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Information on EC 3.2.1.52 - beta-N-acetylhexosaminidase and Organism(s) Bombyx mori and UniProt Accession Q3L6N4

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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:
Bombyx mori
UNIPROT: Q3L6N4
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Word Map
The taxonomic range for the selected organisms is: Bombyx mori
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
BmGlcNAcase 2
-
2-acetamido-2-deoxy-beta-D-glucoside acetamidodeoxyglucohydrolase
-
-
-
-
65 kDa epididymal boar protein
-
-
-
-
beta-acetylaminodeoxyhexosidase
-
-
-
-
beta-acetylhexosaminidase
-
-
-
-
beta-acetylhexosaminidinase
-
-
-
-
beta-D-hexosaminidase
-
-
-
-
beta-D-N-acetylhexosaminidase
-
-
-
-
Beta-GlcNAcase
-
-
-
-
beta-hexosaminidase
-
-
-
-
beta-N-acetyl-D-hexosaminidase
-
-
-
-
beta-N-acetyl-hexosaminidase
-
-
-
-
beta-N-acetylgalactosaminidase
-
-
-
-
beta-N-acetylglucosaminidase
-
-
-
-
Beta-N-acetylhexosaminidase
-
-
-
-
beta-NAHA
-
-
-
-
Beta-NAHASE
-
-
-
-
BmCHI-h
-
-
BmGlcNAcase 1
-
chitobiase
-
-
-
-
Hex
-
-
-
-
hexosaminidase
-
-
-
-
hexosaminidase A
-
-
-
-
N-acetyl-beta-D-hexosaminidase
-
-
-
-
N-acetyl-beta-glucosaminidase
-
-
-
-
N-acetyl-beta-hexosaminidase
-
-
-
-
N-acetylhexosaminidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides
show the reaction diagram
exo-type reaction
-
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
4-nitrophenyl N-acetyl-beta-D-galactosamine + H2O
4-nitrophenol + N-acetylgalactosamine
show the reaction diagram
-
-
-
?
4-nitrophenyl N-acetyl-beta-D-glucosamine + H2O
4-nitrophenol + N-acetylglucosamine
show the reaction diagram
-
-
-
?
(N-acetyl-beta-D-glucosamine)2 + H2O
2 N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
-
?
(N-acetyl-beta-D-glucosamine)3 + H2O
(N-acetyl-beta-D-glucosamine)2 + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
-
?
(N-acetyl-beta-D-glucosamine)4 + H2O
(N-acetyl-beta-D-glucosamine)3 + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
-
?
(N-acetyl-beta-D-glucosamine)5 + H2O
(N-acetyl-beta-D-glucosamine)4 + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
-
?
(N-acetyl-beta-D-glucosamine)6 + H2O
(N-acetyl-beta-D-glucosamine)5 + N-acetyl-beta-D-glucosamine
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-N,N',N''-triacetylchitotriose + H2O
?
show the reaction diagram
-
higher activity against 4-methylumbelliferyl-N,N'-diacetylchitobiose than 4-methylumbelliferyl-N,N',N''-triacetylchitotriose
-
-
?
4-methylumbelliferyl-N,N'-diacetylchitobiose + H2O
?
show the reaction diagram
-
higher activity against 4-methylumbelliferyl-N,N'-diacetylchitobiose than 4-methylumbelliferyl-N,N',N''-triacetylchitotriose
-
-
?
4-nitrophenyl N-acetyl-beta-D-galactosamine + H2O
4-nitrophenol + N-acetylgalactosamine
show the reaction diagram
-
-
-
?
4-nitrophenyl N-acetyl-beta-D-glucosamine + H2O
4-nitrophenol + N-acetylglucosamine
show the reaction diagram
-
-
-
?
chitin + H2O
N-acetylglucosamine
show the reaction diagram
-
colloidal chitin
-
-
?
chitin oligosaccharides + H2O
N-acetyl-D-glucosamine
show the reaction diagram
-
(N-acetyl-D-glucosamine)2-6
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
?
show the reaction diagram
-
-
-
-
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
2 N,N-diacetylchitobiose
show the reaction diagram
-
-
-
-
?
