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evolution
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BcChi-A is glycoside hydrolase family-19 chitinase lacking loops I, II, IV and V, and a C-terminal loop, which are present in the catalytic domain of plant class I and II chitinases. The phylogenetic relationships of BcChi-A and other GH19 chitinases shows that BcChi-A is closely related to GH19 chitinases from bacteria
evolution
chitinase 2 ia a chitinase family 18 enzyme
evolution
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evolutionary adaptation of soybean to environmental cues, i.e. metal toxicity stress
evolution
phylogenetic analysis reveals the possibility of horizontal gene transfer between bacteria, viruses, and insects. The Chit62 enzyme is clearly grouped with other bacterial chitinases, but with a clear distinction from previously reported Serratia marcescens
evolution
the enzyme belongs to carbohydrate-binding module family 18 and glycoside hydrolase family GH19. Possibly the two proteins class IV chitinase and class IV endochitinase, UniProt IDs Q7XAU6 and O24530, are allelic variants encoded by the same gene
evolution
the enzyme belongs to the glycosyl hydrolase family 18 (GH18) of chitinases
evolution
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the enzyme belongs to the glycosyl hydrolase family GH 18
evolution
the enzyme belongs to the glycosyl hydrolase family GH 19
evolution
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the enzyme belongs to the glycosyl hydrolase family GH18
evolution
the enzyme belongs to the glycosyl hydrolase family GH18
evolution
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the enzyme belongs to the glycosyl hydrolase family GH18
evolution
the enzyme belongs to the glycosyl hydrolase family GH18
evolution
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the enzyme belongs to the glycosyl hydrolase family GH19
evolution
the enzyme belongs to the glycosyl hydrolase family GH23, that also includes goose-type (G-type) lysozymes, peptidoglycan lyases, and peptidoglycan lytic transglycosylases. It has a catalytic domain sequence similar to goose-type (G-type) lysozymes, the unique arrangement of the catalytic residues makes a clear contrast to the other GH23 members and also to inverting GH19 chitinases. Enzyme Ra-ChiC produces alpha-anomers by hydrolyzing beta-1,4-glycosidic linkages, indicating that the enzyme is an inverter like GH family 19 chitinases
evolution
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the enzyme is a glycoside hydrolase family 18 chitinase
evolution
the enzyme is a glycoside hydrolase family 19 plant class IV chitinase. Family GH19 chitinases operate by an inverting glycoside mechanism. Comparison of the crystal structure of this plant class IV chitinase with structures from larger class I and II enzymes suggest that class IV chitinases have evolved to accommodate shorter substrates
evolution
the enzyme is a typical glycoside hydrolase family 18 chitinase
evolution
the enzymes of the operon chiCDEFG belong to the glycosyl hydrolase family GH18, while chiF encodes a polypeptide with two chitin-binding domains, but no catalytic domain
evolution
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the enzyme belongs to the glycosyl hydrolase family GH23, that also includes goose-type (G-type) lysozymes, peptidoglycan lyases, and peptidoglycan lytic transglycosylases. It has a catalytic domain sequence similar to goose-type (G-type) lysozymes, the unique arrangement of the catalytic residues makes a clear contrast to the other GH23 members and also to inverting GH19 chitinases. Enzyme Ra-ChiC produces alpha-anomers by hydrolyzing beta-1,4-glycosidic linkages, indicating that the enzyme is an inverter like GH family 19 chitinases
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evolution
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phylogenetic analysis reveals the possibility of horizontal gene transfer between bacteria, viruses, and insects. The Chit62 enzyme is clearly grouped with other bacterial chitinases, but with a clear distinction from previously reported Serratia marcescens
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evolution
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the enzyme belongs to carbohydrate-binding module family 18 and glycoside hydrolase family GH19. Possibly the two proteins class IV chitinase and class IV endochitinase, UniProt IDs Q7XAU6 and O24530, are allelic variants encoded by the same gene
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evolution
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the enzyme belongs to the glycosyl hydrolase family GH19
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evolution
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the enzyme is a glycoside hydrolase family 19 plant class IV chitinase. Family GH19 chitinases operate by an inverting glycoside mechanism. Comparison of the crystal structure of this plant class IV chitinase with structures from larger class I and II enzymes suggest that class IV chitinases have evolved to accommodate shorter substrates
