The enzyme hydrolyses the second glycosidic (1->4) linkage from reducing ends of chitin and chitodextrin molecules, liberating N,N'-diacetylchitobiose disaccharides. cf. EC 3.2.1.200, exo-chitinase (non-reducing end).
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
The enzyme hydrolyses the second glycosidic (1->4) linkage from reducing ends of chitin and chitodextrin molecules, liberating N,N'-diacetylchitobiose disaccharides. cf. EC 3.2.1.200, exo-chitinase (non-reducing end).
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. ChiA performs on average 9.1 cleavages, for the formation of each enzyme-substrate complex. The exo-type of activity observed for ChiA during the degradation of solid crystalline chitin is due to the better accessibility of chain ends. When hydrolyzing soluble substrates, ChiA operates in a processive endo-attack mode of action
enzyme hydrolyzes GlcNAc oligomers longer than (GlcNAc)4. ChiD is an exo-type chitinase that releases (GlcNAc)2 or (GlcNAc)3. ChiD recognizes the reducing end of chitin chains
a tripartite combination of ChiA with ChiB and ChiC exhibits no synergistic effects and produces levels of chitin oligomers similar to that produced by ChiB plus ChiC
digestion of beta-chitin by ChiA occurs from the reducing end to the nonreducing end. Chitinases ChiA and ChiB show synergistic interactions in simultaneous degradation of beta-chitin, but not of glycol chitin
the enzyme has a multidomain structure containing dual catalytic domains and triple chitin-binding domains.The N-terminal catalytic domain mainly hydrolyzes the second glycosidic bond from the nonreducing end of the oligomers, whereas the C-terminal domain randomly hydrolyzes glycosidic bonds other than the first bond from the nonreducing end. Both catalytic domains form diacetylchitobiose as a major end product and possess transglycosylation activity. The N-terminal catalytic domain exclusively liberates diacetylchitobiose, whereas reactions with the C-terminal domain lead to N-acetyl-chitooligosaccharides of various lengths. A synergistic effect is observed when chitin is degraded in the presence of both catalytic domains
digestion of beta-chitin by ChiA occurs from the reducing end to the nonreducing end. Chitinases ChiA and ChiB show synergistic interactions in simultaneous degradation of beta-chitin, but not of glycol chitin
a tripartite combination of ChiA with ChiB and ChiC exhibits no synergistic effects and produces levels of chitin oligomers similar to that produced by ChiB plus ChiC
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ChiA comprises an N-terminal domain, a catalytic (beta/alpha)8 barrel domain and a small (alpha +beta) domain, which is inserted into the (beta/alpha)8 barrel domain. The cocrystallized chito-oligosaccharide is inserted into the catalytic cleft from the reducing end when digested by ChiB
ChiA crystallizes both by salting-in and salting-out in the presence of a variety of precipitating agents in a wide range of concentrations and pH values
ChiA binds nonspecifically polysaccharides, which are found in the growth medium. These sugar impurities have to be removed during the purification process
when applied in combination, a mixture of purified chitinases ChiA, ChiB and ChiC shows a toxic effect similar to that of benzimidazole on ascospore germination of Mycosphaerella fijiensis, causal agent of black Sigatoka in banana
when applied in combination, a mixture of purified chitinases ChiA, ChiB and ChiC shows a toxic effect similar to that of benzimidazole on ascospore germination of Mycosphaerella fijiensis, causal agent of black Sigatoka in banana
Serratia marcescens chitinases with tunnel-shaped substrate-binding grooves show endo activity and different degrees of processivity during enzymatic hydrolysis of chitosan
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.)
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
Potentiation of the synergistic activities of chitinases ChiA, ChiB and ChiC from Serratia marcescens CFFSUR-B2 by chitobiase (Chb) and chitin binding protein (CBP)