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4-methylumbelliferyl beta-D-N,N'-diacetylchitobioside + H2O
4-methylumbelliferone + beta-D-N,N'-diacetylchitobiose
-
-
-
?
4-methylumbelliferyl beta-D-N,N'-diacetylchitobioside + H2O
?
4-methylumbelliferyl beta-N,N',N''-triacetylchitotrioside + H2O
methylumbelliferone + N,N',N''-triacetylchitotriose
4-methylumbelliferyl N,N'-diacetylchitobioside + H2O
methylumbelliferone + N,N'-diacetylchitobiose
4-nitrophenyl beta-N,N',N'', N'''-tetraacetylchitotetraoside + H2O
?
-
-
-
?
4-nitrophenyl beta-N,N',N''-triacetylchitotrioside + H2O
?
-
-
-
?
4-nitrophenyl beta-N,N'-diacetylchitobioside + H2O
?
-
-
-
?
alpha-chitin + H2O
?
-
-
-
?
chitooligosaccharide + H2O
?
-
-
-
?
chitosan + H2O
?
-
65% acetylated chitosan, enzyme shows a processive mode of action, moving the sugar chain two residues at a time and almost exclusively yielding oligomers with even-numbered chain lengths
-
?
chitosan + H2O
N,N'-diacetylchitobiose + ?
-
-
-
?
chitotriose + H2O
?
-
-
-
?
colloidal chitin + H2O
N,N'-diacetylchitobiose + ?
colloidal chitin + H2O
N-acetyl beta-D-glucosamine + chitobiose + chitotriose
colloidal chitin + H2O
N-acetyl D-glucosamine + ?
-
-
-
-
?
colloidal chitin + H2O
N-acetylglucosamine + N,N'-diacetylchitobiose + ?
crab shell chitin + H2O
N,N'-diacetylchitobiose + ?
-
the enzyme processively cleaves off chitobiose from the nonreducing end of chitin or other chitooligomers
-
-
?
crystalline beta-chitin + H2O
N,N'-diacetylchitobiose + ?
GlcNAcbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta(1->4)GlcNAc + H2O
2 N,N'-diacetylchitobiose
-
the enzyme processively cleaves off chitobiose from the nonreducing end of chitin or other chitooligomers
-
-
?
GlcNAcbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta(1->4)GlcNAc + H2O
N,N'-diacetylchitobiose + ?
-
the enzyme processively cleaves off chitobiose from the nonreducing end of chitin or other chitooligomers
-
-
?
GlcNAcbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta(1->4)GlcNAc + H2O
N,N'-diacetylchitobiose + GlcNAcbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta(1->4)GlcNAcbeta
-
ChiBcat hydrolyzes chitooligosaccharides (degree of polymerization = 3 to 6), yielding predominantly chitobiose. (GlcNAc)6 is processively degraded to mostly (GlcNAc)4 and (GlcNAc)2, with limited formation of (GlcNAc)3
-
-
?
glycol chitin + H2O
N,N'-diacetylchitobiose + ?
-
-
-
?
high molecular weight chitin + H2O
?
moderate molecular weight chitin + H2O
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N',N''-triacetylchitotriose + N,N'-diacetylchitobiose + N,N',N'',N'''-tetraacetylchitotetraose
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N'',N'''-tetraacetylchitotetraose
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose
N,N',N'',N'''-tetraacetylchitotetraose + H2O
2 N,N'-diacetylchitobiose
potato shell + H2O
?
-
-
-
-
?
additional information
?
-
4-methylumbelliferyl beta-D-N,N'-diacetylchitobioside + H2O
?
-
-
-
?
4-methylumbelliferyl beta-D-N,N'-diacetylchitobioside + H2O
?
-
-
-
?
4-methylumbelliferyl beta-N,N',N''-triacetylchitotrioside + H2O
methylumbelliferone + N,N',N''-triacetylchitotriose
-
-
-
?
4-methylumbelliferyl beta-N,N',N''-triacetylchitotrioside + H2O
methylumbelliferone + N,N',N''-triacetylchitotriose
-
-
-
?