N,N',N''-triacetylchitotriose + H2O
N-acetyl-D-glucosamine + N,N'-diacetylchitobiose
show the reaction diagram
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
deacetylated chitooligosaccharides + acetate
show the reaction diagram
-
-
-
-
?
N,N'-diacetylchitobiose + H2O
N-acetyl-D-glucosamine
show the reaction diagram
-
-
-
-
?
N-acetyl-beta-D-hexosaminides + H2O
N-acetyl-D-hexosamines
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
phenyl N-acetyl-beta-D-galactosaminide + H2O
phenol + N-acetyl-beta-D-galactosaminide
show the reaction diagram
-
-
-
-
?
phenyl-N-acetyl-beta-D-glucosaminide + H2O
phenol + N-acetyl-beta-D-glucosaminide
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no detectable activity against 4-methylumbelliferyl-GlcNAc, exo-type substrate preference
-
-
?
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
N-acetyl-beta-D-hexosaminides + H2O
N-acetyl-D-hexosamines
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-acetamido-1,2-deoxynojirimycin
-
Ca2+
-
with 0.03 mM 42.9% of activity remains
Mg2+
-
with 0.03 mM 71.4% of activity remains
Zn2+
-
with 0.03 mM 88.6% of activity remains
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
0.0075 mM: activity reaches 110.0%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.64 - 0.787
(N-acetyl-beta-D-glucosamine)2
-
0.05 - 0.87
(N-acetyl-beta-D-glucosamine)3
-
0.03 - 0.16
(N-acetyl-beta-D-glucosamine)4
-
0.07 - 0.09
(N-acetyl-beta-D-glucosamine)5
-
0.056 - 0.1
(N-acetyl-beta-D-glucosamine)6
-
0.31 - 0.64
p-nitrophenyl-beta-2-acetamido-2-deoxy-D-galactopyranoside
0.397 - 0.49
p-nitrophenyl-beta-2-acetamido-2-deoxy-D-glucopyranoside
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
580 - 1010
(N-acetyl-beta-D-glucosamine)2
-
82 - 209
(N-acetyl-beta-D-glucosamine)3
-
42 - 129
(N-acetyl-beta-D-glucosamine)4
-
57 - 76
(N-acetyl-beta-D-glucosamine)5
-
29 - 55
(N-acetyl-beta-D-glucosamine)6
-
320 - 1150
p-nitrophenyl-beta-2-acetamido-2-deoxy-D-galactopyranoside
720 - 890
p-nitrophenyl-beta-2-acetamido-2-deoxy-D-glucopyranoside
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
362.9
-
-
60.6
-
substrate: p-nitrophenyl-beta-2-acetamido-2-deoxy-D-glucopyranoside
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6
-
Ex 1, Ex 2 and alimentary canal enzyme
5.5 - 6
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 7.5
the isozyme shows 70% of maximal activity pH 3.5, 30% at pH 7.5
4.5 - 7.5
50% of maximal activity at pH 4.5 and pH 7.5, inactive at pH 3.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
alimentary canal enzyme
55
-
Ex 1
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme A or BmGlcNAcase 2; isozyme BmGlcNAcase 2
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
of fifth instar larvae, low expression level of BmGlcNAcase 2
Manually annotated by BRENDA team
of fifth instar larvae, low expression level of BmGlcNAcase 2
Manually annotated by BRENDA team
BmGlcNAcase 2, first to fourth instar stage, only in some tissue in the fifth instar larvae stage, overview
Manually annotated by BRENDA team
of fifth instar larvae
Manually annotated by BRENDA team
of fifth instar larvae
Manually annotated by BRENDA team
of fifth instar larvae, low expression level of BmGlcNAcase 2
Manually annotated by BRENDA team
-
BmCHI-h is rapidly secreted from virus-infected BmN cells
Manually annotated by BRENDA team
of fifth instar larvae, BmGlcNAcase 1
Manually annotated by BRENDA team
of fifth instar larvae, BmGlcNAcase 1
