Oxidation of the Mycobacterium tuberculosis key virulence factor protein tyrosine phosphatase A (MptpA) reduces its phosphatase activity.
Mycobacterium tuberculosis
cysteine-redox regulation
nuclear magnetic resonance spectroscopy
protein oxidation
protein tyrosine phosphatase
reactive oxygen species
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
06 2022
06 2022
Historique:
revised:
31
03
2022
received:
01
03
2022
accepted:
01
04
2022
pubmed:
10
4
2022
medline:
30
6
2022
entrez:
9
4
2022
Statut:
ppublish
Résumé
The Mycobacterium tuberculosis tyrosine-specific phosphatase MptpA and its cognate kinase PtkA are prospective targets for anti-tuberculosis drugs as they interact with the host defense response within the macrophages. Although both are structurally well-characterized, the functional mechanism regulating their activity remains poorly understood. Here, we investigate the effect of post-translational oxidation in regulating the function of MptpA. Treatment of MptpA with H
Identifiants
pubmed: 35397176
doi: 10.1002/1873-3468.14348
doi:
Substances chimiques
Bacterial Proteins
0
MptpA protein, Mycobacterium tuberculosis
0
Virulence Factors
0
Tyrosine
42HK56048U
Protein Tyrosine Phosphatases
EC 3.1.3.48
Cysteine
K848JZ4886
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1503-1515Informations de copyright
© 2022 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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