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 Role of Cysteine Residues in Catalysis of Phosphoenolpyruvate Carboxykinase from Mycobacterium tuberculosis.

PloS one - 1 Jan 2017

Machová Iva, Hubálek Martin, Lepšík Martin, Bednárová Lucie, Pazderková Markéta, Kopecký Vladimír, Snášel Jan, Dostál Jiří, Pichová Iva

Abstract excerpt

Mycobacterium tuberculosis (MTb), the causative agent of tuberculosis, can persist in macrophages for decades, maintaining its basic metabolic activities. Phosphoenolpyruvate carboxykinase (Pck; EC 4.1.1.32) is a key player in central carbon metabolism regulation. In replicating MTb, Pck is associated with gluconeogenesis, but in non-replicating MTb, it also catalyzes the reverse anaplerotic reaction. Here, we...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Biocatalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cysteine

Share to Disulfides

Share to Enzyme Stability

Share to Mutant Proteins

Share to Mycobacterium tuberculosis

Share to Tandem Mass Spectrometry

Source

Open in PubMed Open full text

Identifiers

PMID: 28135343
DOI: 10.1371/journal.pone.0170373
PMCID: PMC5279734

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Role of Cysteine Residues in Catalysis of Phosphoenolpyruvate Carboxykinase from Mycobacterium tuberculosis.PMID 28135343Read ↗

Structural and functional studies of phosphoenolpyruvate carboxykinase from Mycobacterium tuberculosis.Semantic proximity Read ↗

Mycobacterium tuberculosis supports protein tyrosine phosphorylation.Semantic proximity Read ↗

Serine threonine protein kinases of mycobacterial genus: phylogeny to functionSemantic proximity Read ↗

Insight into the structural flexibility and function of Mycobacterium tuberculosis isocitrate lyase.Semantic proximity Read ↗

Oxidative Unfolding of the Rubredoxin Domain and the Natively Disordered N-terminal Region Regulate the Catalytic Activity of Mycobacterium tuberculosis Protein Kinase G.Semantic proximity Read ↗

RD-1 encoded EspJ protein gets phosphorylated prior to affect the growth and intracellular survival of mycobacteria.Semantic proximity Read ↗

Role of Serine140 in the mode of action of Mycobacterium tuberculosis β-ketoacyl-ACP Reductase (MabA).Semantic proximity Read ↗

Understanding the role of PknJ in Mycobacterium tuberculosis: biochemical characterization and identification of novel substrate pyruvate kinase A.Semantic proximity Read ↗

Cellular and structural basis of synthesis of the unique intermediate dehydro-F <sub>420</sub> -0 in mycobacteriaSemantic proximity Read ↗

Phosphorylation of KasB Regulates Virulence and Acid-Fastness in Mycobacterium tuberculosisSemantic proximity Read ↗

Delineating the reaction mechanism of reductase domains of Nonribosomal Peptide Synthetases from mycobacteria.Semantic proximity Read ↗

Mechanistic studies of mycobacterial glycolipid biosynthesis by the mannosyltransferase PimESemantic proximity Read ↗

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