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evolution
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the enzyme belongs to the glycosyl hydrolase family GH18
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evolution
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the enzymes of the operon chiCDEFG belong to the glycosyl hydrolase family GH18, while chiF encodes a polypeptide with two chitin-binding domains, but no catalytic domain
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evolution
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the enzyme belongs to the glycosyl hydrolase family GH 18
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evolution
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the enzyme belongs to the glycosyl hydrolase family GH18
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malfunction
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insertional inactivation of a chi54 locus in mutant C61Chi54M abolishes growth on chitin as a sole carbon source, enzyme activity is not detected
malfunction
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isozyme YlCts1p deletion results in remarkably reduced extracellular endochitinase activity in the culture supernatant of Yersinia lipolytica and enhanced cell aggregation
malfunction
enzyme deficiency results in abnormal adult cuticle
malfunction
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insertional inactivation of a chi54 locus in mutant C61Chi54M abolishes growth on chitin as a sole carbon source, enzyme activity is not detected
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metabolism
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activities of the individual chitinases are dependent on the metal type as well as the cultivar pointing to their more complex role in plant defense during this type of stress
metabolism
the isozymes encoded by chiCDEFG operon act in a cooperative manner in chitin degradation
metabolism
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the enzyme ChiEn1 acts synergistically with the endochitinase ChiIII to efficiently hydrolyze insoluble chitin polymers
metabolism
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the enzyme ChiEn1 acts synergistically with the endochitinase ChiIII to efficiently hydrolyze insoluble chitin polymers
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metabolism
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the isozymes encoded by chiCDEFG operon act in a cooperative manner in chitin degradation
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physiological function
chitinase can damage eggs of both the root-knot nematode Meloidogyne incognita and the insect Bombyx mori
physiological function
class IV enzymes are optimized for shorter substrates than the class I and II enzymes, or alternatively, they are better suited for action on substrates where only small regions of chitin chain are accessibl. The intact enzyme shows antifungal acivtiy, while the catalytic subunit alone has very low antifungal activity
physiological function
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endochitinases Chi2, Chi22 actively degrade chitinoligomeric substrates. A mutant strain lacking isoforms chi2, chi21, chi22, chi4 is unable to cleave 4-methylumbelliferyl-(GlcNAc)3. Strains containing only Chi4 or Chi21 also show no activity on 4-methylumbelliferyl-(GlcNAc)3. A strain containing only the endochitinase Chi22 has measurable activity against 4-methylumbelliferyl-(GlcNAc)3 when the cells are grown on either GlcNAc or glucose as a carbon source, although less on the glucose carbon source. A strain containing only Chi2 has measurable activity when grown on both glucose and GlcNAc Chi2, Chi21, and Chi4 are each involved in sexual reproduction
physiological function
enzyme consists of a catalytic domain, a fibronectin type III domain, and a chitin binding domain. The catalytic domain with one amino acid in C-terminal region is sufficient for chitinase activity. The C-terminus is important in binduing to shell powder
physiological function
enzyme efficiently degrades cell wall chitin of the phytopathogenic Rhizoctonia solani, Fusarium oxysporum, Sclerotinia sclerotiorum, Valsa sordida, Septoria tritici and Phytophthora sojae
physiological function
enzyme exhibits in vitro antifungal activity against Botrytis cinerea and is able to cryoprotect lactate dehydrogenase against freeze/thaw inactivation
physiological function
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enzyme has potent inhibitory action toward fungal species including Botrytis cinerea, Physalospora piricola, Fusarium oxysporum, and Pythium aphanidermatum
physiological function
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expression of chitinase in Bacillus thuringiensis under the control of a strong promoter and a 5'-mRNA stabilizing sequence leads to markedly elevated chinolytic activity and a diminution of 10-20% in size of the crystals produced. Strains overexpressing chitinase produce fewer viable spores. No change in protease activity is observed depsite teh overproduction of chitinase
