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Information on EC 3.2.1.52 - beta-N-acetylhexosaminidase and Organism(s) Homo sapiens

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EC Tree
IUBMB Comments
Acts on N-acetylglucosides and N-acetylgalactosides.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
beta-hexosaminidase, hexosaminidase, n-acetyl-beta-glucosaminidase, o-glcnacase, hex a, n-acetylglucosaminidase, hexosaminidase a, beta-n-acetylhexosaminidase, hex b, beta-hexosaminidase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-acetamido-2-deoxy-beta-D-glucoside acetamidodeoxyglucohydrolase
-
-
-
-
65 kDa epididymal boar protein
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-
-
-
beta-acetylaminodeoxyhexosidase
-
-
-
-
beta-acetylhexosaminidase
-
-
-
-
beta-acetylhexosaminidinase
-
-
-
-
beta-D-hexosaminidase
-
-
-
-
beta-D-N-acetylhexosaminidase
-
-
-
-
Beta-GlcNAcase
-
-
-
-
beta-hexosaminidase
beta-hexosaminidase A
beta-hexosaminidase B
-
beta-N-acetyl-D-hexosaminidase
-
-
-
-
beta-N-acetyl-hexosaminidase
-
-
-
-
beta-N-acetylgalactosaminidase
-
-
-
-
beta-N-acetylglucosaminidase
Beta-N-acetylhexosaminidase
-
-
-
-
beta-N-acetylhexosaminidase A
-
-
beta-N-acetylhexosaminidase B
-
-
beta-Nacetylhexosaminidase S
-
-
beta-NAHA
-
-
-
-
Beta-NAHASE
-
-
-
-
chitobiase
-
-
-
-
Hex B
HexB
-
-
HexD
-
-
hexosaminidase
-
-
-
-
hexosaminidase A
-
-
-
-
hexosaminidase D
-
-
hHexA
-
-
lysosomal beta-hexosaminidase
-
-
N-acetyl-beta-D-hexosaminidase
N-acetyl-beta-glucosaminidase
-
-
-
-
N-acetyl-beta-hexosaminidase
N-acetylhexosaminidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
O-glycosyl bond hydrolysis
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-N-acetyl-D-hexosaminide N-acetylhexosaminohydrolase
Acts on N-acetylglucosides and N-acetylgalactosides.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-33-3
c.f. EC 3.2.1.165
9027-52-5
deleted
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3,3-dichlorophenylsulfonphthaleinyl-N-acetyl-beta-D-glucosaminide + H2O
?
show the reaction diagram
-
-
-
-
?
3-fluoro-4-nitrophenyl N-acetyl-beta-D-galactosaminide + H2O
3-fluoro-4-nitrophenol + N-acetyl-beta-D-galactosamine
show the reaction diagram
-
-
-
-
?
3-fluoro-4-nitrophenyl N-acetyl-beta-D-glucosaminide + H2O
3-fluoro-4-nitrophenol + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
-
?
4-methylcoumar-7-yl-beta-N-acetyl-D-glucosamine + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylcoumar-7-yl-beta-N-fluoroacetyl-D-glucosamine + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl 2-acetamido-2-deoxy-beta-D-glucopyranoside 6-sulfate + H2O
4-methylumbelliferone + 2-acetamido-2-deoxy-beta-D-glucopyranoside 6-sulfate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl beta-N-acetylgalactosaminide + H2O
4-methylumbelliferone + beta-N-acetylgalactosamine
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl beta-N-acetylglucosamine + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl N-acetyl-beta-D-glucosaminide + H2O
4-methylumbelliferone + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-galactopyranoside + H2O
4-methylumbelliferone + 2-acetamido-2-deoxy-beta-D-galactopyranoside
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside + H2O
4-methylumbelliferone + 2-acetamido-2-deoxy-beta-D-glucopyranoside
show the reaction diagram
4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside 6-sulfate + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside-6-sulfate + H2O
4-methylumbelliferone + 2-acetamido-2-deoxy-beta-D-glucopyranoside-6-sulfate
show the reaction diagram
4-methylumbelliferyl-6-sulfo-N-acetyl-beta-D-glucosaminide + H2O
?
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-beta-N-acetylglucosamine + H2O
4-methylumbelliferol + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-N-acetylglucosamine + H2O
4-methylumbelliferone + beta-N-acetylglucosamine
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-N-acetylglucosamine-6-sulfate + H2O
4-methylumbelliferol + N-acetyl-D-glucosamine-6-sulfate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide + H2O
4-methylumbelliferone + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
?
4-nitrophenyl 2-deoxy-2-difluoroacetamido-beta-D-galactopyranoside + H2O
4-nitrophenol + 2-deoxy-2-difluoroacetamido-beta-D-galactopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl 2-deoxy-2-fluoroacetamido-beta-D-galactopyranoside + H2O
4-nitrophenol + 2-deoxy-2-fluoroacetamido-beta-D-galactopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl 2-deoxy-2-trifluoroacetamido-beta-D-galactopyranoside + H2O
4-nitrophenol + 2-deoxy-2-trifluoroacetamido-beta-D-galactopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-N-acetyl-D-glucosaminide + H2O
4-nitrophenol + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
-
?
4-nitrophenyl N-acetyl-beta-D-galactosaminide + H2O
4-nitrophenol + N-acetyl-beta-D-galactosamine
show the reaction diagram
-
-
-
-
?
4-nitrophenyl N-acetyl-beta-D-glucosamine + H2O
4-nitrophenol + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
-
?
4-nitrophenyl N-acetyl-beta-D-glucosaminide + H2O
4-nitrophenol + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-2-acetamido-2-deoxy-beta-D-glucopyranoside + H2O
4-nitrophenol + N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
-
?
complex of GM2 activator protein and GM2 ganglioside + H2O
?
show the reaction diagram
-
-
-
-
?
ganglioside GM2 + H2O
ganglioside GM3 + N-acetyl-beta-D-galactosamine
show the reaction diagram
-
-
-
-
?
globotetraosylceramide + H2O
globotriaosylceramide + GalNAc
show the reaction diagram
-
-
-
?
GM2 ganglioside + H2O
?
show the reaction diagram
-
-
-
-
?
GM2 ganglioside + H2O
GM3 ganglioside + N-acetyl-beta-D-galactosamine
show the reaction diagram
N-acetyl-beta-D-hexosaminides + H2O
N-acetyl-D-hexosamines
show the reaction diagram
N-acetyl-galactosaminide-hexasaccharide + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-2-acetamido-2-deoxy-D-galactopyranoside + H2O
2-acetamido-2-deoxy-D-galactose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-2-acetamido-2-deoxy-D-glucopyranoside + H2O
2-acetamido-2-deoxy-D-glucose + p-nitrophenol
show the reaction diagram
p-nitrophenyl-GlcNAc + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
ganglioside GM2 + H2O
ganglioside GM3 + N-acetyl-beta-D-galactosamine
show the reaction diagram
-
-
-
-
?
