The Mycobacterium tuberculosis prolyl dipeptidyl peptidase cleaves the N-terminal peptide of the immunoprotein CXCL-10.
Biol Chem
; 404(6): 633-643, 2023 05 25.
Article
in En
| MEDLINE
| ID: mdl-36632703
ABSTRACT
Dipeptidyl peptidases constitute a class of non-classical serine proteases that regulate an array of biological functions, making them pharmacologically attractive enzymes. With this work, we identified and characterized a dipeptidyl peptidase from Mycobacterium tuberculosis (MtDPP) displaying a strong preference for proline residues at the P1 substrate position and an unexpectedly high thermal stability. MtDPP was also characterized with alanine replacements of residues of its active site that yielded, for the most part, loss of catalysis. We show that MtDPP catalytic activity is inhibited by well-known human DPP4 inhibitors. Using MALDI-TOF mass spectrometry we also describe that in vitro, MtDPP mediates the truncation of the C-X-C motif chemokine ligand 10, indicating a plausible role in immune modulation for this mycobacterial enzyme.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
/
Mycobacterium tuberculosis
Limits:
Humans
Language:
En
Journal:
Biol Chem
Journal subject:
BIOQUIMICA
Year:
2023
Document type:
Article