physiological function
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purified ChiA enhances the permeability of the peritrophic membrane of larvae of Lepidoptera Bombyx mori and Heliothis virescens and inhibits spore germination and growth of the phytopatogenic fungus Alternaria alternata
physiological function
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BChi14 is functionally implicated in the mechanisms underlying chilling tolerance activated by high CO2 concentrations. The purified endochitinase shows very strong cryoprotective activity against freeze-thaw inactivation of lactate dehydrogenase, but the enzyme has no effect on the inhibition of Botrytis cinerea hyphal growth and no antifreeze activity
physiological function
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ChiA significantly inhibits the spore germination of four species of fungi. The IC50 of ChiA on the spore germination of Penicillium glaucum and Sclerotinia fuckelian are 0.0113 mg/ml and 0.0106 mg/ml, respectively. The crude ChiA protein at 12.6 mU reduced the LC50 of the crystal protein of strain 15A3 against the larvae of Spodoptera exigua and Helicoverpa armigera
physiological function
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chitinase hydrolyzes the beta-1,4 glycosidic bond of chitin, the linear polysaccharide of GlcNAc, to produce chitooligosaccharides
physiological function
chitinases are a group of enzymes capable of hydrolysing the bta-(1,4)-glycosidic bonds of chitin, an essential component of the fungal cell wall, the shells of nematode eggs, and arthropod exoskeletons
physiological function
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chitinases are glycoside hydrolases that catalyze the degradation of chitin, a linear beta-1,4-linked polymer of N-acetylglucosamine
physiological function
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sAMC has a role in conversion of chitin wastes into useful products. It also exhibits antifungal activity against Trichoderma viride, Botrytis cinerea, Fusarium oxysporum and Fusarium solani
physiological function
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the purified enzyme inhibits the growth of fungal phytopathogens belonging to the genera Fusarium, Rhizoctonia and Alternaria
physiological function
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the viral chitinase is involved in the final liquefaction of the infected host larvae
physiological function
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chitinase cleaves the beta-1,4-linkage between N-acetyl-D-glucosamine residues in the linear homopolymer chitin, which is an essential component of yeast and fungal cell walls
physiological function
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chitinolytic enzymes attack chitin contained in the cell walls of plant pathogenic fungi and then impair the growth of fungi living in soil. Biodegradation of shrimp head powder by the chitinase of Bacillus cereus TKU028 is conducive to the growth of strain TKU028 and the coexisting bacteria
physiological function
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plant chitinases are considered to be pathogen related proteins used to defend against invasions such as external fungi and insects attacks, that contain chitins
physiological function
recombinant Pichia pastoris-produced chitinase shows strong lytic activity against Fusarium oxysporum and Phytophthora nicotianae
physiological function
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strain C61 displays antifungal activities in vitro. Purified chitinase inhibits spore germination of multiple pathogens. Culture filtrates of the wild-type Chromobacterium sp. C61 and the mutant C61Chi54TS, that has a higer activity than the wild-type, both produce significant in planta biocontrol activity against rice blast, tomato leaf blight and wheat leaf rust. The enzyme expression might be under under quorum sensing control
physiological function
the active enzyme shows biocontrol features against fungal phytopathogens
physiological function
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the chitinase from the stomach of the red scorpionfish Scorpaena scrofa has bioinsecticidal activity toward cowpea weevil Callosobruchus maculatus
physiological function
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the enzyme exhibits antifungal activity against phytopathogenic and human pathogenic fungi
physiological function
the enzyme has in vitro antifungal activity in healthy maize seeds
physiological function
the enzyme is essential to moulting
physiological function
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the purified antifungal alkaline chitinase exhibits remarkable antifungal activity against pathogenic fungi Aspergillus flavus MTCC 2798 and Aspergillus niger MTCC 9652
physiological function
in presence of lytic polysaccharide monooxygenase Cbp21, the apparent kcat values of chitinases ChiA and ChiB increase 6-9fold, while there is no effect on chitinase ChiC
physiological function
