
-
60 min, pH 5.8, 70% loss of activity
60
-
-
for 0-30 min, maximum protection with heat-stable factor
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
freezing destroys activity
-
chemical chaperones stabilize Gaucher disease-associated glucocerebroside variants N370S and G202R against misfolding, enabling their trafficking from the endoplasmic reticulum. The L44P variant is not chaperoned, likely because this mutation destabilizes a domain distinct from the catalytic domain
-
dithiothreitol stabilizes in later stages of chromatographic separation
-
freezing destroys activity
-
glycerol stabilizes in later stages of chromatographic separation
-
phospholipid, preincubation stabilizes
-
freezing destroys activity
-
dialysis, stable to
-
freezing destroys activity
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
forced oxidation of GCase that results in a 40-60% reduction in in vitro biological activity affects the stability of some key structural elements within the catalytic site. These changes in dynamics occur on a longer time scale that is irrelevant for catalysis, effectively ruling out loss of structure in the catalytic site as a major factor contributing to the reduction of the catalytic activity. Oxidation also leads to noticeable destabilization of conformation in remote protein segments on a much larger scale, which is likely to increase the aggregation propensity of GCase and affect its bioavailability
-
716853
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 25% glycerol, several months, no loss of activity
-
-20C, pH 6, 90% ethylene glycol, 20 days, no loss of activity
-
-43C, 50% ethylene glycerol, several weeks, no loss of activity
-
0C, 90% ethylene glycol, several weeks, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Hi-Trap Chelating HP column chromatography and Superdex 200 10/300 gel filtration
-
hydrophobic interaction chromatography
-
immunoaffinity chromatography
-
of the recombinant protein
-
PS20 ProteinChip Arrays with the immobilized anti-GC mAb 8E4
-
recombinant enzyme
-
recombinant enzyme from transgenic tobacco seeds
-
to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in COS-7 cells
-
alterations in enzyme gene are identified in 12 of the 57 subjects with Parkinson`s disease
-
expressed in Chinese hamster ovary cells
-
expressed in Chinese hamster ovary cells and in transgenic carrot cells
-
expressed in CHO cells and Tn-5 cells
-
expressed in COS-7 cells
-
expressed in cultured plant cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expressed in Mus musculus liver
-
expressed in Sf9 insect cells
-
expression in Escherichia coli
-
expression in mouse fibroblasts NIH3T3
-
expression in NIH 3T3 cells
-
expression in Sf9 cells
-
expression of mutant and wild-type enzymes in murine cells
-
expression of wild-type and mutant enzymes by vaccinia based system, the wild-type and mutant enzymes are expressed in Gaucher fibroblast cell line L444P/S107L, HeLa G and BSC40, only enzyme-deficient fibroblasts are suitable for expression using plasmid transfection
-
gene-activated GCase is produced in an immortalized human cell line (HT-1080) utilizing targeted recombination with a promoter that activates the endogenous GCase in the presence of the mannosidase I inhibitor kifunensine, which results in a molecule with predominantly high-mannose-type glycans
-
overexpression in CHO cells, transfected with the tetracycline transactivation conditional expression system, majority of enzyme is secreted and overexpression in C2C12 cells, transducted with MFG-enzyme retrovirus
-
recombinant glucocerebrosidase uptake by Gaucher disease human osteoblast culture model
-
the mutated gene is subcloned into the mammalian expression vector pCR(R) 3.1 and expressed by transient transfection in COS cells
-
using fragments of the enzyme cDNA fused to the luciferase c DNA as a translational read-through reporter, the impact of synonymous codon usage bias on protein expression in Pichia pastoris as a potential system for the high-level heterologous production of human enzyme
-
expression in NIH 3T3 cells
