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4-methylumbelliferyl GlcNAcbeta(1-4)GlcNAc + H2O
?
-
-
-
?
4-methylumbelliferyl GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
?
-
-
-
?
4-nitrophenyl beta-N,N',N'',N'''-tetraacetylchitotetraoside + H2O
4-nitrophenol + beta-N,N',N'',N'''-tetraacetylchitotetraose
-
-
-
?
4-nitrophenyl beta-N,N',N''-triacetylchitotrioside + H2O
4-nitrophenol + beta-N,N',N''-triacetylchitotriose
-
-
-
?
4-nitrophenyl beta-N,N'-diacetylchitobioside + H2O
4-nitrophenol + beta-N,N'-diacetylchitobiose
-
-
-
?
beta-chitin + H2O
?
substrate 3 micrometer beta-chitin
-
-
?
chitin + H2O
N,N'-diacetylchitobiose + ?
-
-
-
?
chito-oligosaccharides + H2O
?
-
-
-
?
chitopentaose + H2O
?
best substrate
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + ?
the polymer disappears very slowly, while the initially produced oligomers almost exclusively had even-numbered chain lengths in the 212 range. ChiA is a processive chitinase
-
-
?
N,N',N'',N'''-tetraacetylchitotetraose + H2O
?
-
-
-
?
N,N',N''-triacetylchitotriose + H2O
?
-
-
-
?
4-methylumbelliferyl GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc + H2O
4-methylumbelliferone + GlcNAcbeta(1-4)GlcNAcbeta(1-4)GlcNAc
-
-
-
-
?
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside + H2O
?
BJL200-ChiA and BJL200-ChiB have an approximately 30fold higher kcat and 15fold lower Km than BJL200-ChiC1 for the oligomeric substrate
-
-
?
allyl penta-N-acetyl-chitopentaose + H2O
?
-
-
-
-
?
beta-chitin + H2O
?
substrate 3 micrometer beta-chitin
-
-
?
cell wall + H2O
chitin oligosaccharides
-
from yeast
N-acetetylglucosamine and diacetylchitobiose
?
chitin + H2O
N,N'-diacetylchitobiose + ?
-
-
-
?
chitin + H2O
N,N'-diacetylchitobiose + N,N',N''-triacetylchitotriose + N-acetylglucosamine
-
isoform ChiA is the most effective enzyme toward insoluble chitin, isoform ChiC1 is the most effective enzyme toward soluble chitin, ChiA, ChiB and ChiC1 hydrolyze water-soluble chitin very efficiently but powdered chitin is a very poor substrate
(GlcNAc)2 is almost exclusively generated from ChiA, ChiB and ChiC1, ChiA produced as minor products GlcNAc and (GlcNAc)3, ChiB produced as minor product only (GlcNAc)3, ChiC1 produced as minor product only GlcNAc
-
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
chitodecaose + H2O
?
best substrate
-
-
?
chitopentaose + H2O
?
-
-
-
?
CM-chitin-RBV + H2O
?
BJL200-ChiC1 is 10-15times faster than BJL200-ChiB and BJL200-ChiA in degrading the polymeric substrate CM-chitin-RBV
-
-
?
colloidal chitin + H2O
?
-
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + ?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + N,N',N'',N'''-tetraacetylchitotetraose + N,N',N''-triacetylchitotriose
-
-
ChiA almost exclusively generates (GlcNAc)2 and (GlcNAc)4, ChiB and ChiC1 generated all three products
-
?
additional information
?
-
chitin + H2O
?
-
-
-
?
chitin + H2O
?
-
-
-
-
?
chitin + H2O
?
-
crystalline beta-chitin, molecular weight analysis of oligomer products, overview
-
-
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
-
-
-
-
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
-
from ground crab shell
with high ratio of chitinase to chitin N-acetylglucosamine only
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
-
[acetyl-3H]chitin
-
-
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
-
[acetyl-3H]chitin
with high ratio of chitinase to chitin N-acetylglucosamine only
?
chitin + H2O
N,N-diacetylchitobiose + N-acetylglucosamine
-
[acetyl-3H]chitin
diacetylchitobiose only, some trisaccharides in early stages
?
chitosan + H2O
?
-
-
-
-
?
chitosan + H2O
?
-
chitosan with different degrees of deacetylation
-
-
?
chitosan + H2O
?
-
soluble chitin-derivative chitosan, molecular weight analysis of oligomer products, overview
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + ?