N-acetyl-beta-D-hexosaminides + H2O
N-acetyl-D-hexosamines
show the reaction diagram
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1E)-2-nitro-1H-indene-1,3(2H)-dione oxime
-
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(1Z)-2-nitro-1H-indene-1,3(2H)-dione oxime
-
-
(2E)-3-(3,4-dihydroisoquinolin-2(1H)-yl)-2-(2-thienylcarbonyl)acrylonitrile
-
-
(3E)-1-methyl-3-([[3-(trifluoromethyl)phenyl]amino]methylene)-1H-thieno[3,2-c][1,2]thiazin-4(3H)-one 2,2-dioxide
-
-
1,1'-(1,3-dioxo-2-phenylpropane-1,3-diyl)bis(2,3-dihydro-1H-indole)
-
-
1,2-dideoxy-2'-butyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
-
1,2-dideoxy-2'-ethyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
-
1,2-dideoxy-2'-isobutyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
-
1,2-dideoxy-2'-isopropyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
-
1,2-dideoxy-2'-methyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
an inhibitor that mimics the oxazoline intermediate proposed in the catalytic mechanism of family 20 glycoside hydrolases, is shown to act as a potent competitive inhibitor. About 17000fold more tightly than GlcNAc
1,2-dideoxy-2'-pentyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
-
1,2-dideoxy-2'-propyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
-
1-acetamido-2-deoxy-D-glucono-1,5-lactone
-
-
1-[2-(1H-benzimidazol-2-yl)phenyl]-3-[4-(benzyloxy)phenyl]urea
-
-
1-[5-acetyl-2-[4-(ethoxycarbonyl)piperidin-1-yl]phenyl]-1-methyldiazenium
-
-
2,2''-[azanediyldi(ethane-2,1-diyl)]di(1H-benzo[de]isoquinoline-1,3(2H)-dione)
-
M-31850
2,2'-(iminodiethane-2,1-diyl)bis(1H-benzo[de]isoquinoline-1,3(2H)-dione)
-
-
2-(2-([(4-methoxyphenyl)methyl]amino)ethyl)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-(2-([(5-methyl-1,3,4-thiadiazol-2-yl)methyl]amino)ethyl)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-(2-hydroxypropyl)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-(2-pyridin-2-ylethyl)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-(4-chlorobenzyl)-5-methyl-2,6-dihydro-1H-pyrrolo[3,4-d]pyridazin-1-one
-
-
2-(tetrahydrofuran-2-ylmethyl)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-acetamido-1,2,4-trideoxy-1,4-imino-L-arabinitol
-
potent noncompetitive inhibitor
2-acetamido-1,2,5-trideoxy-1,5-imino-D-glucitol
-
-
2-acetamido-1,2-dideoxy-1,5-imino-D-glucitol
-
competitive inhibitor
2-acetamido-2-deoxy-N-([4-[(2,4-dichlorobenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-beta-D-glucopyranosylamine
-
7.0% inhibition at 0.1 mM
2-acetamido-2-deoxy-N-([4-[(2,6-dichlorobenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-beta-D-glucopyranosylamine
-
2.7% inhibition at 0.1 mM
2-acetamido-2-deoxy-N-([4-[(2-fluorobenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-beta-D-glucopyranosylamine
-
2.4% inhibition at 0.1 mM
2-acetamido-2-deoxy-N-([4-[(2-hydroxybenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-beta-D-glucopyranosylamine
-
0.9% inhibition at 0.1 mM
2-acetamido-2-deoxy-N-([4-[(2-methoxybenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-alpha-D-glucopyranosylamine
-
19.5% inhibition at 0.1 mM
2-acetamido-2-deoxy-N-([4-[(2-nitrobenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-beta-D-glucopyranosylamine
-
13.9% inhibition at 0.1 mM
2-acetamido-2-deoxy-N-([4-[(3-fluorobenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-beta-D-glucopyranosylamine
-
3.3% inhibition at 0.1 mM
2-acetamido-2-deoxy-N-([4-[(3-hydroxybenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-beta-D-glucopyranosylamine
-
3.1% inhibition at 0.1 mM
2-acetamido-2-deoxy-N-([4-[(3-methoxybenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-beta-D-glucopyranosylamine
-
18.2% inhibition at 0.1 mM
2-acetamido-2-deoxy-N-([4-[(3-nitrobenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-beta-D-glucopyranosylamine
-
10.2% inhibition at 0.1 mM
2-acetamido-2-deoxy-N-([4-[(4-fluorobenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-beta-D-glucopyranosylamine
-
8.0% inhibition at 0.1 mM
2-acetamido-2-deoxy-N-([4-[(4-methoxybenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-beta-D-glucopyranosylamine
-
6.9% inhibition at 0.1 mM
2-acetamido-2-deoxy-N-([4-[(4-nitrobenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-beta-D-glucopyranosylamine
-
16.2% inhibition at 0.1 mM
2-acetamido-2-deoxy-N-[(4-[[2-(trifluoromethyl)benzamido]methyl]-1H-1,2,3-triazol-1-yl)acetyl]-beta-D-glucopyranosylamine
-
11.1% inhibition at 0.1 mM
2-acetamido-N-([4-[(2-amino-3-methylbenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-2-deoxy-beta-D-glucopyranosylamine
-
17.8% inhibition at 0.1 mM
2-acetamido-N-([4-[(2-aminobenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-2-deoxy-beta-D-glucopyranosylamine
-
5.1% inhibition at 0.1 mM
2-acetamido-N-([4-[(2-chlorobenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-2-deoxy-beta-D-glucopyranosylamine
-
3.8% inhibition at 0.1 mM
2-acetamido-N-([4-[(3-aminobenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-2-deoxy-beta-D-glucopyranosylamine
-
10.9% inhibition at 0.1 mM
2-acetamido-N-([4-[(3-chlorobenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-2-deoxy-beta-D-glucopyranosylamine
-
13.8% inhibition at 0.1 mM
2-acetamido-N-([4-[(4-aminobenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-2-deoxy-beta-D-glucopyranosylamine
-
13.5% inhibition at 0.1 mM
2-acetamido-N-([4-[(4-chlorobenzamido)methyl]-1H-1,2,3-triazol-1-yl]acetyl)-2-deoxy-beta-D-glucopyranosylamine
-
23% inhibition at 0.1 mM
2-acetamido-N-[(4-[[([1,1'-biphenyl]-2-carbonyl)amino]methyl]-1H-1,2,3-triazol-1-yl)acetyl]-2-deoxy-beta-D-glucopyranosylamine
-
28.5% inhibition at 0.1 mM
2-acetamido-N-[(4-[[([1,1'-biphenyl]-3-carbonyl)amino]methyl]-1H-1,2,3-triazol-1-yl)acetyl]-2-deoxy-beta-D-glucopyranosylamine
-
6.6% inhibition at 0.1 mM
2-acetamido-N-[(4-[[([1,1'-biphenyl]-4-carbonyl)amino]methyl]-1H-1,2,3-triazol-1-yl)acetyl]-2-deoxy-beta-D-glucopyranosylamine
-
26.2% inhibition at 0.1 mM
2-acetamido-N-[(4-[[4-chloro-2-(propan-2-yl)benzamido]methyl]-1H-1,2,3-triazol-1-yl)acetyl]-2-deoxy-beta-D-glucopyranosylamine
-
9.2% inhibition at 0.1 mM
2-amino-4-ethyl-5-(4-(trifluoromethyl)phenyl)pyrimidine
-
-
2-amino-4-ethyl-5-(4-chlorophenyl)pyrimidine
-
-
2-amino-6-(methoxymethyl)pyrimidin-4-ol
-
-
2-amino-6-ethyl-5-(4-chlorophenyl)pyrimidin-4(3H)-one
-
-
2-hydroxy-3-phenyl-4H-pyrimido[2,1-b][1,3]benzothiazol-4-one
-
-
2-[(2-acetamido-2-deoxy-beta-D-glucopyranosyl)thio]-N-(81-[5-(1,3-dioxo-1H-benzo[de]isoquinolin-2(3H)-yl)pentyl]-1H-1,2,3-triazol-4-yl]methyl)acetamide
-
49.1% inhibition at 0.1 mM
2-[(2-acetamido-2-deoxy-beta-D-glucopyranosyl)thio]-N-([1-[3-(1,3-dioxo-1H-benzo[de]isoquinolin-2(3H)-yl)propyl]-1H-1,2,3-triazol-4-yl]methyl)acetamide
-
48.7% inhibition at 0.1 mM
2-[(2-acetamido-2-deoxy-beta-D-glucopyranosyl)thio]-N-([1-[4-(1,3-dioxo-1H-benzo[de]isoquinolin-2(3H)-yl)butyl]-1H-1,2,3-triazol-4-yl]methyl)acetamide
-
42.9% inhibition at 0.1 mM
2-[2-[(2-acetamido-beta-D-glucopyranosyl)thio]ethyl]-1H-benzo[de]isoquinoline-isoquinoline-1,3(2H)-dione
-
-