P17439
expression in Escherichia coli
-
comparative and genetic analysis of the porcine glucocerebrosidase gene
Q70KH2
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1263del55
-
the activity is significantly reduced
1326insT
-
the activity is significantly reduced
303-305delCAC
-
mutation identified in a homozygous state in one patient of Gaucher disease type 1 or 3
72delC
-
the activity is significantly reduced
C16S
-
homozygosity for the missense mutation C16S results in the loss of a cysteine residue. The genotype would be predicted to result in virtually zero enzyme activity
D140H
-
mean activity of mutant compared to wild-type: 67.7%
D140H/E326K
-
mean activity of mutant compared to wild-type: 22.2%
D358E
-
no activity on glucosylceramide and 4-methylumbelliferyl-beta-D-glucopyranoside
D409H
-
the activity is significantly reduced
D409H
-
a transport block in the endoplasmic reticulum of the enzyme with the mutation D409H
D409H
-
mutation present in humans with Gaucher disease
D409H
-
the GBA mutation is associated with severe Lewy body disorder
D409H
-
the mutant shows about 17% activity compared to the wild type enzyme
D409H/T369M
-
the activity is significantly reduced
D419A
-
the mutation is associated with Parkinsons disease
D448H
-
the mutation is associated with Parkinsons disease
D482N
-
the mutation is associated with Parkinsons disease
E235A
-
the mutant is catalytically inactive
E326K
-
the GBA mutation is associated with Lewy body disorder
E326K
-
the mutant shows about 30% activity compared to the wild type enzyme
E326K
-
Gaucher disease causing mutation in human. Mean activity of mutant compared to wild-type: 38.7%. Considering the biochemical data together with the patients' data: E326K is a very mild mutation and, therefore, does not appear as a single mutation on a Gaucher disease allele. It further depresses the enzymatic activity of any other GBA mutation with which it appears in cis
E326K/N188R
-
the GBA mutation is associated with Lewy body disorder
E340A
-
the mutant is catalytically inactive
E388K
-
the GBA mutation is associated with Lewy body disorder
F109V
P04062
Gaucher disease mutation, less active
F213I
-
inhibitors 5-((4-methylphenyl)thio)-quinazoline 2,4-diamine and 5-(3,5-dichlorophenoxy)-N-(4-pyridinyl)-2-furamide raise the levels of functional GCase 1.5-2.5-fold in N370S or F213I Gaucher disease fibroblasts. Treated fibroblasts from patients with Gaucher disease show decreased levels of enzyme in their endoplasmic reticulum and increased levels in lysosomes. Compound stabilizes a domain III active-site loop
F213L
-
isofagomine enhances mutant enzyme activity in pre-treated N370S/N370S and F213L/L444P patient fibroblasts with Gaucher disease
G202E
-
the activity is significantly reduced
G202R
-
point mutation can cause Gaucher disease, mutant is destabilized in the neutral pH environment of the endoplasmic reticulum, rendering it prone to endoplasmic reticulum associated degradation
G202R
-
a transport block in the endoplasmic reticulum of the enzyme with the mutation G202R
G202R
-
the mutant shows about 25% activity compared to the wild type enzyme
G232E
-
the mutation is associated with Parkinsons disease
G377S
P04062
Gaucher disease mutation, less active
G377S
-
the mutant shows about 25% activity compared to the wild type enzyme
G389V
-
the GBA mutation is associated with Lewy body disorder
H255Q
-
the GBA mutation is associated with severe Lewy body disorder
H255Q
-
the mutant shows about 75% activity compared to the wild type enzyme
H255Q/D409H
-
the mutant shows about 20% activity compared to the wild type enzyme
I402T
-
the mutant shows about 19% activity compared to the wild type enzyme
K46E
-
the mutation is associated with Parkinsons disease
L174P
-
mutation present in humans with Gaucher disease
L296V
-
mutation associated with the severe phenotype of type 1 Gaucher disease
L336P
-
37% activity in comparison to wild-type enzyme, a natural occurring mutation in a patient with Gaucher disease
L444P
-
Gaucher disease mutation, reduced amounts of protein in cells
