ArticleProtein science : a publication of the Protein Society2021
Transition metal cation inhibition of Mycobacterium tuberculosis esterase RV0045C.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Shifting Mycobacterial Serine Hydrolase Activity Visualized Using Multi-Layer In-Gel Activity Assays.Molecules (Basel, Switzerland) · 2024Article
- Roles of Lipolytic enzymes inFrontiers in microbiology · 2024Review
- Sequence and Structural Motifs Controlling the Broad Substrate Specificity of the Mycobacterial Hormone-Sensitive Lipase LipN.ACS omega · 2023Article
- RevisitingBiomolecules · 2021Article
- Transition metal cation inhibition of Mycobacterium tuberculosis esterase RV0045C.Protein science : a publication of the Protein Society · 2021Article
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Authors and funding
11 authors.
Funding
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Abstract
Mycobacterium tuberculosis virulence is highly metal-dependent with metal availability modulating the shift from the dormant to active states of M. tuberculosis infection. Rv0045c from M. tuberculosis is a proposed metabolic serine hydrolase whose folded stability is dependent on divalent metal concentration. Herein, we measured the divalent metal inhibition profile of the enzymatic activity of Rv0045c and found specific divalent transition metal cations (Cu
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