Comparative functional analysis between human and mouse chitotriosidase: Substitution at amino acid 218 modulates the chitinolytic and transglycosylation activity

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00023884%3A_____%2F20%3A00008775" target="_blank" >RIV/00023884:_____/20:00008775 - isvavai.cz</a>
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S0141813020342653#" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0141813020342653#</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.ijbiomac.2020.08.173" target="_blank" >10.1016/j.ijbiomac.2020.08.173</a>

Result language
angličtina
Original language name
Comparative functional analysis between human and mouse chitotriosidase: Substitution at amino acid 218 modulates the chitinolytic and transglycosylation activity
Original language description
Chitotriosidase (Chit1) and acidic mammalian chitinase (AMCase) have been attracting research interest due totheir involvement invariouspathologicalconditions such as Gaucher's disease and asthma,respectively.Both en-zymes are highly expressed in mice, while the level of AMCase mRNA was low in human tissues. In addition, thechitinolytic activity of the recombinant human AMCase was significantly lower than that of the mouse counter-part. Here, we revealed a substantially higher chitinolytic and transglycosylation activity of human Chit1 againstartificial and natural chitin substrates as compared to the mouse enzyme. We found that the substitution of leu-cine (L) by tryptophan (W) at position 218 markedly reduced both activities in human Chit1. Conversely, theL218W substitution in mouse Chit1 increased the activity of the enzyme. These results suggest that Chit1 maycompensate for the low of AMCase activity in humans, while in mice, highly active AMCase may supplementslow Chit1 activity.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30101 - Human genetics

Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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