UNASSIGNED: Insect chitinases are involved in degradation of chitin from the exoskeleton or peritrophic metrix of midgut. In @entity9222 , two duplicated Cht5s (LmCht5-1 and LmCht5-2) have been shown to have distinct molecular characteristics and biological roles. To explore the protein properties of the two LmCht5s, we heterologously expressed both enzymes using baculovirus expression system in SF9 cells, and characterized kinetic and @entity1735 -binding properties of purified enzymes. LmCht5-1 and LmCht5-2 exhibited similar pH and temperature optimums. LmCht5-1 has lower Km value for the oligomeric substrate ( @entity61878 )3 ), and higher Km value for the longer substrate (CM-Chitin-RBV) compared with LmCht5-2. A comparison of @entity3534 and homology modeling of catalytic domain presented similar TIM barrel structure and differentiated @entity3534 between two proteins. LmCht5-1 has a CBD bound to colloidal chitin tightly, but LmCht5-2 does not have a CBD for binding to colloidal chitin. Our results suggested both LmCht5-1 and LmCht5-2, which have the critical @entity3264 residue in region II of catalytic domain, exhibited chitinolytic activity cleaving both polymeric and oligomeric substrates. LmCht5-1 had relatively higher activity against the oligomeric substrate, @entity61878 3 , whereas LmCht5-2 exhibited higher activity towards the longer substrate, CM-Chitin-RBV. These findings are helpful for further research to clarify their different roles in insect growth and development. This article is protected by copyright. All rights reserved.

Heterologous expression and characterization of two chitinase 5 enzymes from the XXXX @entity9222 .

@entity3534 :: ('MESH:D000596', 'Chemical') :: ['amino acids'] @entity61878 :: ('MESH:C025158', 'Chemical') :: ['4MU-(GlcNAc)', '4MU-(GlcNAc'] @entity3264 :: ('D018698', 'Chemical') :: ['glutamate'] @entity1735 :: ('CHEBI:16646', 'Chemical') :: ['carbohydrate'] @entity9222 :: ('7004', 'Species') :: ['Locusta migratoria']
@entity9222 :: (7004,Species) :: ['migratory locust']
