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3.2.1.52: beta-N-acetylhexosaminidase

This is an abbreviated version!
For detailed information about beta-N-acetylhexosaminidase, go to the full flat file.

Word Map on EC 3.2.1.52

Reaction

(N-acetyl-D-glucosamine)4
+ 3 H2O = 4 2-(acetylamino)-2-deoxy-beta-D-glucopyranose

Synonyms

2-acetamido-2-deoxy-beta-D-glucoside acetamidodeoxyglucohydrolase, 3-beta-N-acetylglucosaminidase, 65 kDa epididymal boar protein, Am2301, Am2446, At1g65600/F5I14_13, beta-acetylaminodeoxyhexosidase, beta-acetylhexosaminidase, beta-acetylhexosaminidinase, beta-D-hexosaminidase, beta-D-N-acetylhexosaminidase, Beta-GlcNAcase, beta-glucosidase, beta-HEX, beta-HexNAcase, beta-hexosaminidase, beta-hexosaminidase A, beta-hexosaminidase B, beta-hexosaminidase I, beta-hexosaminidase II, beta-N-acetyl-D-glucosaminidase, 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-NAGase, beta-NAHA, Beta-NAHASE, bifunctional exo-beta-glucosidase/N-acetyl-beta-glucosaminidase, BmCHI-h, BmGlcNAcase 1, BmGlcNAcase 2, BmNPV CHIA, CbsA, Chi-I, Chi-II, chitobiase, chitobiase 2, CpGV V-CHIA, dispersin B, DmHEXA, DmHEXB, DspB, EC 3.2.1.29, EC 3.2.1.30, endo-beta-N-acetylglucosaminidase, EXC1Y, EXC2Y, exo-acting chitinase, exo-beta-D-N-acetylglucosaminidase, exo-beta-hexosaminidase, exo-type beta-N-acetylhexosaminidase, exochitinase, F3F20.4 protein, FDL, GH84C, GlcNAcase, Hex, Hex A, Hex B, Hex-1, Hex1, Hex2, Hex20, Hex4, HexB, HexD, HEXDC, hEXO1, HEXO2, HEXO3, hexosaminidase, hexosaminidase A, hexosaminidase B, hexosaminidase D, hHexA, lacto-N-biosidase, lnba, lysosomal beta-hexosaminidase, More, N-acetyl-beta-D-hexosaminidase, N-acetyl-beta-glucosaminidase, N-acetyl-beta-hexosaminidase, N-acetylglucosaminidase, N-acetylhexosaminidase, NAG-68, NAG-B, NAG1, NAG2, Nag3, NagA, NAGase, NagJ, NagZ, NAHA, NAHase, neutral hexosaminidase C, O-GlcNAcase, Pcb-NAHA1, Sfhex, SSO3039, StrH, zymocin alpha-subunit

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.52 beta-N-acetylhexosaminidase