presence of CBP21 increases solubilization of chitin substrates with high degrees of crystallinity when combined with each of the three chitinases ChiA, ChiB, or ChiC, but this synergy is reduced upon decline in crystallinity
physiological function
presence of CBP21 increases solubilization of chitin substrates with high degrees of crystallinity when combined with each of the three chitinases ChiA, ChiB, or ChiC, but this synergy is reduced upon decline in crystallinity. Isoform ChiA shows lowest effects
physiological function
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enzyme inhibits the growth of phytopathogenic fungi like Fusarium oxysporum and Curvularia lunata
physiological function
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the endochitinase of Clonostachys rosea expression in Bacillus amyloliquefaciens enhances the Botrytis cinerea resistance of tomato
physiological function
the enzyme inhibits spore germination and activates plant defense responses
physiological function
the enzyme is required for maintaining the integrity of the cuticle as a compact structure of alternating electron-dense and electron-lucent laminae. The enzyme is required for formation of properly oriented long chitin fibers inside pore canals that are vertically oriented columnar structures, which contribute to the mechanical strength of a lightweight, yet rigid, adult cuticle
physiological function
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chitinolytic enzymes attack chitin contained in the cell walls of plant pathogenic fungi and then impair the growth of fungi living in soil. Biodegradation of shrimp head powder by the chitinase of Bacillus cereus TKU028 is conducive to the growth of strain TKU028 and the coexisting bacteria
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physiological function
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chitinases are glycoside hydrolases that catalyze the degradation of chitin, a linear beta-1,4-linked polymer of N-acetylglucosamine
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physiological function
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the active enzyme shows biocontrol features against fungal phytopathogens
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physiological function
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the purified antifungal alkaline chitinase exhibits remarkable antifungal activity against pathogenic fungi Aspergillus flavus MTCC 2798 and Aspergillus niger MTCC 9652
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physiological function
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the purified enzyme inhibits the growth of fungal phytopathogens belonging to the genera Fusarium, Rhizoctonia and Alternaria
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physiological function
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the enzyme exhibits antifungal activity against phytopathogenic and human pathogenic fungi
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physiological function
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the enzyme inhibits spore germination and activates plant defense responses
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physiological function
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the enzyme has in vitro antifungal activity in healthy maize seeds
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physiological function
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strain C61 displays antifungal activities in vitro. Purified chitinase inhibits spore germination of multiple pathogens. Culture filtrates of the wild-type Chromobacterium sp. C61 and the mutant C61Chi54TS, that has a higer activity than the wild-type, both produce significant in planta biocontrol activity against rice blast, tomato leaf blight and wheat leaf rust. The enzyme expression might be under under quorum sensing control
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physiological function
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enzyme inhibits the growth of phytopathogenic fungi like Fusarium oxysporum and Curvularia lunata
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physiological function
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ChiA significantly inhibits the spore germination of four species of fungi. The IC50 of ChiA on the spore germination of Penicillium glaucum and Sclerotinia fuckelian are 0.0113 mg/ml and 0.0106 mg/ml, respectively. The crude ChiA protein at 12.6 mU reduced the LC50 of the crystal protein of strain 15A3 against the larvae of Spodoptera exigua and Helicoverpa armigera
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additional information
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deletion of four loops likely leads the enzyme to optimize the (beta-1,4-GlcNAc)n hydrolytic reaction rather than hydrolysis of polymeric substrates
additional information
NtChiV is a non-processive enzyme. The aglycon binding site of NtChiV appears to consist of three subsites, +1, +2, and +3. Structural comparison with other family GH-18 chitinases, overview
additional information
