Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The α/β Hydrolase Fold Proteins of Mycobacterium tuberculosis, with Reference to their Contribution to Virulence

4 Aug 2016

Abstract excerpt

The α/β hydrolase fold superfamily is an ancient and widely diversified group of primarily hydrolytic enzymes. In this review, the adaptations of these proteins to the pathogenic lifestyle of Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, are examined. Of the 105 α/β hydrolases identified in Mtb, many are associated with lipid metabolism, particularly in the biosynthesis and maintenance of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biochemical and Molecular Research
Share to Enzyme Structure and Function
Share to Tuberculosis Research and Epidemiology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 27480283
DOI: 10.2174/1389203717666160729093515

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The α/β Hydrolase Fold Proteins of Mycobacterium tuberculosis, with Reference to their Contribution to VirulencePMID 27480283Read ↗

Roles of Lipolytic enzymes in Mycobacterium tuberculosis pathogenesisSemantic proximity Read ↗

MmPPOX Inhibits Mycobacterium tuberculosis Lipolytic Enzymes Belonging to the Hormone-Sensitive Lipase Family and Alters Mycobacterial GrowthSemantic proximity Read ↗

Lipid hydrolizing enzymes in virulence:<i>Mycobacterium tuberculosis</i>as a model systemSemantic proximity Read ↗

Peptidoglycan Hydrolases RipA and Ami1 Are Critical for Replication and Persistence of Mycobacterium tuberculosis in the Host.Semantic proximity Read ↗

Cell wall peptidoglycan inMycobacterium tuberculosis: An Achilles’ heel for the TB-causing pathogenSemantic proximity Read ↗

Structural Basis for the Strict Substrate Selectivity of the Mycobacterial Hydrolase LipW.Semantic proximity Read ↗

The <em>Mycobacterium tuberculosis</em>: A Silent KillerSemantic proximity Read ↗

Expression and characterization of the protein Rv1399c from Mycobacterium tuberculosis. A novel carboxyl esterase structurally related to the HSL family.Semantic proximity Read ↗

MTB-LysB1:A Novel Endolysin Against Multidrug-Resistant <i>Mycobacterium tuberculosis</i>Semantic proximity Read ↗

Cutinase‐like proteins of <i>Mycobacterium tuberculosis</i> : characterization of their variable enzymatic functions and active site identificationSemantic proximity Read ↗

Exposure of <i>Mycobacterium tuberculosis</i> to human alveolar lining fluid shows temporal and strain-specific adaptation to the lung environmentSemantic proximity Read ↗

Revisiting Anti-tuberculosis Therapeutic Strategies That Target the Peptidoglycan Structure and SynthesisSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.