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Evolutionary Analysis of Dipeptidyl Peptidase I
1Department of Chemistry and Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 113, 1000 Ljubljana, Slovenia.
International Journal of Molecular Sciences
|February 15, 2022
Summary
Human dipeptidyl peptidase I (DPPI) is a cysteine peptidase. This study reveals conserved chloride dependence and varied oligomerization, primarily in Amorphea, shedding light on DPPI evolution.
Area of Science:
- Biochemistry
- Evolutionary Biology
- Molecular Biology
Background:
- Human dipeptidyl peptidase I (DPPI) is a papain-like cysteine peptidase.
- DPPI possesses a unique exclusion domain, enabling its specific activity and homotetramerization.
- Unlike most peptidases in its family, DPPI's oligomeric state is unique, and its activity depends on chloride ions.
Purpose of the Study:
- To investigate the evolutionary history of DPPI.
- To identify structural determinants of DPPI's enzymatic activity and preferences.
- To reconstruct the evolutionary trajectory of DPPI oligomerization.
Main Methods:
- Phylogenetic analysis of 57 DPPI sequences.
- Comparative analysis of amino acid residues and N-glycosylation sites.
- Homology modeling and analysis of subunit contacts.
Main Results:
- DPPI is present in Amorphea, Alveolates, and Giardia.
- Chloride-binding residues are highly conserved, indicating conserved chloride dependence.
- N-glycosylation sites increased in animals, especially vertebrates.
- Oligomerization appears restricted to DPPIs within the Amorphea group.
Conclusions:
- Chloride ion dependence is an evolutionarily conserved trait of DPPI.
- DPPI oligomerization is lineage-specific, predominantly observed in Amorphea.
- Evolutionary analysis provides insights into DPPI's structural and functional diversification.