2-[2-[2-[(2-acetamido-beta-D-glucopyranosyl)thio]ethylamino]ethyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[2-[3-[(2-acetamido-beta-D-glucopyranosyl)thio]propylamino]ethyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[2-[5-[(2-acetamido-beta-D-glucopyranosyl)thio]pentylamino]ethyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[2-[6-[(2-acetamido-beta-D-glucopyranosyl)thio]hexylamino]ethyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[3-[(2-acetamido-beta-D-glucopyranosyl)thio]propyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[3-[2-[(2-acetamido-beta-D-glucopyranosyl)thio]ethylamino]propyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[3-[3-[(2-acetamido-beta-D-glucopyranosyl)thio]propylamino]propyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[3-[5-[(2-acetamido-beta-D-glucopyranosyl)thio]pentylamino]propyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[3-[6-[(2-acetamido-beta-D-glucopyranosyl)thio]hexylamino]propyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[4-[(2-acetamido-beta-D-glucopyranosyl)thio]butyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[4-[2-[(2-acetamido-beta-D-glucopyranosyl)thio]ethylamino]butyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[4-[3-[(2-acetamido-beta-D-glucopyranosyl)thio]propylamino]butyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[4-[5-[(2-acetamido-beta-D-glucopyranosyl)thio]pentylamino]butyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[4-[6-[(2-acetamido-beta-D-glucopyranosyl)thio]hexylamino]butyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[5-[(2-acetamido-beta-D-glucopyranosyl)thio]pentyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-[6-[(2-acetamido-beta-D-glucopyranosyl)thio]hexyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
3,5-bis(4-fluorophenyl)-1-phenyl-4,5-dihydro-1H-pyrazole
-
-
3-methoxy-1-(3,4,5-trimethoxyphenyl)-9,10-dihydrophenanthrene-2-carbonitrile
-
-
3-[2-(benzyloxy)-5-fluorophenyl]-5-(4-tert-butylphenyl)-1-(2,4-dichlorophenyl)-4,5-dihydro-1H-pyrazole
-
-
4,5-dihydronaphtho[1,2-b]thiophene-2-carbohydrazide
-
-
4-ethyl-5-[4-(trifluoromethyl)phenyl]pyrimidine
-
-
4-hydroxy-3-(methylthio)-N'-[(1E)-2-thienylmethylene]-4,5,6,7-tetrahydro-2-benzothiophene-1-carbohydrazide
-
-
4-[(E)-2-phenylvinyl]benzaldehyde O-(anilinocarbonyl)oxime
-
-
4-[4-(phenylethynyl)phenyl]-N-[4-(trifluoromethoxy)phenyl]butanamide
-
-
5-(3,5-dimethylphenyl)-6-ethylpyrimidine-2,4-diamine
-
-
5-(3-nitrophenyl)-2-furaldehyde N-(3-fluorophenyl)thiosemicarbazone
-
-
5-(4-chloro-1-methyl-1H-pyrazol-3-yl)-4,5-dihydro-1,3,4-thiadiazole-2-thiol
-
-
5-(4-chlorophenyl)-6-butylpyrimidine-2,4-diamine
-
-
5-(4-chlorophenyl)-6-ethylpyrimidine-2,4-diamine
-
-
5-(4-chlorophenyl)-6-isopropylpyrimidine-2,4-diamine
-
-
5-(4-chlorophenyl)-6-methylpyrimidine-2,4-diamine
-
-
5-(4-chlorophenyl)-6-propylpyrimidine-2,4-diamine
-
-
6-(aminomethyl)-5-(4-chlorophenyl)pyrimidine-2,4-diamine
-
-
6-ethyl-5-(4-(trifluoromethyl)phenyl)pyrimidine-2,4-diamine
-
-
6-ethyl-5-(4-methoxyphenyl)pyrimidine-2,4-diamine
-
-
6-ethyl-5-(m-tolyl)pyrimidine-2,4-diamine
-
-
6-ethyl-5-(o-tolyl)pyrimidine-2,4-diamine
-
-
6-ethyl-5-(p-tolyl)pyrimidine-2,4-diamine
-
-
6-ethyl-5-phenylpyrimidine-2,4-diamine
-
-
acetate
Ag+
-
enzyme incubated before addition of substrate: with 0.0025 mM 18% of activity remains
allyl ((1-(2-((2-acetamido-2-deoxy-beta-D-glucopyrano-syl)amino)-2-oxoethyl)-1H-1,2,3-triazol-4-yl)methyl)carbamate
-
16.4% inhibition at 0.1 mM
ascorbate
-
only in presence of Cu2+
Cu2+
-
only in presence of ascorbate
elinafide
-
-
ethyl 3-(N-[[(4-chlorophenyl)amino]carbonyl]-S-methylsulfinimidoyl)-6,7-dihydro-2-benzothiophene-1-carboxylate
-
-
ethyl 5-[[3-(trifluoromethyl)phenyl]amino]pyrazolo[1,5-a]quinazoline-3-carboxylate
-
-
Fe2+
-
with 0.2 mM 28% of activity remains, citrate buffer, not inhibitory in succinate or acetate buffer
Gal-NAG-thiazoline
-
-
galactosamine
-
with 30 mM 84.3-89.3% of liver enzyme type A and 79.6-87.8% of liver enzyme type B remains
GalNAc-isofagomine
-
GlcNAc
-
-
glucosamine
-
with 30 mM 72.2-76.3% of liver enzyme type A and 65.7-73.3% of liver enzyme type B remains
iminocyclitol
-
-
N-((1-(2-((2-acetamido-2-deoxy-beta-D-glucopyranosyl)amino)-2-oxoethyl)-1H-1,2,3-triazol-4-yl)methyl)benzamide
-
13.1% inhibition at 0.1 mM
N-((1-(2-((2-acetamido-2-deoxy-beta-D-glucopyranosyl)amino)-2-oxoethyl)-1H-1,2,3-triazol-4-yl)methyl)picolinamide
-
6.6% inhibition at 0.1 mM
N-((3S,4R,5S)-1-(7-(bis(4-methoxybenzyl)amino)heptyl)-4,5-dihydroxy-5-(hydroxymethyl)piperidin-3-yl)acetamide
-
-
N-((3S,4R,5S)-4,5-dihydroxy-5-(hydroxymethyl)-1-(7-(4-methoxybenzylamino)heptyl)piperidin-3-yl)acetamide
-
-
N-(3,5-dichlorophenyl)-2-[[4-(3,4-dimethylthieno[2,3-b]thien-2-yl)pyrimidin-2-yl]thio]acetamide
-
-
N-(7-((3S,4R,5S)-5-acetamido-3,4-dihydroxy-3-(hydroxymethyl)piperidin-1-yl)heptyl)-5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamide
-
-
N-acetyl-D-galactosamine
N-acetyl-D-glucosamine
N-acetylglucosamine thiazoline
-
-
N-benzyl-2-acetamido-1,2,4-trideoxy-1,4-imino-D-arabinitol
-
weak competitive inhibitor
N-benzyl-2-acetamido-1,2,4-trideoxy-1,4-imino-L-arabinitol
-
potent noncompetitive inhibitor, inhibits human placenta beta-N-acetylhexosaminidase 2.5fold better than DNJ-NAc 13
N-[(1S,2R,5R,6R)-2-amino-5,6-dihydroxy-4-(hydroxymethyl)-cyclohex-3-en-1-yl]acetamide hydrochloride
-
1-acetamido derivative of 6-epi-valienamine, route enabling synthesis described
N-[1(7-amino-heptyl)]-2-acetamido-1,2,5-trideoxy-1,5-imino-D-glucitol
-
competitive inhibitor
N-[1(7-azido-heptyl)]-2-acetamido-1,2,5-trideoxy-1,5-imino-D-glucitol
-
-
N-[[1-[2-(1,3-dioxo-1H-benzo[de]isoquinolin-2(3H)-yl)ethyl]-1H-1,2,3-triazol-4-yl]methyl]-2-(2-acetamido-beta-D-glucopyranosylthio)acetamide
-
46.6% inhibition at 0.1 mM
NAG-thiazoline
-
-
nagstatin
-
-
naphthalene-1,4-diyl bis(trifluoroacetate)
-
-
naphthalimide
-
-
O-(2-acetamido-2-deoxy-D-glucopyranosylidene) amino-N-phenylcarbamate
-
PUGNAc
O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino N-phenylcarbamate
-
inhibitor of both human O-GlcNAcase and human beta-hexosaminidase
O-(2-deoxy-2-butamido-D-glucopyranosylidene)amino N-phenylcarbamate
-
inhibitor of both human O-GlcNAcase and human beta-hexosaminidase
O-(2-deoxy-2-hexamido-D-glucopyranosylidene)amino N-phenylcarbamate
-
inhibitor of both human O-GlcNAcase and human beta-hexosaminidase
O-(2-deoxy-2-isobutamido-D-glucopyranosylidene)amino N-phenylcarbamate
-
inhibitor of both human O-GlcNAcase and human beta-hexosaminidase
O-(2-deoxy-2-isovaleramido-D-glucopyranosylidene)amino N-phenylcarbamate
-
inhibitor of both human O-GlcNAcase and human beta-hexosaminidase
O-(2-deoxy-2-propamido-D-glucopyranosylidene)amino N-phenylcarbamate
-
inhibitor of both human O-GlcNAcase and human beta-hexosaminidase
O-(2-deoxy-2-valeramido-D-glucopyranosylidene)amino N-phenylcarbamate
-
inhibitor of both human O-GlcNAcase and human beta-hexosaminidase
p-chloromercuribenzoate
-
form A: 93% inhibition with 0.1 mM, form P: 98% inhibition with 0.1 mM
p-chloromercuriphenylsulfonate
-
with 1 mM 38.3% of liver enzyme type S, 14.2% of brain enzyme type S, 1.9-2.2% of liver enzyme type A and 2.6-9.9% of liver enzyme type B remains