L444P
-
23.4% activity in comparison to wild-type enzyme, the mutation is used as control
L444P
-
the activity is significantly reduced
L444P
-
point mutation can cause Gaucher disease, mutant is destabilized in the neutral pH environment of the endoplasmic reticulum, rendering it prone to endoplasmic reticulum associated degradation
L444P
-
a transport block in the endoplasmic reticulum of the enzyme with the mutation L444P
L444P
-
mutation results in enzyme with low folding efficacy
L444P
-
mutation present in humans with Gaucher disease
L444P
-
mutation isolated from patient with Gaucher disease. Examination of the frequency of L444P mutation in patients with Parkinson's disease and patients with demetia with Lewis bodies
L444P
-
isofagomine enhances mutant enzyme activity in pre-treated N370S/N370S and F213L/L444P patient fibroblasts with Gaucher disease
L444P
-
mutation responsible for Gaucher disease in 42% of patients tested
L444P
-
the GBA mutation is associated with severe Lewy body disorder
L444P
-
the mutant shows about 3% activity compared to the wild type enzyme
L444P
-
lacidipine is found to rescue the activity of glucocerebrosidase variants carrying the two most common mutations, L444P and N370S, in Gaucher disease patient-derived fibroblasts. Treatment of patient-derived fibroblasts with lacidipine leads to rescue of folding, lysosomal trafficking, and activity of mutated glucocerebrosidase variants
L444P/V460V
-
the activity is significantly reduced
N188S
-
the mutant shows about 55% activity compared to the wild type enzyme
N188S/E326K
-
the mutant shows about 10% activity compared to the wild type enzyme
N370S
-
-
N370S
-
abnormal catalytic site
N370S
-
Gaucher disease type I mutation
N370S
-
32.1% activity in comparison to wild-type enzyme, the mutation is used as control
N370S
-
the activity is significantly reduced
N370S
-
point mutation can cause Gaucher disease, mutant is destabilized in the neutral pH environment of the endoplasmic reticulum, rendering it prone to endoplasmic reticulum associated degradation
N370S
-
in Gaucher cell homozygous for this mutation the activity, measured in presence of taurocholate and Triton X-100 as activators is approximately 10% of the normal value. When activated by a mixture of saposin C and large unilamellar vesicles composed of anionic phospholipids such as phosphatidylserine and cholesterol, the activity reaches 50-70% of the control value. The mutation affects the capacity of glucosylceramidase to interact with anionic phospholipid-containing membranes and saposin C
N370S
-
retarded transport of glucocerebrosidase carrying the mutation
N370S
-
increased activity
N370S
-
Gaucher disease-causing mutation
N370S
-
decreased activity
N370S
-
mutation isolated from patient with Gaucher disease. Examination of the frequency of N370S mutation in patients with Parkinson's disease and patients with demetia with Lewis bodies
N370S
-
isofagomine enhances mutant enzyme activity in pre-treated N370S/N370S and F213L/L444P patient fibroblasts with Gaucher disease
N370S
-
inhibitors 5-((4-methylphenyl)thio)-quinazoline 2,4-diamine and 5-(3,5-dichlorophenoxy)-N-(4-pyridinyl)-2-furamide raise the levels of functional GCase 1.5-2.5-fold in N370S or F213I Gaucher disease fibroblasts. Treated fibroblasts from patients with Gaucher disease show decreased levels of enzyme in their endoplasmic reticulum and increased levels in lysosomes. Compound stabilizes a domain III active-site loop
N370S
-
mutation responsible for Gaucher disease in 30% of patients tested
N370S
-
the GBA mutation is associated with mild Lewy body disorder
N370S
-
the mutant shows about 7% activity compared to the wild type enzyme
N370S
-
lacidipine is found to rescue the activity of glucocerebrosidase variants carrying the two most common mutations, L444P and N370S, in Gaucher disease patient-derived fibroblasts. Treatment of patient-derived fibroblasts with lacidipine leads to rescue of folding, lysosomal trafficking, and activity of mutated glucocerebrosidase variants
N370S
-