ChiC shows rapid disappearance of the polymer and production of a continuum of odd- and even-numbered oligomers. ChiC is a nonprocessive endochitinase
-
-
?
N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose + H2O
N,N'-diacetylchitobiose + ?
the polymer disappears very slowly, while the initially produced oligomers almost exclusively had even-numbered chain lengths in the 212 range. ChiB is a processive chitinase
-
-
?
additional information
?
-
wild-type ChiA and mutant ChiAW167A substrate specificity, product determinations, overview, the enzyme also performs transglycosylation with chito-oligosaccharides as acceptors, overview
-
-
?
additional information
?
-
-
wild-type ChiA and mutant ChiAW167A substrate specificity, product determinations, overview, the enzyme also performs transglycosylation with chito-oligosaccharides as acceptors, overview
-
-
?
additional information
?
-
the enzyme is also active with chitooligosachharides from GlnNAc to GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAc, overview
-
-
?
additional information
?
-
-
the enzyme is also active with chitooligosachharides from GlnNAc to GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAcbeta(1-4)GlnNAc, overview
-
-
?
additional information
?
-
-
isozyme ChiA Nima shows high antibacterial activity against Enterobacter cloacae, Escherichia coli, Staphylococcus aureus and Staphylococcus xylosus, overview
-
-
?
additional information
?
-
-
aromatic residues in the catalytic center of chitinase A affect processivity, enzyme activity, and biomass converting efficiency. Progressivity of isozymes is dependent on the substrate, the processive mechanism is essential for an efficient conversion of crystalline substrates but comes at a large cost in terms of intrinsic enzyme speed, overview
-
-
?
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Cabib, E.; Sburlati, A.
Enzymatic determination of chitin
Methods Enzymol.
161
457-459
1988
Serratia marcescens
-
brenda
Cabib, E.
Assay for chitinase using tritiated chitin
Methods Enzymol.
161
424-426
1988
Serratia marcescens, Triticum aestivum
-
brenda
Cabib, E.
Chitinase from Serratia marcescens
Methods Enzymol.
161
460-462
1988
Serratia marcescens
-
brenda
Ohtakara, A.; Izume, M.; Mitsutomi, M.
Action of microbial chitinases on chitosan with different degrees of deacetylation
Agric. Biol. Chem.
52
3181-3182
1988
Aeromonas hydrophila, Streptomyces sp., Serratia marcescens, Streptomyces antibioticus, Streptomyces griseus
-
brenda
Jones, J.D.G.; Grady, K.L.; Suslow, T.V.; Bedbrook, J.R.
Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens
EMBO J.
5
467-473
1986
Serratia marcescens
brenda
Roberts, R.L.; Cabib, E.
Serratia marcescens chitinase: one-step purification and use for the determination of chitin
Anal. Biochem.
127
402-412
1982
Serratia marcescens
brenda
Watanabe, T.; Kanai, R.; Kawase, T.; Tanabe, T.; Mitsutomi, M.; Sakuda, S.; Miyashita, K.
Family 19 chitinases of Streptomyces species: characterization and distribution
Microbiology
145
3353-3363
1999
Niallia circulans, Streptomyces sp., Serratia marcescens, Streptomyces atrovirens, Streptomyces coelicolor, Streptomyces cyanocolor, Streptomyces eurythermus, Streptomyces griseus, Streptomyces ipomoeae, Streptomyces lividans, Streptomyces plicatus, Streptomyces prasinopilosus, Streptomyces scabiei, Niallia circulans WL12, Streptomyces griseus HUT6037
brenda
Suzuki, K.; Sugawara, N.; Suzuki, M.; Uchiyama, T.; Katouno, F.; Nikaidou, N.; Watanabe, T.
Chitinases A, B, and C1 of Serratia marcescens 2170 produced by recombinant Escherichia coli: enzymatic properties and synergism on chitin degradation
Biosci. Biotechnol. Biochem.
66
1075-1083
2002
Serratia marcescens, Serratia marcescens 2170
brenda
van Aalten, D.M.; Komander, D.; Synstad, B.; Gaseidnes, S.; Peter, M.G.; Eijsink, V.G.
Structural insights into the catalytic mechanism of a family 18 exo-chitinase
Proc. Natl. Acad. Sci. USA
98
8979-8984
2001
Serratia marcescens (P11797), Serratia marcescens
brenda
Huang, G.L.; Zahng, D.W.; Zhao, H.J.; Zhang, H.C.; Wang, P.G.