PUGNAc
pyrimethamine
S-(thiophen-3-ylmethyl) (2,2'-bithiophen-5-ylcarbonyl)thiocarbamate
-
-
thioguanine
-
-
TMG-chitotriomycin
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bovine serum albumin
-
-
-
cysteine
D-galactosamine
-
with 30 mM the activity of liver and brain enzymes reaches 135% and 114.3%
D-glucosamine
-
with 30 mM the activity of liver and brain enzymes reaches 135% and 110.7%
GM12 activator protein
-
-
-
Human serum albumin
-
-
-
N-benzyl-2-acetamido-1,2,4-trideoxy-1,4-imino-L-arabinitol
-
enhancement of beta-N-acetylhexosaminidase B activity at higher concentrations of inhibitor, whereas beta-N-acetylhexosaminidase A and/or beta-N-acetylhexosaminidase S activity are increased at much lower concentrations
taurocholate
-
concentrations of 0.05 M and 0.1 M cause 140% and 160% of activity
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.172 - 1.73
3-fluoro-4-nitrophenyl N-acetyl-beta-D-galactosaminide
0.852
3-fluoro-4-nitrophenyl N-acetyl-beta-D-glucosaminide
-
wild type enzyme, at pH 7.4 and 37°C
0.88
4-methylcoumar-7-yl-beta-N-acetyl-D-glucosamine
-
-
3.8
4-methylcoumar-7-yl-beta-N-fluoroacetyl-D-glucosamine
-
-
0.3 - 0.4
4-methylumbelliferyl beta-N-acetylgalactosaminide
-
liver and brain enzymes type S
0.108
4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-galactopyranoside
-
-
0.55 - 1
4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside
1.8
4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside-6-sulfate
-
-
0.8 - 0.9
4-methylumbelliferyl-beta-N-acetylglucosaminide
-
liver and brain enzymes type S
0.102
4-nitrophenyl 2-deoxy-2-difluoroacetamido-beta-D-galactopyranoside
-
wild type enzyme, at pH 7.4 and 37°C
0.533
4-nitrophenyl 2-deoxy-2-fluoroacetamido-beta-D-galactopyranoside
-
wild type enzyme, at pH 7.4 and 37°C
0.103
4-nitrophenyl 2-deoxy-2-trifluoroacetamido-beta-D-galactopyranoside
-
wild type enzyme, at pH 7.4 and 37°C
0.0525 - 0.196
4-nitrophenyl N-acetyl-beta-D-galactosaminide
0.607
4-nitrophenyl N-acetyl-beta-D-glucosaminide
-
wild type enzyme, at pH 7.4 and 37°C
0.046 - 0.12
complex of GM2 activator protein and GM2 ganglioside
-
0.17
p-nitrophenyl-beta-2-acetamido-2-deoxy-D-galactopyranoside
-
-
0.83
p-nitrophenyl-beta-2-acetamido-2-deoxy-D-glucopyranoside
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0048 - 2.9333
3-fluoro-4-nitrophenyl N-acetyl-beta-D-galactosaminide
1.54
3-fluoro-4-nitrophenyl N-acetyl-beta-D-glucosaminide
-
wild type enzyme, at pH 7.4 and 37°C
0.27
4-nitrophenyl 2-deoxy-2-difluoroacetamido-beta-D-galactopyranoside
-
wild type enzyme, at pH 7.4 and 37°C
2.6
4-nitrophenyl 2-deoxy-2-fluoroacetamido-beta-D-galactopyranoside
-
wild type enzyme, at pH 7.4 and 37°C
0.042
4-nitrophenyl 2-deoxy-2-trifluoroacetamido-beta-D-galactopyranoside
-
wild type enzyme, at pH 7.4 and 37°C
0.0515 - 1.4883
4-nitrophenyl N-acetyl-beta-D-galactosaminide
0.51
4-nitrophenyl N-acetyl-beta-D-glucosaminide
-
wild type enzyme, at pH 7.4 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0028 - 13.75
3-fluoro-4-nitrophenyl N-acetyl-beta-D-galactosaminide
1.817
3-fluoro-4-nitrophenyl N-acetyl-beta-D-glucosaminide
-
wild type enzyme, at pH 7.4 and 37°C
2.65
4-nitrophenyl 2-deoxy-2-difluoroacetamido-beta-D-galactopyranoside
-
wild type enzyme, at pH 7.4 and 37°C
4.98
4-nitrophenyl 2-deoxy-2-fluoroacetamido-beta-D-galactopyranoside
-
wild type enzyme, at pH 7.4 and 37°C
0.41
4-nitrophenyl 2-deoxy-2-trifluoroacetamido-beta-D-galactopyranoside
-
wild type enzyme, at pH 7.4 and 37°C
0.26 - 18.167
4-nitrophenyl N-acetyl-beta-D-galactosaminide
0.835
4-nitrophenyl N-acetyl-beta-D-glucosaminide
-
wild type enzyme, at pH 7.4 and 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0061
(1E)-2-nitro-1H-indene-1,3(2H)-dione oxime
-
-
4.6
1,2-dideoxy-2'-butyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
-
0.032
1,2-dideoxy-2'-ethyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
-
4
1,2-dideoxy-2'-isobutyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
-
0.72
1,2-dideoxy-2'-isopropyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
-
0.00007
1,2-dideoxy-2'-methyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
-
11
1,2-dideoxy-2'-pentyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
-
0.34
1,2-dideoxy-2'-propyl-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline
-
-
0.0008
2,2'-(iminodiethane-2,1-diyl)bis(1H-benzo[de]isoquinoline-1,3(2H)-dione)
-
-
0.015
2-acetamido-1,2,4-trideoxy-1,4-imino-L-arabinitol
-
-
0.00054
2-acetamido-1,2,5-trideoxy-1,5-imino-D-glucitol
-
pH 4.25, 30°C, isozyme Hex B
0.0095
2-acetamido-1,2-dideoxy-1,5-imino-D-glucitol
-
-
0.00091
2-[2-[6-[(2-acetamido-beta-D-glucopyranosyl)thio]hexylamino]ethyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
at pH 4.0 and 30°C
0.03042
2-[3-[2-[(2-acetamido-beta-D-glucopyranosyl)thio]ethylamino]propyl]-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
at pH 4.0 and 30°C
0.00042
Gal-NAG-thiazoline
-
wild type enzyme, at pH 7.4 and 37°C
1.2
GlcNAc
-
-
0.00000069
N-((3S,4R,5S)-1-(7-(bis(4-methoxybenzyl)amino)heptyl)-4,5-dihydroxy-5-(hydroxymethyl)piperidin-3-yl)acetamide
-
pH 4.25, 30°C, isozyme Hex B
0.0000012
N-((3S,4R,5S)-4,5-dihydroxy-5-(hydroxymethyl)-1-(7-(4-methoxybenzylamino)heptyl)piperidin-3-yl)acetamide
-
pH 4.25, 30°C, isozyme Hex B
0.0000267
N-(7-((3S,4R,5S)-5-acetamido-3,4-dihydroxy-3-(hydroxymethyl)piperidin-1-yl)heptyl)-5-(2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamide
-
pH 4.25, 30°C, isozyme Hex B
0.0061
N-acetylglucosamine thiazoline
-
-
0.18
N-benzyl-2-acetamido-1,2,4-trideoxy-1,4-imino-D-arabinitol
-
-
0.0037
N-benzyl-2-acetamido-1,2,4-trideoxy-1,4-imino-L-arabinitol
-
-
0.0062
N-[(1S,2R,5R,6R)-2-amino-5,6-dihydroxy-4-(hydroxymethyl)-cyclohex-3-en-1-yl]acetamide hydrochloride
-
substrate concentration 0.5 mM, two enzyme concentrations of 0.0406 and 0.012 micrograms per microliter
0.0000021
N-[1(7-amino-heptyl)]-2-acetamido-1,2,5-trideoxy-1,5-imino-D-glucitol
-
pH 4.25, 30°C, isozyme Hex B
0.0017
N-[1(7-azido-heptyl)]-2-acetamido-1,2,5-trideoxy-1,5-imino-D-glucitol
-
pH 4.25, 30°C, isozyme Hex B
0.000036
O-(2-acetamido-2-deoxy-D-glucopyranosylidene) amino-N-phenylcarbamate
-
-
0.000036
O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino N-phenylcarbamate
-
-
0.026
O-(2-deoxy-2-butamido-D-glucopyranosylidene)amino N-phenylcarbamate
-
-
0.02
O-(2-deoxy-2-isobutamido-D-glucopyranosylidene)amino N-phenylcarbamate
-
-
0.0012
O-(2-deoxy-2-propamido-D-glucopyranosylidene)amino N-phenylcarbamate
-
33fold increase in the KI value for beta-hexosaminidase as compared to the parent O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino N-phenylcarbamate
0.22
O-(2-deoxy-2-valeramido-D-glucopyranosylidene)amino N-phenylcarbamate
-
-
0.013
pyrimethamine
-
-
additional information
O-(2-deoxy-2-hexamido-D-glucopyranosylidene)amino N-phenylcarbamate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
27
(1E)-2-nitro-1H-indene-1,3(2H)-dione oxime
Homo sapiens
-
-
0.0018
(1Z)-2-nitro-1H-indene-1,3(2H)-dione oxime
Homo sapiens
-
-
0.042
(2E)-3-(3,4-dihydroisoquinolin-2(1H)-yl)-2-(2-thienylcarbonyl)acrylonitrile
