Protein acetylation on 2-isopropylmalate synthase from Thermus thermophilus HB27
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Summary
The present results suggest that leucine biosynthesis is regulated by post-translational protein modifications, in addition to feedback inhibition/repression, and that metabolic enzymes are regulated by protein acetylation in T. thermophilus.
- Type
- article
- Published
- 2019-03-27
- Cited by
- 6
- References
- 51
- OpenAlex
- https://openalex.org/W2924775120
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:85527794
Keywords
Thermus thermophilus, Acetylation, Lysine, Biochemistry, Biology
References
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- Amino-acid substitutions at the domain interface affect substrate and allosteric inhibitor binding in α-isopropylmalate synthase from Mycobacterium tuberculosis.
- Lysine Propionylation Is a Prevalent Post-translational Modification in Thermus thermophilus
- Structural and functional characterization of α-isopropylmalate synthase and citramalate synthase, members of the LeuA dimer superfamily.
- Allosteric Regulation of a Protein Acetyltransferase in Micromonospora aurantiaca by the Amino Acids Cysteine and Arginine*
- Subdomain II of α-Isopropylmalate Synthase Is Essential for Activity
- Crystal structure of LeuA from Mycobacterium tuberculosis, a key enzyme in leucine biosynthesis.
- Absolute Metabolite Concentrations and Implied Enzyme Active Site Occupancy in Escherichia coli
- Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions
- Structural, Kinetic and Proteomic Characterization of Acetyl Phosphate-Dependent Bacterial Protein Acetylation
- A link between transcription and intermediary metabolism: a role for Sir2 in the control of acetyl-coenzyme A synthetase.
- Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica.
- Mapping of the allosteric network in the regulation of alpha-isopropylmalate synthase from Mycobacterium tuberculosis by the feedback inhibitor L-leucine: solution-phase H/D exchange monitored by FT-ICR mass spectrometry.
- Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability.
- Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
Cited by
- Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions
- Comparative genomic analysis between newly sequenced Brucella abortus vaccine strain A19 and another Brucella abortus vaccine S19.
- Characterizing the Effect of the Lysine Deacetylation Modification on Enzyme Activity of Pyruvate Kinase I and Pathogenicity of Vibrio alginolyticus
- Recent Contributions of Proteomics to Our Understanding of Reversible Nε-Lysine Acylation in Bacteria
- Antibacterial Ingredients and Modes of the Methanol-Phase Extract from the Fruit of Amomum villosum Lour.
- Catalytic regulation of CoA transferase by an NAD+-sensing accessory protein and protein acetylation
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