Engineering

Engineering on EC 3.2.1.52 - beta-N-acetylhexosaminidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D183N
-
no activity with 4-methylumbelliferyl N-acetyl-beta-D-glucosamine. Kcat/KM for 4-nitrophenyl N-acetyl-beta-D-glucosamine is 13333fold lower than wild-type value. Biofilm-detachment activity is very low
E184Q
-
no activity with 4-methylumbelliferyl N-acetyl-beta-D-glucosamine. Kcat/KM for 4-nitrophenyl N-acetyl-beta-D-glucosamine is 70.6fold lower than wild-type value. pH-optimum is shifted from pH 5.8 for wild-type enzyme to pH 6.8 for the mutant enzyme
E332Q
-
no activity with 4-methylumbelliferyl N-acetyl-beta-D-glucosamine. Kcat/KM for 4-nitrophenyl N-acetyl-beta-D-glucosamine is 2000fold lower than wild-type value. Biofilm-detachment activity is 28fold less efficient than the wild-type
R27A
-
no activity with 4-methylumbelliferyl N-acetyl-beta-D-glucosamine. Kcat/KM for 4-nitrophenyl N-acetyl-beta-D-glucosamine is 2400fold lower than wild-type value. Biofilm-detachment activity is 20fold less efficient than the wild-type
R27K
-
no activity with 4-methylumbelliferyl N-acetyl-beta-D-glucosamine. Kcat/KM for 4-nitrophenyl N-acetyl-beta-D-glucosamine is 1714fold lower than wild-type value. Biofilm-detachment activity is 26fold less efficient than the wild-type
W237A
-
no activity with 4-methylumbelliferyl N-acetyl-beta-D-glucosamine and 4-nitrophenyl N-acetyl-beta-D-glucosamine. Biofilm-detachment activity is 167fold less efficient than the wild-type
W330Y
-
no activity with 4-methylumbelliferyl N-acetyl-beta-D-glucosamine and 4-nitrophenyl N-acetyl-beta-D-glucosamine. Biofilm-detachment activity is 19.2fold less efficient than the wild-type
Y187A
-
Kcat/KM for 4-nitrophenyl N-acetyl-beta-D-glucosamine is 40fold lower than wild-type value. Kcat/KM for 4-methylumbelliferyl N-acetyl-beta-D-glucosamine is 4.9fold lower than wild-type value. Biofilm-detachment activity is 8.3fold less efficient than the wild-type
Y278A
-
Kcat/KM for 4-nitrophenyl N-acetyl-beta-D-glucosamine is 923fold lower than wild-type value. Kcat/KM for 4-methylumbelliferyl N-acetyl-beta-D-glucosamine is 45fold lower than wild-type value. Biofilm-detachment activity is 11fold less efficient than the wild-type
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
E328A
activity similar to wild-type
E328Q
about 20% decrease in activity
H433A
about 20% decrease in activity
V327G
about 30% decrease in activity
W448A
mutation results in a more than 1000fold loss in enzyme activity, due mainly to the effect on kcat
W448F
about 50% decrease in activity
W490A
mutation leads to a 2277fold decrease in sensitivity toward TMG-chitotriomycin as well as an 18fold decrease in binding affinity for the substrate (GlcNAc)2
D321E
-
site-directed mutagenesis, the Hex1 mutant shows reduced activity compared to the wild-type enzyme
D321N
-
site-directed mutagenesis, almost inactive Hex1 mutant
E322D
-
site-directed mutagenesis, the Hex1 mutant shows highly reduced activity compared to the wild-type enzyme
E322Q
-
site-directed mutagenesis, the Hex1 mutant shows reduced activity compared to the wild-type enzyme
D306A
the mutant enzyme is inactive with 4-nitrophenyl N-acetyl-beta-D-glucosaminide and chitobiose
D306E
the mutant enzyme shows 4.2% activity with 4-nitrophenyl N-acetyl-beta-D-glucosaminide compared to the wild type and is inactive with chitobiose
D306E/E307D
the mutant enzyme shows 2.7% activity with 4-nitrophenyl N-acetyl-beta-D-glucosaminide compared to the wild type and is inactive with chitobiose
D306N
the mutant enzyme is inactive with 4-nitrophenyl N-acetyl-beta-D-glucosaminide and chitobiose
E307A
the mutant enzyme shows 2.0% activity with 4-nitrophenyl N-acetyl-beta-D-glucosaminide compared to the wild type and is inactive with chitobiose
E307D
the mutant enzyme shows 8.6% activity with 4-nitrophenyl N-acetyl-beta-D-glucosaminide compared to the wild type and is inactive with chitobiose
E307Q
the mutant enzyme shows 1.5% activity with 4-nitrophenyl N-acetyl-beta-D-glucosaminide compared to the wild type and is inactive with chitobiose
D306A
-
the mutant enzyme is inactive with 4-nitrophenyl N-acetyl-beta-D-glucosaminide and chitobiose
-
D306E
-
the mutant enzyme shows 4.2% activity with 4-nitrophenyl N-acetyl-beta-D-glucosaminide compared to the wild type and is inactive with chitobiose
-
D306N
-
the mutant enzyme is inactive with 4-nitrophenyl N-acetyl-beta-D-glucosaminide and chitobiose
-
E307A
-
the mutant enzyme shows 2.0% activity with 4-nitrophenyl N-acetyl-beta-D-glucosaminide compared to the wild type and is inactive with chitobiose
-
E307D
-
the mutant enzyme shows 8.6% activity with 4-nitrophenyl N-acetyl-beta-D-glucosaminide compared to the wild type and is inactive with chitobiose
-
W443A
mutant of catalytic domain GH20-1, comparable Km but much lower kcat values than wild-type, enzymatic activities kcat/Km of about 1% towards 4-nitrophenyl-N-acetylglucosamine and one-fourth towards N-acetylglucosaminyl-beta-1,2-Man
W443A/W876A
significant decrease in activity
W443A/W876A/Y482A/Y914A
no detectable activity
W443A/Y482A
mutant of catalytic domain GH20-1, no detectable activity
W443F
mutant of catalytic domain GH20-1, one-sixth of wild-type activity towards 4-nitrophenyl-N-acetylglucosamine
W876A
mutant of catalytic domain GH20-2, one-third of wild-type activity towards 4-nitrophenyl-N-acetylglucosamine
W876A/Y914A
mutant of catalytic domain GH20-2, no detectable activity
W876F
mutant of catalytic domain GH20-2, one-eighth of wild-type activity towards 4-nitrophenyl-N-acetylglucosamine
Y482A
Y482A/Y914A
complete loss of activity
Y482F
mutant of catalytic domain GH20-1, one-third of wild-type activity towards 4-nitrophenyl-N-acetylglucosamine
Y914A
mutant of catalytic domain GH20-2, increase in kcat value
Y914F
mutant of catalytic domain GH20-2, activity comparable to wild-type
D246N
-
mutant
E314Q
-
mutant
R162H
-
mutant
additional information