4-methylumbelliferyl N,N'-diacetylchitobioside + H2O
methylumbelliferone + N,N'-diacetylchitobiose
-
-
-
?
4-methylumbelliferyl N,N'-diacetylchitobioside + H2O
methylumbelliferone + N,N'-diacetylchitobiose
-
-
-
?
bean peel + H2O
?
-
-
-
-
?
bean peel + H2O
?
-
-
-
-
?
beta-chitin + H2O
?
-
ChiB is active from the nonreducing end to the reducing end
-
?
beta-chitin + H2O
?
-
ChiB is active from the nonreducing end to the reducing end
-
?
beta-chitin + H2O
?
-
-
-
?
chitin + H2O
?
-
-
-
-
?
colloidal chitin + H2O
?
-
100% activity
-
-
?
colloidal chitin + H2O
?
-
100% activity
-
-
?
colloidal chitin + H2O
?
-
-
-
?
colloidal chitin + H2O
?
minimal activity
-
-
?
colloidal chitin + H2O
N,N'-diacetylchitobiose + ?
-
-
-
?
colloidal chitin + H2O
N,N'-diacetylchitobiose + ?
-
the enzyme processively cleaves off chitobiose from the nonreducing end of chitin or other chitooligomers
-
-
?
colloidal chitin + H2O
N-acetyl beta-D-glucosamine + chitobiose + chitotriose
-
-
-
-
?
colloidal chitin + H2O
N-acetyl beta-D-glucosamine + chitobiose + chitotriose
-
-
-
-
?
colloidal chitin + H2O
N-acetylglucosamine + N,N'-diacetylchitobiose + ?
-
ChiB produces relatively large amounts of chitin monomer and dimer, but very low amounts of trimer
-
?
colloidal chitin + H2O
N-acetylglucosamine + N,N'-diacetylchitobiose + ?
-
ChiB produces relatively large amounts of chitin monomer and dimer, but very low amounts of trimer
-
?
crystalline beta-chitin + H2O
N,N'-diacetylchitobiose + ?
the enzyme degrades the chitin from the non-reducing end
-
-
?
crystalline beta-chitin + H2O
N,N'-diacetylchitobiose + ?
the enzyme degrades the chitin from the non-reducing end
-
-
?
glycol chitin + H2O
?
-
-
-
?
glycol chitin + H2O
?
-
-
-
?
high molecular weight chitin + H2O
?
-
90% activity compared to colloidal chitin
-
-
?
high molecular weight chitin + H2O
?
-
90% activity compared to colloidal chitin
-
-
?
moderate molecular weight chitin + H2O
?
-
40% activity compared to colloidal chitin
-
-
?
moderate molecular weight chitin + H2O
?
-
40% activity compared to colloidal chitin
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N'',N'''-tetraacetylchitotetraose
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N'',N'''-tetraacetylchitotetraose
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N'',N'''-tetraacetylchitotetraose
-
-
-
?
N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
N,N'-diacetylchitobiose + 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
-
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
2 N,N'-diacetylchitobiose
-
sole product
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
2 N,N'-diacetylchitobiose
-
sole product
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
2 N,N'-diacetylchitobiose
-
-
-
?
additional information
?
-
the enzyme hydrolyzes N-acetylglucosamine oligomers producing dimers from the nonreducing end of the substrates. It shows predominantly exo-splitting mode, but contains a slight endo-splitting activity and catalyzes an anomeric retention reaction. The enzyme catalyzes transglycosylation reaction in a low efficiency
-
-
?
additional information
?
-
-
no activity with low molecular weight chitin. The enzyme is not active on rice bran, rice straw, corn stalks, corn leaves and bagasse
-
-
?
additional information
?
-
-
no activity with low molecular weight chitin. The enzyme is not active on rice bran, rice straw, corn stalks, corn leaves and bagasse
-
-
?
additional information
?
-
the enzmye preferentially hydrolyzes the second glycosidic link from the non-reducing end of (GlcNAc)n
-
-
?
additional information
?
-
-
no activity with chitobiose and 4-nitrophenyl-N-acetylglucosamine
-
-
?
additional information
?
