Abstract
Humans do not synthesize chitin, yet they produce a number of active and inactive chitinases. One of the active enzymes is chitotriosidase whose serum levels are elevated in a number of diseases such as Gaucher's disease and upon fungal infection. Since the biological role of chitotriosidase in disease pathogenesis is not understood we screened a panel of mammalian GlcNAc-containing glycoconjugates as alternate substrates. LacNAc and LacdiNAc-terminating substrates are hydrolyzed, the latter with a turnover comparable to that of pNP-chitotriose. Glycolipids or glycoproteins with LacNAc and LacdiNAc represent potential chitinase substrates and the subsequent alteration of glycosylation pattern could be a factor in disease pathogenesis.
Original language | English |
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Journal | F E B S Letters |
Volume | 588 |
Issue number | 5 |
Pages (from-to) | 746-751 |
Number of pages | 6 |
ISSN | 0014-5793 |
DOIs | |
Publication status | Published - 3 Mar 2014 |
Keywords
- Faculty of Health and Medical Sciences
- Chitinases
- Family 18 glycosidases
- Kinetics
- GlcNAc-containing substrates
- Glycoconjugates
- LacNAc
- LacdiNac