Homo sapiens
-
-
0.27
(3E)-1-methyl-3-([[3-(trifluoromethyl)phenyl]amino]methylene)-1H-thieno[3,2-c][1,2]thiazin-4(3H)-one 2,2-dioxide
Homo sapiens
-
-
0.034
1,1'-(1,3-dioxo-2-phenylpropane-1,3-diyl)bis(2,3-dihydro-1H-indole)
Homo sapiens
-
-
0.012
1-[2-(1H-benzimidazol-2-yl)phenyl]-3-[4-(benzyloxy)phenyl]urea
Homo sapiens
-
-
0.065
1-[5-acetyl-2-[4-(ethoxycarbonyl)piperidin-1-yl]phenyl]-1-methyldiazenium
Homo sapiens
-
-
0.0002 - 6
2,2'-(iminodiethane-2,1-diyl)bis(1H-benzo[de]isoquinoline-1,3(2H)-dione)
0.031
2-(2-hydroxypropyl)-1H-benzo[de]isoquinoline-1,3(2H)-dione
Homo sapiens
-
-
0.108
2-(2-pyridin-2-ylethyl)-1H-benzo[de]isoquinoline-1,3(2H)-dione
Homo sapiens
-
-
0.0058 - 29
2-(4-chlorobenzyl)-5-methyl-2,6-dihydro-1H-pyrrolo[3,4-d]pyridazin-1-one
0.138
2-(tetrahydrofuran-2-ylmethyl)-1H-benzo[de]isoquinoline-1,3(2H)-dione
Homo sapiens
-
-
0.025 - 0.044
2-amino-6-(methoxymethyl)pyrimidin-4-ol
0.072
2-hydroxy-3-phenyl-4H-pyrimido[2,1-b][1,3]benzothiazol-4-one
Homo sapiens
-
-
0.0065
3,5-bis(4-fluorophenyl)-1-phenyl-4,5-dihydro-1H-pyrazole
Homo sapiens
-
-
0.035
3-methoxy-1-(3,4,5-trimethoxyphenyl)-9,10-dihydrophenanthrene-2-carbonitrile
Homo sapiens
-
-
0.162
3-[2-(benzyloxy)-5-fluorophenyl]-5-(4-tert-butylphenyl)-1-(2,4-dichlorophenyl)-4,5-dihydro-1H-pyrazole
Homo sapiens
-
-
0.024
4,5-dihydronaphtho[1,2-b]thiophene-2-carbohydrazide
Homo sapiens
-
-
0.03
4-hydroxy-3-(methylthio)-N'-[(1E)-2-thienylmethylene]-4,5,6,7-tetrahydro-2-benzothiophene-1-carbohydrazide
Homo sapiens
-
-
0.18
4-[(E)-2-phenylvinyl]benzaldehyde O-(anilinocarbonyl)oxime
Homo sapiens
-
-
0.071
4-[4-(phenylethynyl)phenyl]-N-[4-(trifluoromethoxy)phenyl]butanamide
Homo sapiens
-
-
0.042
5-(3-nitrophenyl)-2-furaldehyde N-(3-fluorophenyl)thiosemicarbazone
Homo sapiens
-
-
0.079
5-(4-chloro-1-methyl-1H-pyrazol-3-yl)-4,5-dihydro-1,3,4-thiadiazole-2-thiol
Homo sapiens
-
-
0.042
elinafide
Homo sapiens
-
-
0.039
ethyl 3-(N-[[(4-chlorophenyl)amino]carbonyl]-S-methylsulfinimidoyl)-6,7-dihydro-2-benzothiophene-1-carboxylate
Homo sapiens
-
-
0.045
ethyl 5-[[3-(trifluoromethyl)phenyl]amino]pyrazolo[1,5-a]quinazoline-3-carboxylate
Homo sapiens
-
-
0.02
N-(3,5-dichlorophenyl)-2-[[4-(3,4-dimethylthieno[2,3-b]thien-2-yl)pyrimidin-2-yl]thio]acetamide
Homo sapiens
-
-
0.093
naphthalene-1,4-diyl bis(trifluoroacetate)
Homo sapiens
-
-
0.0031 - 0.014
pyrimethamine
0.029
S-(thiophen-3-ylmethyl) (2,2'-bithiophen-5-ylcarbonyl)thiocarbamate
Homo sapiens
-
-
0.13
thioguanine
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0012 - 0.0025
-
substrate: 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside-6-sulfate
0.0024 - 0.01
-
light lysosomal fraction, I-cell
0.0032 - 0.008
-
light lysosomal fraction, normal
0.0033 - 0.0066
-
light lysosomal fraction, Pseudo-Hurler
0.0051 - 0.0079
-
heavy lysosomal fraction, I-cell
0.0061 - 0.0075
-
heavy lysosomal fraction, Pseudo-Hurler
0.0061 - 0.0211
-
heavy lysosomal fraction, normal
0.123
-
substrate: 4-methylumbelliferyl-beta-N-acetylglucosaminide, brain enzyme type S
0.16
recombinant enzyme, substrate: 4-methylumbelliferyl-6-sulfo-N-acetyl-beta-D-glucosaminide
0.28
recombinant enzyme, substrate: 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide
0.447
-
substrate: 4-methylumbelliferyl-beta-N-acetylglucosaminide, liver enzyme type S
130
-
hexosaminidase I2, substrate: 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside
150
-
hexosaminidase A, substrate: 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside
320
-
hexosaminidase B, substrate: 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside
77.84
-
substrate: 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside, normal enzyme
90.63
-
substrate: 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside, I-cell enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 4
-
substrate: 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside-6-sulfate
4.25
-
assay at
4.5 - 5
-
-
4.7
-
in a citrate-phosphate buffer
5
-
substrate: 4-methylumbelliferyl-beta-N-acetylglucosaminide or -acetylgalactosaminide, liver and brain enzymes type S
6.5 - 7
-
-
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 5.1
-
pH 3.5: about 45% of maximal activity, pH 5.1: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
elevated activity of N-acetyl-beta-hexosaminidase in subjects with asthma
Manually annotated by BRENDA team
-
about 2fold increase in N-acetyl-beta-D-hexosaminidase activity compared to normal adult retroauricular skin
Manually annotated by BRENDA team
-
fetal membrane
Manually annotated by BRENDA team
-
a similar pattern in activity of isoforms of isoenzymes A and B in normal and cancerous renal tissue is observed
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
desalinated
Manually annotated by BRENDA team
-
total activity of N-acetyl-beta-hexosaminidase (HEX), as well as HEX A and HEX B, in pleomorphic adenoma is significantly higher compared with normal human salivary gland
Manually annotated by BRENDA team
-
a similar pattern in activity of isoforms of isoenzymes A and B in normal and cancerous renal tissue is observed
Manually annotated by BRENDA team
-
no significant difference is found in total enzyme activity between normozoospermic controls and patients with secretory azoospermia. Ioenzyme A activity is significantly lower and the ratio between total enzyme activity and isoenzyme A activity is significantly higher in azoospermic patients compared to controls. This difference does not represent a useful marker of secretory azoospermia
Manually annotated by BRENDA team
-
normal adult retroauricular skin
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
Hex is linked to osteoarthritis and lysosomal storage disorders
physiological function
-
Hex is the predominant glycosidase released by chondrocytes to degrade glycosaminoglycan
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HEXB_HUMAN
556
1
63137
Swiss-Prot
Secretory Pathway (Reliability: 1)
HEXD_HUMAN
486
0
53790
Swiss-Prot
other Location (Reliability: 4)
HEXA_HUMAN
529
0
60703
Swiss-Prot
Secretory Pathway (Reliability: 2)
H3BP20_HUMAN
540
0
61999
TrEMBL
Secretory Pathway (Reliability: 2)
A0A804HLJ5_HUMAN
474
0
54351
TrEMBL
Secretory Pathway (Reliability: 2)
H3BS10_HUMAN
509
0
58440
TrEMBL
Secretory Pathway (Reliability: 2)
G3XL83_HUMAN
44
0
4959
TrEMBL
other Location (Reliability: 1)
H0Y9B6_HUMAN
202
0
23251
TrEMBL
other Location (Reliability: 3)
A0A0S2Z3U8_HUMAN
223
0
25310
TrEMBL
Secretory Pathway (Reliability: 2)
H0YA83_HUMAN
170
0
19523
TrEMBL
other Location (Reliability: 2)
G3XL82_HUMAN
58
0
6380
TrEMBL
other Location (Reliability: 2)
H3BTD4_HUMAN
373
0
42741
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0S2Z3L7_HUMAN
345
0
39679
TrEMBL
Secretory Pathway (Reliability: 2)
Q9BVJ8_HUMAN
409
0
47094
TrEMBL
other Location (Reliability: 3)
B4DVL8_HUMAN
301
0
34579
TrEMBL
other Location (Reliability: 2)
A0A804HJ97_HUMAN
257
0
29124
TrEMBL
Secretory Pathway (Reliability: 2)
A0A804HIU3_HUMAN
358
0
40909
TrEMBL
Secretory Pathway (Reliability: 2)
A0A804HIQ5_HUMAN
485
0
55663
TrEMBL
Secretory Pathway (Reliability: 2)