-
ChiB is an exoenzyme which degrades the polymer chains from their nonreducing ends. The degradation of chitosan with 65% acetylated units showed biphasic kinetics: the faster phase is dominated by cleavage on the reducing side of two acetylated units (occupying subsites -2 and -1), while the slower kinetic phase reflects cleavage on the reducing side of a deacetylated and an acetylated unit (bound to subsites -2 and -1, respectively). The enzyme does not show preferences with respect to acetylation of the sugar bound in the +1 subsite. Even chitosans with low degrees of acetylation can be degraded by ChiB
-
-
?
additional information
?
-
-
processive enzyme, in which the substrate remains bound to the active cleft after successful hydrolysis and is moved along for the next hydrolysis to occur. ChiB performs on average 3.4 cleavages, for the formation of each enzyme-substrate complex. The exo-type of activity observed for ChiB during the degradation of solid crystalline chitin is due to the better accessibility of chain ends. When hydrolyzing soluble substrates, ChiB operates in a processive endo-attack mode of action
-
-
?
additional information
?
-
no activity with N,N',N''-triacetylchitotriose
-
-
?
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Tanaka, T.; Fukui, T.; Imanaka, T.
Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
J. Biol. Chem.
276
35629-35635
2001
Thermococcus kodakarensis (Q9UWR7)
brenda
Ohnuma, T.; Numata, T.; Osawa, T.; Mizuhara, M.; Lampela, O.; Juffer, A.H.; Skriver, K.; Fukamizo, T.
A class V chitinase from Arabidopsis thaliana: gene responses, enzymatic properties, and crystallographic analysis
Planta
234
123-137
2011
Arabidopsis thaliana (O81862)
brenda
Gao, J.; Bauer, M.W.; Shockley, K.R.; Pysz, M.A.; Kelly, R.M.
Growth of hyperthermophilic archaeon Pyrococcus furiosus on chitin involves two family 18 chitinases
Appl. Environ. Microbiol.
69
3119-3128
2003
Pyrococcus furiosus
brenda
Hult, E.L.; Katouno, F.; Uchiyama, T.; Watanabe, T.; Sugiyama, J.
Molecular directionality in crystalline beta-chitin: hydrolysis by chitinases A and B from Serratia marcescens 2170
Biochem. J.
388
851-856
2005
Serratia marcescens (P11797), Serratia marcescens 2170 (P11797)
brenda
Sikorski, P.; Sorbotten, A.; Horn, S.J.; Eijsink, V.G.; Varum, K.M.
Serratia marcescens chitinases with tunnel-shaped substrate-binding grooves show endo activity and different degrees of processivity during enzymatic hydrolysis of chitosan
Biochemistry
45
9566-9574
2006
Serratia marcescens
brenda
Gutierrez-Roman, M.; Holguin-Melendez, F.; Dunn, M.; Guillen-Navarro, K.; Huerta-Palacios, G.
Antifungal activity of Serratia marcescens CFFSUR-B2 purified chitinolytic enzymes and prodigiosin against Mycosphaerella fijiensis, causal agent of black Sigatoka in banana (Musa spp.)
BioControl
60
565-572
2015
Serratia marcescens (R9WYJ0), Serratia marcescens CFFSUR-B2 (R9WYJ0)
-
brenda
Sorbotten, A.; Horn, S.J.; Eijsink, V.G.; Varum, K.M.
Degradation of chitosans with chitinase B from Serratia marcescens. Production of chito-oligosaccharides and insight into enzyme processivity
FEBS J.
272
538-549
2005
Serratia marcescens (Q54276)
brenda
Howard, M.B.; Ekborg, N.A.; Taylor, L.E.; Weiner, R.M.; Hutcheson, S.W.
Chitinase B of "Microbulbifer degradans" 2-40 contains two catalytic domains with different chitinolytic activities
J. Bacteriol.
186
1297-1303
2004
Saccharophagus degradans (Q7PC53), Saccharophagus degradans DSM 17024 (Q7PC53)
brenda
Woytowich, A.E.; Selvaraj, G.; Khachatourians, G.G.