Manually annotated by BRENDA team
first to fifth instar stage
Manually annotated by BRENDA team
of fifth instar larvae, BmGlcNAcase 1
Manually annotated by BRENDA team
of fifth instar larvae, BmGlcNAcase 1
Manually annotated by BRENDA team
of fifth instar larvae, BmGlcNAcase 1
Manually annotated by BRENDA team
of fifth instar larvae, BmGlcNAcase 1
Manually annotated by BRENDA team
of fifth instar larvae, BmGlcNAcase 1
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
BmCHI-h is rapidly secreted from virus-infected BmN cells
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q3L6N4_BOMMO
536
0
61551
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
61500
x * 61500, isozyme BmGlcNAcase 2
119000
-
gel filtration
125000
135000
-
Ex 1, gel filtration
57500
61000
-
SDS-PAGE
67500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 61500, isozyme BmGlcNAcase 2
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
neutral sugar
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
-
alimentary canal enzyme, stable
393704
5 - 9
-
Ex 2, stable
393704
5.5 - 8.5
-
stable
393705
6 - 8
-
Ex 1, stable
393704
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
stable below, for 10 min
40
-
alimentary canal enzyme, stable below
48
-
Ex 1, stable below
58
-
alimentary canal enzyme, 50% of activity remains
62
-
Ex 1, 50% of activity remains
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilization reduces activity to 34.5%
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, after 27 days 87.1% of activity remains
-
4°C, not stable, rapid decrease of activity after the first 12 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3350fold to homogeneity
-
64fold to homogeneity
-
Ex 1: 3000fold, Ex 2: 3200fold
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene and isozyme BmGlcNAcase 2, DNA and amino acid sequence determnination and analysis, genetic structure, phylogenetic analysis, and sequence comparisons, expression in Trichoplusia ni TN5 cells using the baculovirus tranfection method
gene and isozyme BmGlcNAcase 1, expression in Trichoplusia ni TN5 cells using the baculovirus tranfection method
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Koga, D.; Shimazaki, C.; Yamamoto, K.; Inoue, K.; Kimura, S.; Ide, A.
beta-N-Acetyl-D-glucosaminidases from integument of the silkworm, Bombyx mori: Comparative biochemistry with the pupal alimentary canal enzyme
Agric. Biol. Chem.
51
1679-1681
1987
Bombyx mori
-
Manually annotated by BRENDA team
Koga, D.; Nakashima, M.; Matsukara, T.; Kimura, S.; Ide, A.
Purification and properties of beta-N-acetyl-D-glucosaminidase from alimentary canal of the silkworm, Bombyx mori
Agric. Biol. Chem.
50
2357-2368
1986
Bombyx mori
-
Manually annotated by BRENDA team
Kimura, S.
Insect haemolymph exo-beta-N-acetylglucosaminidase from Bombyx mori
Biochim. Biophys. Acta
446
399-406
1976
Bombyx mori
Manually annotated by BRENDA team
Daimon, T.; Katsuma, S.; Kang, W.; Shimada, T.
Comparative studies of Bombyx mori nucleopolyhedrovirus chitinase and its host ortholog, BmChi-h
Biochem. Biophys. Res. Commun.
345
825-833
2006
Bombyx mori, Bombyx mori nucleopolyhedrovirus
Manually annotated by BRENDA team
Kokuho, T.; Yasukochi, Y.; Watanabe, S.; Inumaru, S.
Molecular cloning and expression profile analysis of a novel beta-D-N-acetylhexosaminidase of domestic silkworm (Bombyx mori)
Genes Cells
15
525-536
2010
Bombyx mori (P49010), Bombyx mori (Q3L6N4), Bombyx mori
Manually annotated by BRENDA team