H3BU85_HUMAN
360
0
41169
TrEMBL
Secretory Pathway (Reliability: 2)
A0A804HKX5_HUMAN
473
0
54164
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0S2Z3W3_HUMAN
529
0
60703
TrEMBL
Secretory Pathway (Reliability: 2)
Q5URX0_HUMAN
331
0
38258
TrEMBL
other Location (Reliability: 2)
A0A0S2Z3M0_HUMAN
170
0
19459
TrEMBL
Secretory Pathway (Reliability: 2)
J3QKL0_HUMAN
544
0
58411
TrEMBL
other Location (Reliability: 4)
G3XL49_HUMAN
59
0
6444
TrEMBL
other Location (Reliability: 2)
B4DMX7_HUMAN
105
0
12072
TrEMBL
other Location (Reliability: 2)
A0A804HIC8_HUMAN
390
0
44687
TrEMBL
Secretory Pathway (Reliability: 2)
A0A024RAJ6_HUMAN
556
1
63111
TrEMBL
Secretory Pathway (Reliability: 1)
J3KT84_HUMAN
117
0
13121
TrEMBL
other Location (Reliability: 2)
A0A087WUJ7_HUMAN
227
0
25902
TrEMBL
Secretory Pathway (Reliability: 2)
B4DVA7_HUMAN
540
0
62013
TrEMBL
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
hexosaminidase A
100000 - 110000
-
hexosaminidase I2, gradient gel electrophoresis
105000
-
sedimentation equilibrium using untreated enzyme, carboxymethylated enzyme in 6 M guanidine-HCl, meniscus depletion experiments with fresh enzyme prepatation at pH 11.5
107000
-
gel filtration
112000
-
-
120000
-
enzyme after dialysis and freeze-drying, 6 M guanidine-HCl, pH 7.2
130000
-
Hex I2, gel filtration
140000
-
gel filtration
152000
-
brain enzyme type S, gel filtration
154000
-
liver enzyme type S, gel filtration
26000
-
1 * 54000 + 1 * 26000, placental enzyme, SDS-PAGE
260000
-
pH 2.5, fresh enzyme prepatation, meniscus depletion experiments
29000
29500
-
1 * 68000 + 1 * 59600 + 1 * 55600 + 1 * 29500, SDS-PAGE, mucolipidosis enzyme
54000
-
1 * 54000 + 1 * 26000, placental enzyme, SDS-PAGE
55000
55600
-
1 * 68000 + 1 * 59600 + 1 * 55600 + 1 * 29500, SDS-PAGE, mucolipidosis enzyme
56000
-
hexosaminidase A, major components: 1 * 56000 + 1 * 29000, minor components: 26000 - 22000, SDS-PAGE
58000
-
1 * 58000 + 1 * 55000 + 1 * 29000, SDS-PAGE, normal enzyme
59600
-
1 * 68000 + 1 * 59600 + 1 * 55600 + 1 * 29500, SDS-PAGE, mucolipidosis enzyme
66000
-
major Hex I2 form: alpha, beta, 1 * 66000 + 1 * 66000, beta chain 2 residues short of being identical to alpha chain, SDS-PAGE
68000
-
1 * 68000 + 1 * 59600 + 1 * 55600 + 1 * 29500, SDS-PAGE, mucolipidosis enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
heterodimer
-
-
tetramer
-
1 * 68000 + 1 * 59600 + 1 * 55600 + 1 * 29500, SDS-PAGE, mucolipidosis enzyme
trimer
-
1 * 58000 + 1 * 55000 + 1 * 29000, SDS-PAGE, normal enzyme
additional information
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop method, crystal structure of beta-hexosaminidase B, alone at 2.4 A and in complex with the mechanistic inhibitor GalNAc-isofagomine at 2.2 A or N-acetyl-beta-D-glucosamine-thiazoline at 2.5 A resolution
hanging-drop vapour-diffusion method, crystal structure of a complex of beta-hexosaminidase B with a transition state analogue inhibitor 1-acetamido-2-deoxy-D-glucono-1,5-lactone at 2.3 A resolution
-
hexosaminidase B, space group P6122 i.e. enantiomorph, 3.2 A resolution
-
vapor diffusion method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
betaAsp452Asn/betaLeu453Arg
-
the mutant enzyme of HexB exhibits more than 30fold increase in its ability to hydrolyze a 6-sulfated substrate and is able to hydrolyze GM2 ganglioside when the GM2 activator protein is replaced by sodium taurocholate
D148A
-
the mutant shows 868fold decreased catalytic efficiency with 3-fluoro-4-nitrophenyl N-acetyl-beta-D-galactosaminide compared to the wild type enzyme
D148N
-
the mutant shows 4190fold decreased catalytic efficiency with 3-fluoro-4-nitrophenyl N-acetyl-beta-D-galactosaminide compared to the wild type enzyme
E149A
-
the mutant shows 1.6fold decreased catalytic efficiency with 4-nitrophenyl N-acetyl-beta-D-galactosaminide and 0.85fold increased catalytic efficiency with 3-fluoro-4-nitrophenyl N-acetyl-beta-D-galactosaminide compared to the wild type enzyme
E149Q
-
the mutant shows 2.2fold decreased catalytic efficiency with 4-nitrophenyl N-acetyl-beta-D-galactosaminide compared to the wild type enzyme
H92A
-
the mutant shows 69fold decreased catalytic efficiency with 4-nitrophenyl N-acetyl-beta-D-galactosaminide compared to the wild type enzyme
R178H
-
from patient with the genetic disease GM2-gangliosidosis B1 variant, mutated Hex A, altered active site of alpha subunit
R424Q
-
the mutant form of HexA shows about 3fold increase in its Km-value for the complex of GM2 activator protein and GM2 ganglioside
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 37
-
stable up to 24 h
50 - 52
-
Hex A is labile, Hex B is stable, at lower sample concentrations Hex B is less stable at 52°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
resistant to mechanical inactivation by homogenization or freezing and thawing
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimethyl sulfoxide
-
with 7.5% 14% of activity remains
dimethylformamide
-
with 7.5% 9% of activity remains
dithiothreitol
-
reduction, produces fragments of 63000, 56000, 36000 and 28000 Da
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, hexosaminidase A, B and I2 separated from each other
-
4°C, liver enzyme type S, concentrated by ultrafiltration to 0.18 mg/ml, in 0.04 citrate buffer and in presence of 0.2 mg/ml bovine serum albumin stable for at least 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1500fold
-
195fold to homogeneity
-
hexosaminidase A, B and I2 purified 2699, 10320 and 13077fold
-
His-Trap column chromatography
-
HisTrap nickel column chromatography and S200 gel filtration
-
liver enzyme type S 13500fold, brain enzyme type S 5240fold, liver enzymes types A and B
-
partial
-
recombinant enzyme. HexA is purified with immobilized metal affinity column for the His tag attached to the beta-subunit
to homogeneity, normal enzyme 64863fold, I-cell enzyme 20140fold
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expressed in Pichia pastoris
-
expressed in Pichia pastoris GS115 cells
-
recombinant His-tagged HexA is produced in the methylotrophic yeast Ogataea minuta (alpha-1,6-mannosyltransferase-deficient). Genes encoding the alpha- and beta-subunits of HexA are integrated into the yeast cell, and the heterodimer is expressed together with its isozymes HexS (alphaalpha) and HexB (betabeta). A total of 57 mg of beta-hexosaminidase isozymes, of which 13 mg was HexA (alphabeta), is produced per liter of medium. The C terminus of the beta-subunit appears to be truncated in Ogataea minuta recombinant HexA
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
-
a spectrophotometric method for the determination of lysosomally derived N-acetyl-beta-D-hexosaminidase in synovial fluid on a microplate reader is optimized to improve its utility. The assay is sufficiently sensitive for small volumes of synovial fluid, and is useful for the clinical diagnosis of joint diseases
drug development
-
the enzyme is a target for GlcNAc-inspired iminocyclitiols drug development
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kinoshita, K.; Taniguchi, N.; Makita, A.; Narita, M.; Oikawa, K.