Analysis of the chiB gene of Serratia liquefaciens
J. Biotechnol.
80
277-283
2000
Serratia liquefaciens (Q8KWS2)
brenda
Gutierrez-Roman, M.I.; Dunn, M.F.; Tinoco-Valencia, R.; Holguin-Melendez, F.; Huerta-Palacios, G.; Guillen-Navarro, K.
Potentiation of the synergistic activities of chitinases ChiA, ChiB and ChiC from Serratia marcescens CFFSUR-B2 by chitobiase (Chb) and chitin binding protein (CBP)
World J. Microbiol. Biotechnol.
30
33-42
2014
Serratia marcescens (R9WYJ0), Serratia marcescens CFFSUR-B2 (R9WYJ0)
brenda
Hamre, A.G.; Froberg, E.E.; Eijsink, V.G.H.; Sorlie, M.
Thermodynamics of tunnel formation upon substrate binding in a processive glycoside hydrolase
Arch. Biochem. Biophys.
620
35-42
2017
Serratia marcescens (P11797)
brenda
Koseki, J.; Gouda, H.; Hirono, S.
Molecular orbital study of the formation of intramolecular hydrogen bonding of a ligand molecule in a protein aromatic hydrophobic pocket
Chem. Pharm. Bull.
64
1031-1035
2016
Serratia marcescens (P11797)
brenda
Sugimoto, H.; Nakamura, K.; Nishino, Y.; Idezawa, Y.; Fujinuma, A.; Suzuki, K.; Watanabe, T.
Differences in the roles of the two surface-exposed tyrosine residues, Y240 and Y481, of Serratia marcescens chitinase B during processive degradation of crystalline chitin
J. Gen. Appl. Microbiol.
61
255-261
2016
Serratia marcescens (P11797), Serratia marcescens 2170 (P11797)
brenda
Gaber, Y.; Mekasha, S.; Vaaje-Kolstad, G.; Eijsink, V.G.H.; Fraaije, M.W.
Characterization of a chitinase from the cellulolytic actinomycete Thermobifida fusca
Biochim. Biophys. Acta
1864
1253-1259
2016
Thermobifida fusca (Q47RL1)
brenda
Kumar, M.; Brar, A.; Vivekanand, V.; Pareek, N.
Production of chitinase from thermophilic Humicola grisea and its application in production of bioactive chitooligosaccharides
Int. J. Biol. Macromol.
104
1641-1647
2017
Trichocladium griseum, Trichocladium griseum ITCC 10,360.16
brenda
Shehata, A.; Abd El Aty, A.; Darwish, D.; Abdel Wahab, W.; Mostafa, F.
Purification, physicochemical and thermodynamic studies of antifungal chitinase with production of bioactive chitosan-oligosaccharide from newly isolated Aspergillus griseoaurantiacus KX010988
Int. J. Biol. Macromol.
107
990-999
2018
Aspergillus griseoaurantiacus, Aspergillus griseoaurantiacus KX010988
brenda
Laribi-Habchi, H.; Bouanane-Darenfed, A.; Drouiche, N.; Pauss, A.; Mameri, N.
Purification, characterization, and molecular cloning of an extracellular chitinase from Bacillus licheniformis stain LHH100 isolated from wastewater samples in Algeria
Int. J. Biol. Macromol.
72
1117-1128
2015
Bacillus licheniformis (A0A0G2QUN1)
brenda
Kabir, S.; Rahman, M.; Tasnim, S.; Karim, M.; Khatun, N.; Hasan, I.; Amin, R.; Islam, S.; Nurujjaman, M.; Kabir, A.; Sana, N.; Ozeki, Y.; Asaduzzaman, A.
Purification and characterization of a novel chitinase from Trichosanthes dioica seed with antifungal activity
Int. J. Biol. Macromol.
84
62-68
2016
Trichosanthes dioica
brenda
Jitonnom, J.; Sattayanon, C.; Kungwan, N.; Hannongbua, S.
A DFT study of the unusual substrate-assisted mechanism of Serratia marcescens chitinase B reveals the role of solvent and mutational effect on catalysis
J. Mol. Graph. Model.
56
53-59
2015
Serratia marcescens (P11797)
brenda