mean activity of mutant compared to wild-type: 17.7%
N370Sr
-
mutation results in a protein that is largely properly folded and stable but with low specific activity at pH values greater than 5
N396T
P04062
Gaucher disease mutation, less active
N396T
-
mutation causing Gaucher disease, mutation stabilizes closed conformation and destabilizes open conformation of the enzyme, thus limiting substrate access to the active site
N409S
-
the mutation is associated with Parkinsons disease
P171P
-
the GBA mutation is associated with Lewy body disorder
P266L
-
28.5% activity in comparison to wild-type enzyme, a natural occurring mutation in a patient with Gaucher disease
P415R
-
Gaucher disease mutation, reduced amounts of protein in cells
P415R
P04062
-
Q497R
-
mutation present in humans with Gaucher disease
R120Q
-
Gaucher disease type I mutation, inactive
R170C
-
the mutation is associated with Parkinsons disease
R296Q
-
the mutation is associated with Parkinsons disease
R359Q
P04062
Gaucher disease mutation, less active
R395P
P04062
Gaucher disease mutation, less active
R395P
-
mutation causing Gaucher disease, destabilizes the open conformation of the enzyme due to the loss of a stabilizing salt bridge with Glu388, thus limiting substrate access to the active site
R463C
-
Gaucher disease type I mutation, less active with saposin C
R463C
-
the GBA mutation is associated with severe Lewy body disorder
R496H
-
the GBA mutation is associated with mild Lewy body disorder
R502C
-
the mutation is associated with Parkinsons disease
S196P
-
the activity is significantly reduced
S356F
-
mutation associated with the severe phenotype of type 1 Gaucher disease
S364R
-
42.7% activity in comparison to wild-type enzyme, a natural occurring mutation in a patient with Gaucher disease
S465del
-
5.5% activity in comparison to wild-type enzyme, a natural occurring mutation in a patient with Gaucher disease
T369M
-
the activity is significantly reduced
T369M
-
the GBA mutation is associated with Lewy body disorder
T43K
-
decreased activity on glucosylceramides
V15M
-
22.8% activity in comparison to wild-type enzyme, a natural occurring mutation in a patient with Gaucher disease
V394L
-
mutation causing Gaucher disease, mutation stabilizes closed conformation and destabilizes open conformation of the enzyme, thus limiting substrate access to the active site
V394L/V394L
-
8% of wild type activity
V497L
-
the mutation is associated with Parkinsons disease
W184R
P04062
Gaucher disease mutation, less active
W184R
-
the GBA mutation is associated with Lewy body disorder
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
D223E
-
mutation decreases the activity
D223G
-
the mutation reduces the activity, but can be partially restored by addition of formate
D223N
-
mutation completely abolishes the activity
E411A
-
the mutation reduces the activity, but can be partially restored by addition of azide
M123T
-
34.3% activity in comparison to wild-type enzyme, a natural occurring mutation in a patient with Gaucher disease
additional information
-
more than 200 natural occurring mutations are identified in patients with Gaucher disease
additional information
-
mutations in the glucocerebrosidase are contributory to Parkinson disease in Ashkenazi Jews. The majoriry of glucocerebrosidase mutation carriers who do not develop Parkinson disease are equipped with an efficient genetic mechanism that either prevents the deposition of glucocerebroside or adequately degrades deposited glucocerebroside or excessive alpha-synuclein
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
the measurement of ABG activities in dry blood spots using a tandem mass spectrometry is suitable for high-throughput analysis of at-risk individuals and potentially for newborn screening for Gaucher disease
medicine
-
-
medicine
-
enzyme replacement therapy
medicine
-
Gaucher disease, sphingolipoidose
medicine
-
mutations in the gene that incodes enzyme cause the Gaucher disease
medicine
-
more than 150 enzyme gene mutations are described in Gaucher patients
medicine
-
