Comparative functional analysis between human and mouse chitotriosidase: Substitution at amino acid 218 modulates the chitinolytic and transglycosylation activity
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu srovnávací studie, časopisecké články
PubMed
32853624
DOI
10.1016/j.ijbiomac.2020.08.173
PII: S0141-8130(20)34265-3
Knihovny.cz E-zdroje
- Klíčová slova
- Chitinolytic activity, Chitotriosidase, Transglycosylation,
- MeSH
- chitin metabolismus MeSH
- chitinasy genetika metabolismus MeSH
- Escherichia coli genetika růst a vývoj MeSH
- glykosylace MeSH
- hexosaminidasy genetika metabolismus MeSH
- lidé MeSH
- myši MeSH
- regulace genové exprese enzymů MeSH
- rekombinantní proteiny metabolismus MeSH
- substituce aminokyselin * MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- srovnávací studie MeSH
- Názvy látek
- chitin MeSH
- chitinasy MeSH
- chitotriosidase MeSH Prohlížeč
- hexosaminidasy MeSH
- rekombinantní proteiny MeSH
Chitotriosidase (Chit1) and acidic mammalian chitinase (AMCase) have been attracting research interest due to their involvement in various pathological conditions such as Gaucher's disease and asthma, respectively. Both enzymes are highly expressed in mice, while the level of AMCase mRNA was low in human tissues. In addition, the chitinolytic activity of the recombinant human AMCase was significantly lower than that of the mouse counterpart. Here, we revealed a substantially higher chitinolytic and transglycosylation activity of human Chit1 against artificial and natural chitin substrates as compared to the mouse enzyme. We found that the substitution of leucine (L) by tryptophan (W) at position 218 markedly reduced both activities in human Chit1. Conversely, the L218W substitution in mouse Chit1 increased the activity of the enzyme. These results suggest that Chit1 may compensate for the low of AMCase activity in humans, while in mice, highly active AMCase may supplements low Chit1 activity.
Department of Applied Chemistry Kogakuin University Hachioji Tokyo 192 0015 Japan
Department of Chemistry and Life Science Kogakuin University Hachioji Tokyo 192 0015 Japan
Citace poskytuje Crossref.org
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