Purification and characterization of beta-N-acetylhexosaminidase I from human placenta
J. Biochem.
104
827-831
1988
Homo sapiens
Manually annotated by BRENDA team
Dewji, N.N.; De-Keyser, D.R.; Stirling, J.L.
Purification and characterization of beta-N-acetylhexosaminidase I2 from human liver
Biochem. J.
234
157-162
1986
Homo sapiens
Manually annotated by BRENDA team
Kress, B.C.; Hirani, S.; Freeze, H.H.; Little, L.; Miller, A.L.
Mucolipidosis III beta-N-acetyl-D-hexosaminidase A. Purification and properties
Biochem. J.
207
421-428
1982
Homo sapiens
Manually annotated by BRENDA team
Potier, M.; Teitelbaum, J.; Melancon, S.B.; Dallaire, L.
Purification and some properties of liver and brain beta-N-acetyl-hexosaminidase S
Biochim. Biophys. Acta
566
80-87
1979
Homo sapiens
Manually annotated by BRENDA team
Dawson, G.; Propper, R.L.; Dorfman, A.
Partial purification of beta-N-acetylhexosaminidase A by affinity chromatography
Biochem. Biophys. Res. Commun.
54
1102-1110
1973
Homo sapiens
Manually annotated by BRENDA team
Perez, L.F.; Ribeiro, H.M.; Casal, J.A.; Pinto, R.A.; Sa Miranda, M.C.; Tutor, J.C.
Thermodynamic characterization of the mutated isoenzyme A of beta-N-acetylhexosaminidase in GM2-gangliosidosis B1 variant
Clin. Chim. Acta
285
45-51
1999
Homo sapiens
Manually annotated by BRENDA team
Ribeiro, M.G.; Pinto, R.A.; Dos Santos, M.R.; Maia, M.; Sa Miranda, M.C.
Biochemical characterization of beta-acetylhexosaminidase in different biological specimens from eleven patients with GM2-gangliosidosis B1 variant
J. Inherit. Metab. Dis.
14
715-720
1991
Homo sapiens
Manually annotated by BRENDA team
Prence, E.M.; Zalewski, I.; Natowicz, M.R.
Unusual thermolability properties of beta-hexosaminidase: Studies of enzyme from cultured cells and clinical implications
Am. J. Med. Genet.
65
320-324
1996
Homo sapiens
Manually annotated by BRENDA team
Perez, L.F.; Martinez, M.I.; Ribeiro, H.M.; Pinto, R.A.; Sa Miranda, M.C.; Tutor, J.C.
Characterization of the isoenzyme profile of beta-N-acetylhexosaminidase in the urine of newborns
Clin. Chem. Lab. Med.
37
765-769
1999
Homo sapiens
Manually annotated by BRENDA team
Church, W.B.; Swenson, L.; James, M.N.G.
Crystallization of human beta-N-acetylhexosaminidase B
J. Mol. Biol.
227
577-580
1992
Homo sapiens
Manually annotated by BRENDA team
Miller, A.L.; Norton, V.; Robertson, R.; Jenks, M.; Yeh, R.Y.; Wright, D.
Light and heavy lysosomes: characterization of N-acetyl-beta-D-hexosaminidase isolatad from normal and I-cell disease lymphoblasts
Glycobiology
3
313-318
1993
Homo sapiens
Manually annotated by BRENDA team
Den Tandt, W.R.; Scharpe, S.
Characteristics of hexosaminidase A in homogenates of white blood cells using methylumbelliferyl-N-acetyl-beta-D-glucosaminide-6-sulphate as substrate
Clin. Chim. Acta
199
231-236
1991
Homo sapiens
Manually annotated by BRENDA team
Prence, E.M.; Natowicz, M.R.; Zalewski, I.
Unusual thermolability properties of leukocyte beta-hexosaminidase: Implications in screening for carriers of Tay-Sachs disease
Clin. Chem.
39
1811-1814
1993
Homo sapiens
Manually annotated by BRENDA team
Mahuran, D.J.
Characterization of human placental beta-hexosaminidase I2: Proteolytic processing intermediates of hexosaminidase A
J. Biol. Chem.
265
6794-6799
1990
Homo sapiens
Manually annotated by BRENDA team
Verpoorte, J.A.
Isolation and characterization of the major beta-N-acetyl-D-glucosaminidase from human plasma
Biochemistry
13
793-799
1974
Homo sapiens
Manually annotated by BRENDA team
Stirling, J.L.
Separation and characterization of N-acetyl-beta-glucosaminidases A and P from maternal serum
Biochim. Biophys. Acta
271
154-162
1972
Homo sapiens
Manually annotated by BRENDA team
Sharma, R.; Bukovac, S.; Callahan, J.; Mahuran, D.
A single site in human beta-hexosaminidase A binds both 6-sulfate-groups on hexosamines and the sialic acid moiety of GM2 ganglioside
Biochim. Biophys. Acta
1637
113-118
2003
Homo sapiens
Manually annotated by BRENDA team
Mark, B.L.; Mahuran, D.J.; Cherney, M.M.; Zhao, D.; Knapp, S.; James, M.N.
Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease
J. Mol. Biol.
327
1093-1109
2003
Homo sapiens (P07686), Homo sapiens
Manually annotated by BRENDA team
Maier, T.; Strater, N.; Schuette, C.G.; Klingenstein, R.; Sandhoff, K.; Saenger, W.
The X-ray crystal structure of human beta-hexosaminidase B provides new insights into Sandhoff disease
J. Mol. Biol.
328
669-681
2003
Homo sapiens
Manually annotated by BRENDA team
Lemieux, M.J.; Mark, B.L.; Cherney, M.M.; Withers, S.G.; Mahuran, D.J.; James, M.N.
Crystallographic Structure of Human beta-Hexosaminidase A: Interpretation of Tay-Sachs Mutations and Loss of G(M2) Ganglioside Hydrolysis
J. Mol. Biol.
359
913-929
2006
Homo sapiens
Manually annotated by BRENDA team
Olszewska, E.; Olszewski, S.; Borzym-Kluczyk, M.; Zwierz, K.
Role of N-acetyl-beta-d-hexosaminidase in cholesteatoma tissue
Acta Biochim. Pol.
54
365-370
2007
Homo sapiens
Manually annotated by BRENDA team
Akeboshi, H.; Chiba, Y.; Kasahara, Y.; Takashiba, M.; Takaoka, Y.; Ohsawa, M.; Tajima, Y.; Kawashima, I.; Tsuji, D.; Itoh, K.; Sakuraba, H.; Jigami, Y.
Production of recombinant beta-hexosaminidase A, a potential enzyme for replacement therapy for Tay-Sachs and Sandhoff diseases, in the methylotrophic yeast Ogataea minuta
Appl. Environ. Microbiol.
