Analysis of productive binding modes in the human chitotriosidase
- 11 September 2013
- journal article
- Published by Wiley in FEBS Letters
- Vol. 587 (21), 3508-3513
- https://doi.org/10.1016/j.febslet.2013.09.004
Abstract
Human chitotriosidase (HCHT) is a family 18 chitinase that is an innate part of the immune system. We have mapped preferred productive binding modes of chito-oligosaccharide substrates to HCHT and the data show that HCHT has strong binding affinity in the +3 subsite. Moreover, HCHT shows anomer-specific binding affinities in subsites +2 and +3. These features could endorse HCHT with higher endo-activity and a higher transglycosylation potentialKeywords
Funding Information
- Norwegian Research Council (164653/V40, 178428/V40, 209335/F20, 177542/V30)
This publication has 34 references indexed in Scilit:
- Mutational Effects on Transglycosylating Activity of Family 18 Chitinases and Construction of a Hypertransglycosylating MutantBiochemistry, 2011
- Signatures of activation parameters reveal substrate-dependent rate determining steps in polysaccharide turnover by a family 18 chitinaseCarbohydrate Polymers, 2010
- The Roles of Three Serratia marcescens Chitinases in Chitin Conversion Are Reflected in Different Thermodynamic Signatures of Allosamidin BindingThe Journal of Physical Chemistry B, 2010
- Aromatic Residues in the Catalytic Center of Chitinase A from Serratia marcescens Affect Processivity, Enzyme Activity, and Biomass Converting EfficiencyJournal of Biological Chemistry, 2009
- Triad of polar residues implicated in pH specificity of acidic mammalian chitinaseProtein Science, 2009
- TLR‐ and NOD2‐dependent regulation of human phagocyte‐specific chitotriosidaseFEBS Letters, 2007
- Costs and benefits of processivity in enzymatic degradation of recalcitrant polysaccharidesProceedings of the National Academy of Sciences, 2006
- Serratia marcescens Chitinases with Tunnel-Shaped Substrate-Binding Grooves Show Endo Activity and Different Degrees of Processivity during Enzymatic Hydrolysis of ChitosanBiochemistry, 2006
- Chitinases and chitinase-like proteins in TH2 inflammation and asthmaJournal of Allergy and Clinical Immunology, 2005
- Molecular directionality in crystalline β-chitin: hydrolysis by chitinases A and B from Serratia marcescens 2170Biochemical Journal, 2005