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NtChiV is a non-processive enzyme. The aglycon binding site of NtChiV appears to consist of three subsites, +1, +2, and +3. Structural comparison with other family GH-18 chitinases, overview
additional information
at a concentration and pH expected in ripe grapes, no inhibition of wine yeast growth by the chitinase is observed
additional information
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at a concentration and pH expected in ripe grapes, no inhibition of wine yeast growth by the chitinase is observed
additional information
catalytic domain structure with and without bound substrate, structure comparisons and structure-function relationship, overview
additional information
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catalytic domain structure with and without bound substrate, structure comparisons and structure-function relationship, overview
additional information
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chitinases in Glycine max roots specifically respond to different metal types and reveal a polymorphism that coincides with sensitivity to metal toxicity
additional information
Glu691 and Glu1177 in the two GH-18 domains are catalytic residues, two catalytic domains act synergistically to degrade chitin. The reaction mechanism of ChiW is suggested to be similar to the mechanism of GH-18 chitinases, in which one glutamate residue functions as a general acid/base catalyst and a GlcNAc C-2 acetamide group of the chitin substrate at subsite -1 carries out a nucleophilic attack on the GlcNAc C-1 carbon atom generating an oxazoline ion intermediate. Other important residues of the chitinase subfamily A enzymes for saccharide binding and catalytic reaction are also highly conserved in the ChiW GH-18 domains: Trp568 (Trp1055), Trp905 (Trp1396), Trp652 (Trp1138), and Trp772 (Trp1258) for saccharide binding, Tyr766 (Tyr1252), Asp687 (Asp1173), and Asp689 (Asp1175) for the catalytic reaction
additional information
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Glu691 and Glu1177 in the two GH-18 domains are catalytic residues, two catalytic domains act synergistically to degrade chitin. The reaction mechanism of ChiW is suggested to be similar to the mechanism of GH-18 chitinases, in which one glutamate residue functions as a general acid/base catalyst and a GlcNAc C-2 acetamide group of the chitin substrate at subsite -1 carries out a nucleophilic attack on the GlcNAc C-1 carbon atom generating an oxazoline ion intermediate. Other important residues of the chitinase subfamily A enzymes for saccharide binding and catalytic reaction are also highly conserved in the ChiW GH-18 domains: Trp568 (Trp1055), Trp905 (Trp1396), Trp652 (Trp1138), and Trp772 (Trp1258) for saccharide binding, Tyr766 (Tyr1252), Asp687 (Asp1173), and Asp689 (Asp1175) for the catalytic reaction
additional information
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isozyme YlCts1p contains an N-terminal secretion signal peptide, a long C-terminal Ser/Thr-rich domain, and a chitin-binding domain
additional information
key roles for Glu62, Arg177, and Glu165 in hydrolysis, and for Ser103 and Tyr106 in substrate binding. Glu62 is directly involved in catalysis, while the hevein-like domain is not needed for enzyme activity. Proton donor and general base are Glu62 and Glu71, respectively. The catalytic triad highly conserved in GH19 chitinases, is composed of Glu62, Arg177, and Glu165
additional information
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key roles for Glu62, Arg177, and Glu165 in hydrolysis, and for Ser103 and Tyr106 in substrate binding. Glu62 is directly involved in catalysis, while the hevein-like domain is not needed for enzyme activity. Proton donor and general base are Glu62 and Glu71, respectively. The catalytic triad highly conserved in GH19 chitinases, is composed of Glu62, Arg177, and Glu165
additional information
structure-function analysis, highly conserved Glu141 acts as a catalytic acid, and Asp226 located at the roof of the tunnel activates a water molecule as a catalytic base, Asp226 is critical for catalysis
additional information
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structure-function analysis, highly conserved Glu141 acts as a catalytic acid, and Asp226 located at the roof of the tunnel activates a water molecule as a catalytic base, Asp226 is critical for catalysis
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additional information
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at a concentration and pH expected in ripe grapes, no inhibition of wine yeast growth by the chitinase is observed
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additional information
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key roles for Glu62, Arg177, and Glu165 in hydrolysis, and for Ser103 and Tyr106 in substrate binding. Glu62 is directly involved in catalysis, while the hevein-like domain is not needed for enzyme activity. Proton donor and general base are Glu62 and Glu71, respectively. The catalytic triad highly conserved in GH19 chitinases, is composed of Glu62, Arg177, and Glu165
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