ArticleThe Journal of biological chemistry2009
Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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49 citing papers in PubMed, 163 citations in OpenAlex.
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- Microbial chitinases in the plant holobiont: ecological roles and structural determinants.FEMS microbiology reviews · 2026Review
- The energetic landscape of CH-π interactions in protein-carbohydrate binding.Chemical science · 2025Article
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- Enhancing the endo-activity of the thermophilic chitinase to yield chitooligosaccharides with high degrees of polymerization.Bioresources and bioprocessing · 2024Article
- PbrChiA: a key chitinase of pear in response toHorticulture research · 2023Article
- The evolutionary advantage of an aromatic clamp in plant family 3 glycoside exo-hydrolases.Nature communications · 2022Article
- Structural inspection and protein motions modelling of a fungal glycoside hydrolase family 18 chitinase by crystallography depicts a dynamic enzymatic mechanism.Computational and structural biotechnology journal · 2021Article
- Efficient Preparation of Chitooligosaccharide With a Potential Chitosanase Csn-SH and Its Application for Fungi Disease Protection.Frontiers in microbiology · 2021Article
- Combined Approach to Engineer a Highly Active Mutant of Processive Chitinase Hydrolyzing Crystalline Chitin.ACS omega · 2020Article
- Enzymatic processing of lignocellulosic biomass: principles, recent advances and perspectives.Journal of industrial microbiology & biotechnology · 2020Review
- A trimodular bacterial enzyme combining hydrolytic activity with oxidative glycosidic bond cleavage efficiently degrades chitin.The Journal of biological chemistry · 2020Article
- Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation.Nature communications · 2020Article
- Single-molecule imaging analysis reveals the mechanism of a high-catalytic-activity mutant of chitinase A fromThe Journal of biological chemistry · 2020Article
- Substrate binding in the processive cellulase Cel7A: Transition state of complexation and roles of conserved tryptophan residues.The Journal of biological chemistry · 2020Article
- Enzymatic Modification of Native Chitin and Conversion to Specialty Chemical Products.Marine drugs · 2020Review
- Crystalline chitin hydrolase is a burnt-bridge Brownian motor.Biophysics and physicobiology · 2020Article
- The crystal structure of the chitinase ChiA74 of Bacillus thuringiensis has a multidomain assembly.Scientific reports · 2019Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The processive Serratia marcescens chitinases A (ChiA) and B (ChiB) are thought to degrade chitin in the opposite directions. A recent study of ChiB suggested that processivity is governed by aromatic residues in the +1 and +2 (aglycon) subsites close to the catalytic center. To further investigate the roles of aromatic residues in processivity and to gain insight into the structural basis of directionality, we have mutated Trp(167), Trp(275), and Phe(396) in the -3, +1, and +2 subsites of ChiA, respectively, and characterized the hydrolytic activities of the mutants toward beta-chitin and the soluble chitin-derivative chitosan. Although the W275A and F396A mutants showed only modest reductions in processivity, it was almost abolished by the W167A mutation. Thus, although aglycon subsites seem to steer processivity in ChiB, a glycon (-3) subsite seems to be adapted to do so in ChiA, in line with the notion that the two enzymes have different directionalities. Remarkably, whereas all three single mutants and the W167A/W275A double mutant showed reduced efficiency toward chitin, they showed up to 20-fold higher activities toward chitosan. These results show that the processive mechanism is essential for an efficient conversion of crystalline substrates but comes at a large cost in terms of intrinsic enzyme speed. This needs to be taken into account when devising enzymatic strategies for biomass turnover.
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