Chemo-enzymatic synthesis of 1,4-oxazepanyl sugar as potent inhibitor of chitinase
Bioorg. Med. Chem.
14
2446-2449
2006
Serratia marcescens
brenda
Aronson, N.N.Jr.; Halloran, B.A
Alexeyev, M.F.; Zhou, X.E.; Wang, Y.; Meehan, E.J.; Chen, L.: Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation
Biosci. Biotechnol. Biochem.
70
243-251
2006
Serratia marcescens (P07254), Serratia marcescens
brenda
Horn, S.J.; Sorbotten, A.; Synstad, B.; Sikorski, P.; Sorlie, M.; Varum, K.M.; Eijsink, V.G.
Endo/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens
FEBS J.
273
491-503
2006
Serratia marcescens (P07254), Serratia marcescens (P11797), Serratia marcescens (Q068W1), Serratia marcescens
brenda
Zees, A.C.; Pyrpassopoulos, S.; Vorgias, C.E.
Insights into the role of the (alpha+beta) insertion in the TIM-barrel catalytic domain, regarding the stability and the enzymatic activity of chitinase A from Serratia marcescens
Biochim. Biophys. Acta
1794
23-31
2009
Serratia marcescens (P07254), Serratia marcescens
brenda
Gouda, H.; Yanai, Y.; Sugawara, A.; Sunazuka, T.; Omura, S.; Hirono, S.
Computational analysis of the binding affinities of the natural-product cyclopentapeptides argifin and argadin to chitinase B from Serratia marcescens
Bioorg. Med. Chem.
16
3565-3579
2008
Serratia marcescens (P11797), Serratia marcescens
brenda
Synstad, B.; Vaaje-Kolstad, G.; Cederkvist, F.H.; Saua, S.F.; Horn, S.J.; Eijsink, V.G.; Sorlie, M.
Expression and characterization of endochitinase C from Serratia marcescens BJL200 and its purification by a one-step general chitinase purification method
Biosci. Biotechnol. Biochem.
72
715-723
2008
Serratia marcescens (Q700B8), Serratia marcescens, Serratia marcescens BJL200 (Q700B8), Serratia marcescens BJL200
brenda
Barboza-Corona, J.E.; Gutierrez-Acosta, O.B.; Imperial-Cervantes, M.; Bideshi, D.K.; de la Fuente-Salcido, N.; Bautista-Justo, M.; Salcedo-Hernandez, R.
Generation of antibacterial oligosaccharides derived from chitin using heterologous endochitinase synthesized in Escherichia coli
J. Appl. Microbiol.
105
1511-1520
2008
Bacillus thuringiensis, Serratia marcescens
brenda
Zakariassen, H.; Aam, B.B.; Horn, S.J.; Varum, K.M.; Soerlie, M.; Eijsink, V.G.
Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency
J. Biol. Chem.
284
10610-10617
2009
Serratia marcescens, Serratia marcescens BJL200
brenda
Duzhak, A.B.; Panfilova, Z.I.; Duzhak, T.G.; Vasyunina, E.A.
Extracellular chitinases of mutant superproducing strain Serratia marcescens M-1
Biochemistry (Moscow)
74
209-214
2009
Serratia marcescens (P07254), Serratia marcescens (P11797), Serratia marcescens (Q8VQN1), Serratia marcescens
brenda
Babashpour, S.; Aminzadeh, S.; Farrokhi, N.; Karkhane, A.; Haghbeen, K.
Characterization of a chitinase (Chit62) from Serratia marcescens B4A and its efficacy as a bioshield against plant fungal pathogens
Biochem. Genet.
50
722-735
2012
Serratia marcescens (E5FGC5), Serratia marcescens B4A (E5FGC5), Serratia marcescens B4A
brenda
Hamre, A.G.; Eide, K.B.; Wold, H.H.; Sorlie, M.
Activation of enzymatic chitin degradation by a lytic polysaccharide monooxygenase
Carbohydr. Res.
407
166-169
2015
Serratia marcescens (P07254), Serratia marcescens (Q54276)
brenda
Nakagawa, Y.S.; Eijsink, V.G.; Totani, K.; Vaaje-Kolstad, G.
Conversion of alpha-chitin substrates with varying particle size and crystallinity reveals substrate preferences of the chitinases and lytic polysaccharide monooxygenase of Serratia marcescens
J. Agric. Food Chem.
61
11061-11066
2013
Serratia marcescens, Serratia marcescens (P07254), Serratia marcescens (Q54276)
brenda