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EC Tree
IUBMB Comments The enzyme, characterized from the bacterium Vibrio furnissii, is an endo-cleaving chitodextrinase that participates in the the chitin catabolic pathway found in members of the Vibrionaceae. Unlike EC 3.2.1.14, chitinase, it has no activity on chitin. The smallest substrate is a tetrasaccharide, and the final products are N,N'-diacetylchitobiose and small amounts of N,N',N''-triacetylchitotriose. cf. EC 3.2.1.200, exo-chitinase (non-reducing end), and EC 3.2.1.201, exo-chitinase (reducing end).
The expected taxonomic range for this enzyme is: Vibrio furnissii
Reaction Schemes
Hydrolysis of chitodextrins, releasing N,N'-diacetylchitobiose and small amounts of N,N',N''-triacetylchitotriose
Synonyms
chitodextrinase, endoi, periplasmic chitodextrinase,
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endolytic chitodextrinase
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periplasmic chitodextrinase
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chitodextrinase
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ambiguous
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Endo I
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ambiguous
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endoI
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Hydrolysis of chitodextrins, releasing N,N'-diacetylchitobiose and small amounts of N,N',N''-triacetylchitotriose
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(1->4)-2-acetamido-2-deoxy-beta-D-glucan diacetylchitobiohydrolase (endo-cleaving)
The enzyme, characterized from the bacterium Vibrio furnissii, is an endo-cleaving chitodextrinase that participates in the the chitin catabolic pathway found in members of the Vibrionaceae. Unlike EC 3.2.1.14, chitinase, it has no activity on chitin. The smallest substrate is a tetrasaccharide, and the final products are N,N'-diacetylchitobiose and small amounts of N,N',N''-triacetylchitotriose. cf. EC 3.2.1.200, exo-chitinase (non-reducing end), and EC 3.2.1.201, exo-chitinase (reducing end).
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4-methylumbelliferyl beta-D-N,N'-diacetylchitobioside + H2O
4-methylumbelliferone + N,N'-diacetylchitobiose
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?
4-nitrophenyl beta-D-N,N'-diacetylchitobioside + H2O
4-nitrophenol + N,N'-diacetylchitobiose
chitooligosaccharide + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose + ?
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N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
2 N,N',N''-triacetylchitotriose
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
N,N',N'',N'''-tetraacetylchitotetraose + H2O
2 N,N'-diacetylchitobiose
additional information
?
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4-nitrophenyl beta-D-N,N'-diacetylchitobioside + H2O
4-nitrophenol + N,N'-diacetylchitobiose
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?
4-nitrophenyl beta-D-N,N'-diacetylchitobioside + H2O
4-nitrophenol + N,N'-diacetylchitobiose
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?
4-nitrophenyl beta-D-N,N'-diacetylchitobioside + H2O
4-nitrophenol + N,N'-diacetylchitobiose
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?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
2 N,N',N''-triacetylchitotriose
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?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
2 N,N',N''-triacetylchitotriose
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?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
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?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
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?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
2 N,N'-diacetylchitobiose
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N,N',N'',N'''-tetraacetylchitotetraose + H2O
2 N,N'-diacetylchitobiose
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additional information
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chitodextrinase cleaves soluble oligomers, but not chitin, to the di- and trisaccharides
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additional information
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the enzyme converts chitin oligosaccharides to GlcNAc and (GlcNAc)2. No substrates: chitin, glucosamine oligosaccharides, glycoproteins, and glycopeptides containing (GlcNAc)2
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additional information
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the enzyme converts chitin oligosaccharides to GlcNAc and (GlcNAc)2. No substrates: chitin, glucosamine oligosaccharides, glycoproteins, and glycopeptides containing (GlcNAc)2
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?
additional information
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the enzyme converts chitin oligosaccharides to GlcNAc and (GlcNAc)2. No substrates: chitin, glucosamine oligosaccharides, glycoproteins, and glycopeptides containing (GlcNAc)2
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Mg2+
2 mM, 20-25% stimulation
NaCl
activity remains relatively constant over the range 50-250 mM NaCl (pH 7.0), but decreases significantly below and above these concentrations
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2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1->4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1->4)-2-acetamido-2-deoxy-beta-D-glucopyranose
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4-nitrophenyl beta-D-N,N',N''-triacetylchitotrioside
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4-nitrophenyl beta-D-N-acetylglucosamine
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Hg2+
5 mM, 25% loss of activity
KCl
10-30% decrease in activity
N,N',N'',N''',N'''',N'''''-hexacetylchitohexaose
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N,N',N'',N''',N''''-pentacetylchitopentaose
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N,N',N'',N'''-tetraacetylchitotetraose
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N,N'-diacetylchitobiose
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NaCl
activity remains relatively constant over the range 50-250 mM NaCl (pH 7.0), but decreases significantly below and above these concentrations
additional information
not affected by 5 mM EDTA or EGTA, nor by the addition of up to 5mM Ca2+ or Zn2+
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additional information
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not affected by 5 mM EDTA or EGTA, nor by the addition of up to 5mM Ca2+ or Zn2+
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0.066
4-nitrophenyl beta-D-N,N'-diacetylchitobioside
pH 7.4, 25°C
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0.57
2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1->4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1->4)-2-acetamido-2-deoxy-beta-D-glucopyranose
pH 7.5, 37°C
0.22
4-nitrophenyl beta-D-N,N',N''-triacetylchitotrioside
pH 7.5, 37°C
0.65
4-nitrophenyl beta-D-N-acetylglucosamine
pH 7.5, 37°C
0.077
N,N',N'',N''',N'''',N'''''-hexacetylchitohexaose
pH 7.5, 37°C
0.088
N,N',N'',N''',N''''-pentacetylchitopentaose
pH 7.5, 37°C
0.09
N,N',N'',N'''-tetraacetylchitotetraose
pH 7.5, 37°C
1.025
N,N'-diacetylchitobiose
pH 7.5, 37°C
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325
substrate 4-nitrophenyl beta-D-N,N'-diacetylchitobioside, pH 7.5, 37°C
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7.5
58-70% of maximum activity
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UniProt
brenda
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UniProt
brenda
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brenda
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brenda
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CHID_VIBFU
1046
0
112380
Swiss-Prot
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monomer
1 * 112380, calculated, 1 * 120000, SDS-PAGE
monomer
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1 * 112380, calculated, 1 * 120000, SDS-PAGE
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proteolytic modification
srquence contains an N-terminal 31 amino acids signal peptide
proteolytic modification
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srquence contains an N-terminal 31 amino acids signal peptide
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52
15 min, complete inactivation
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expression in Escherichia coli
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expression is induced by N,N'-diacetylchitobiose
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Bassler, B.; Yu, C.; Lee, Y.; Roseman, S.
Chitin utilization by marine bacteria: Degradation and catabolism of chitin oligosaccharides by Vibrio furnissii
J. Biol. Chem.
266
24276-24286
1991
Vibrio furnissii (P96156)
brenda
Keyhani, N.; Roseman, S.
The chitin catabolic cascade in the marine bacterium Vibrio furnissii: Molecular cloning, isolation, and characterization of a periplasmic chitodextrinase
J. Biol. Chem.
271
33414-33424
1996
Vibrio furnissii (P96156), Vibrio furnissii, Vibrio furnissii UniProt (P96156)
brenda
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3.2.1.202 endo-chitodextinase
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