73
4805-4812
2007
Homo sapiens (P07686), Homo sapiens
Manually annotated by BRENDA team
Tropak, M.B.; Blanchard, J.E.; Withers, S.G.; Brown, E.D.; Mahuran, D.
High-throughput screening for human lysosomal beta-N-acetyl hexosaminidase inhibitors acting as pharmacological chaperones
Chem. Biol.
14
153-164
2007
Homo sapiens
Manually annotated by BRENDA team
Borzym-Kluczyk, M.; Radziejewska, I.; Olszewska, E.; Szajda, S.; Zwierz, K.
Statistical evaluation of the isoform patterns of N-acetyl-beta-hexosaminidase from human renal cancer tissue separated by isoelectrofocusing
Clin. Biochem.
40
403-406
2007
Homo sapiens
Manually annotated by BRENDA team
Massaccesi, L.; Lombardo, A.; Venerando, B.; Tettamanti, G.; Goi, G.
Isoenzyme pattern and partial characterization of hexosaminidases in the membrane and cytosol of human erythrocytes
Clin. Biochem.
40
467-477
2007
Homo sapiens
Manually annotated by BRENDA team
Tassi, C.; Angelini, A.; Beccari, T.; Capodicasa, E.
Fluorimetric determination of activity and isoenzyme composition of N-acetyl-beta-D-hexosaminidase in seminal plasma of fertile men and infertile patients with secretory azoospermia
Clin. Chem. Lab. Med.
44
843-847
2006
Homo sapiens
Manually annotated by BRENDA team
Marciniak, J.; Zalewska, A.; Popko, J.; Zwierz, K.
Optimization of an enzymatic method for the determination of lysosomal N-acetyl-beta-D-hexosaminidase and beta-glucuronidase in synovial fluid
Clin. Chem. Lab. Med.
44
933-937
2006
Homo sapiens
Manually annotated by BRENDA team
Borzym-Kluczyk, M.; Olszewska, E.; Radziejewska, I.; Lewszuk, A.; Zwierz, K.
Isoenzymes of N-acetyl-beta-hexosaminidase in human pleomorphic adenoma and healthy salivary glands: a preliminary study
Clin. Chem. Lab. Med.
46
131-136
2008
Homo sapiens
Manually annotated by BRENDA team
Popko, J.; Marciniak, J.; Zalewska, A.; Gorska, A.; Zwierz, K.; Sierakowski, S.; Urban, M.
Activity of N-acetyl-beta-hexosaminidase and its isoenzymes in serum and synovial fluid from patients with different arthropathies
Clin. Exp. Rheumatol.
24
690-693
2007
Homo sapiens
Manually annotated by BRENDA team
Tropak, M.B.; Mahuran, D.
Lending a helping hand, screening chemical libraries for compounds that enhance beta-hexosaminidase A activity in GM2 gangliosidosis cells
FEBS J.
274
4951-4961
2007
Homo sapiens
Manually annotated by BRENDA team
Tomasiak, M.M.; Tomasiak, M.; Zietkowski, Z.; Skiepko, R.; Bodzenta-Lukaszyk, A.
N-Acetyl-beta-hexosaminidase activity in asthma
Int. Arch. Allergy Immunol.
146
133-137
2008
Homo sapiens
Manually annotated by BRENDA team
Scaffidi, A.; Stubbs, K.A.; Dennis, R.J.; Taylor, E.J.; Davies, G.J.; Vocadlo, D.J.; Stick, R.V.
A 1-acetamido derivative of 6-epi-valienamine: an inhibitor of a diverse group of beta-N-acetylglucosaminidases
Org. Biomol. Chem.
5
3013-3019
2007
Bacteroides thetaiotaomicron, Homo sapiens
Manually annotated by BRENDA team
Dudzik, D.; Knas, M.; Gocal, M.; Borzym-Kluczyk, M.; Szajda, S.D.; Knas-Karaszewska, K.; Tomaszewski, J.; Zwierz, K.
Activity of N-acetyl-beta-D-hexosaminidase (HEX) and its isoenzymes A and B in human milk during the first 3 months of breastfeeding
Adv. Med. Sci.
53
300-304
2008
Homo sapiens
Manually annotated by BRENDA team
Gutternigg, M.; Rendic, D.; Voglauer, R.; Iskratsch, T.; Wilson, I.B.
Mammalian cells contain a second nucleocytoplasmic hexosaminidase
Biochem. J.
419
83-90
2009
Homo sapiens, Mus musculus (Q3U4H6), Mus musculus
Manually annotated by BRENDA team
Rountree, J.S.; Butters, T.D.; Wormald, M.R.; Boomkamp, S.D.; Dwek, R.A.; Asano, N.; Ikeda, K.; Evinson, E.L.; Nash, R.J.; Fleet, G.W.
Design, synthesis, and biological evaluation of enantiomeric beta-N-acetylhexosaminidase inhibitors LABNAc and DABNAc as potential agents against Tay-Sachs and Sandhoff disease
ChemMedChem
4
378-392
2009
Bos taurus, Homo sapiens, Canavalia sp.
Manually annotated by BRENDA team
Olszewska, E.; Borzym-Kluczyk, M.; Rzewnicki, I.; Rutkowska, J.; Knas, M.; Rogowski, M.; Waniewska, E.; Wielgosz, R.
Hexosaminidase as a new potential marker for larynx cancer
Clin. Biochem.
42
1187-1189
2009
Homo sapiens
Manually annotated by BRENDA team
Szajda, S.D.; Snarska, J.; Jankowska, A.; Puchalski, Z.; Zwierz, K.
Isoenzymes A and B of N-acetyl-beta-D-hexosaminidase in serum and urine of patients with pancreatic cancer
Hepatogastroenterology
55
695-698
2008
Homo sapiens
Manually annotated by BRENDA team
Macauley, M.S.; Whitworth, G.E.; Debowski, A.W.; Chin, D.; Vocadlo, D.J.
O-GlcNAcase uses substrate-assisted catalysis: kinetic analysis and development of highly selective mechanism-inspired inhibitors
J. Biol. Chem.
280
25313-25322
2005
Homo sapiens
Manually annotated by BRENDA team
Stubbs, K.A.; Zhang, N.; Vocadlo, D.J.
A divergent synthesis of 2-acyl derivatives of PUGNAc yields selective inhibitors of O-GlcNAcase
Org. Biomol. Chem.
4
839-845
2006
Homo sapiens
Manually annotated by BRENDA team
Ho, C.W.; Popat, S.D.; Liu, T.W.; Tsai, K.C.; Ho, M.J.; Chen, W.H.; Yang, A.S.; Lin, C.H.
Development of GlcNAc-inspired iminocyclitiols as potent and selective N-acetyl-beta-hexosaminidase inhibitors
Chem. Biol.
5
489-497
2010
Homo sapiens
Manually annotated by BRENDA team
Alteen, M.G.; Oehler, V.; Nemcovicova, I.; Wilson, I.B.; Vocadlo, D.J.; Gloster, T.M.
Mechanism of human nucleocytoplasmic hexosaminidase D
Biochemistry
55
2735-2747
2016
Homo sapiens
Manually annotated by BRENDA team
Dong, L.; Shen, S.; Chen, W.; Lu, H.; Xu, D.; Jin, S.; Yang, Q.; Zhang, J.
Glycosyl triazoles as novel insect beta-N-acetylhexosaminidase OfHex1 inhibitors Design, synthesis, molecular docking and MD simulations
Bioorg. Med. Chem.
27
2315-2322
2019
Homo sapiens, Ostrinia furnacalis (Q06GJ0)
Manually annotated by BRENDA team
Shen, S.; Chen, W.; Dong, L.; Yang, Q.; Lu, H.; Zhang, J.
Design and synthesis of naphthalimide group-bearing thioglycosides as novel beta-N-acetylhexosaminidases inhibitors
J. Enzyme Inhib. Med. Chem.
33
445-452
2018
Homo sapiens
Manually annotated by BRENDA team
Tropak, M.B.; Zhang, J.; Yonekawa, S.; Rigat, B.A.; Aulakh, V.S.; Smith, M.R.; Hwang, H.J.; Ciufolini, M.A.; Mahuran, D.J.
Pyrimethamine derivatives insight into binding mechanism and improved enhancement of mutant beta-N-acetylhexosaminidase activity
J. Med. Chem.
58
4483-4493
2015
Homo sapiens
Manually annotated by BRENDA team