in fibroblasts of patients with Niemann-Pick disease type C, the cholesterol storage affects the stability of enzyme, decreasing its mass and activity
medicine
-
the enzyme gene mutations are encounterd in individuals with parkinsonism
medicine
-
an inherited deficiency in this enzyme leads to the onset of Gaucher disease
medicine
-
manipulating the endoplasmic reticulum environment with chemical chaperones can correct the instability of mutant enzyme (causing Gaucher disease)
medicine
-
lentivirus-mediated gene transfer results in high-level glucocerebrosidase expression in multiple tissues without any evidence of local or systemic toxicity. Lentivirus-mediated gene transfer may respresent an effective method of achieving widespread and persistent therapeutic benefit for the treatment of patients with Gaucher disease
medicine
-
enzyme activity is decreased in psoriatic skin compared to normal control, increased in lesional compared to non-lesional psoriatic skin. Alterations in water permeability barrier in lesional psoriatic skin can serve as a trigger for the upregulation of the expression of enzymes like glycosylceramide-beta-glucosidase with consequent stimulation of ceramide generation
medicine
-
recombinant human acid beta-glucosidase stored in tobacco seed is stable, active and taken up by human fibroblasts. The recombinant enzyme can be used for enzyme replacement therapy
medicine
-
glucocerebrosidase mutations exert a large effect on susceptibility for Lewis body disorders at the individual level but are associated with a modest population-attributable risk in individuals of European ancestry
medicine
-
isofagomine enhances mutant enzyme activity in pre-treated N370S/N370S and F213L/L444P patient fibroblasts with Gaucher disease
medicine
-
inhibitors 5-((4-methylphenyl)thio)-quinazoline 2,4-diamine and 5-(3,5-dichlorophenoxy)-N-(4-pyridinyl)-2-furamide raise the levels of functional GCase 1.52.5-fold in N370S or F213I Gaucher disease fibroblasts. Treated fibroblasts from patients with Gaucher disease show decreased levels of enzyme in their endoplasmic reticulum and increased levels in lysosomes. Compound stabilizes a domain III active-site loop
medicine
-
mutations N370S and L444P are the most prevalent among patients with Gaucher disease. Two missense changes S356F, L296V are associated with the severe phenotype of type 1 Gaucher disease. Mutation 303e305delCAC was identified in a homozygous state in one patient type 1 or type 3
medicine
-
study on children with type 3 Gaucher disease who had received enzyme replacement therapy or a bone marrow transplant. 60% of subjects have intelectual skills below average with significant discrepancies between verbal and performance IQ. No correlation between intelligence measures and genotype or the extent of systemic involvement. The dosage, age at initiation, and the length of enzyme replacement therapy had no significant effect on IQ scores
medicine
-
determination of the activity of alpha-mannosidase, beta-mannosidase, beta-glucocerebrosidase, beta-galactosidase and beta-hexosaminidase in cerebrospinal fluid of patients suffering from dementia with Lewis bodies, Alzheimer's disease, fronto-temporal dementia and controls. beta-Glucocerebrosidase activity is selectively reduced in dementia with Lewis bodies, further suggesting that this enzyme might specifically be impaired in synucleinopathies
medicine
-
GBA mutations are associated with pathologically purer Lewy body disorders, characterized by more extensive (cortical) Lewy body, and less severe Alzheimer disease pathological findings and are a useful marker for Lewy body disorders
medicine
-
imiglucerase is used in enzyme replacement therapy for Gaucher disease
medicine
-
GBA mutations represent a significant risk factor for the development of Parkinsons disease
medicine
-
measurement of lysosomal glucocerebrosidase activity in mouse liver using a fluorescence-activated cell sorter assay. This assay should be applicable to investigation of other Gaucher disease treatments in both human and animal models
medicine
-
Gaucher disease mouse models