Search Results - "Bulloch, Esther M. M."
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Poly-γ-glutamylation of biomolecules
Published in Nature communications (12-02-2024)“…Poly-γ-glutamate tails are a distinctive feature of archaeal, bacterial, and eukaryotic cofactors, including the folates and F 420 . Despite decades of…”
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Implications of Binding Mode and Active Site Flexibility for Inhibitor Potency against the Salicylate Synthase from Mycobacterium tuberculosis
Published in Biochemistry (Easton) (19-06-2012)“…MbtI is the salicylate synthase that catalyzes the first committed step in the synthesis of the iron chelating compound mycobactin in Mycobacterium…”
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3
The Substrate Capture Mechanism of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Provides a Mode for Inhibition
Published in Biochemistry (Easton) (12-03-2013)“…Anthranilate phosphoribosyltransferase (AnPRT, EC 2.4.2.18) is a homodimeric enzyme that catalyzes the reaction between 5′-phosphoribosyl 1′-pyrophosphate…”
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4
Protein domain definition should allow for conditional disorder
Published in Protein science (01-11-2013)“…: Proteins are often classified in a binary fashion as either structured or disordered. However this approach has several deficits. Firstly, protein folding is…”
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Alternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis
Published in Biochemical journal (01-07-2014)“…AnPRT (anthranilate phosphoribosyltransferase), required for the biosynthesis of tryptophan, is essential for the virulence of Mycobacterium tuberculosis…”
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Transient Dimerization of Human MxA Promotes GTP Hydrolysis, Resulting in a Mechanical Power Stroke
Published in Structure (London) (07-10-2014)“…Myxovirus resistance (Mx) proteins restrict replication of numerous viruses. They are closely related to membrane-remodeling fission GTPases, such as dynamin…”
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Identification of Histone Demethylases in Saccharomyces cerevisiae
Published in The Journal of biological chemistry (11-05-2007)“…Based on the prediction that histone lysine demethylases may contain the JmjC domain, we examined the methylation patterns of five knock-out strains (ecm5Δ,…”
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Structural Analysis of the Menangle Virus P Protein Reveals a Soft Boundary between Ordered and Disordered Regions
Published in Viruses (31-08-2021)“…The paramyxoviral phosphoprotein (P protein) is the non-catalytic subunit of the viral RNA polymerase, and coordinates many of the molecular interactions…”
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Structural Views along the Mycobacterium tuberculosis MenD Reaction Pathway Illuminate Key Aspects of Thiamin Diphosphate-Dependent Enzyme Mechanisms
Published in Structure (London) (06-07-2016)“…Menaquinone (MQ) is an essential component of the respiratory chains of many pathogenic organisms, including Mycobacterium tuberculosis (Mtb). The first…”
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Inhibition Studies of Mycobacterium tuberculosis Salicylate Synthase (MbtI)
Published in ChemMedChem (05-07-2010)“…Mycobacterium tuberculosis salicylate synthase (MbtI), a member of the chorismate‐utilizing enzyme family, catalyses the first committed step in the…”
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Removal of the C-Terminal Regulatory Domain of α-Isopropylmalate Synthase Disrupts Functional Substrate Binding
Published in Biochemistry (Easton) (20-03-2012)“…α-Isopropylmalate synthase (α-IPMS) catalyzes the metal-dependent aldol reaction between α-ketoisovalerate (α-KIV) and acetyl-coenzyme A (AcCoA) to give…”
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Structure and function of GlmU from Mycobacterium tuberculosis
Published in Acta crystallographica. Section D, Biological crystallography. (01-03-2009)“…Antibiotic resistance is a major issue in the treatment of infectious diseases such as tuberculosis. Existing antibiotics target only a few cellular pathways…”
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Repurposing the Chemical Scaffold of the Anti-Arthritic Drug Lobenzarit to Target Tryptophan Biosynthesis in Mycobacterium tuberculosis
Published in Chembiochem : a European journal of chemical biology (14-04-2014)“…The emergence of extensively drug‐resistant strains of Mycobacterium tuberculosis (Mtb) highlights the need for new therapeutics to treat tuberculosis. We are…”
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A covalent adduct of MbtN, an acyl-ACP dehydrogenase from Mycobacterium tuberculosis, reveals an unusual acyl-binding pocket
Published in Acta crystallographica. Section D, Biological crystallography. (01-04-2015)“…Mycobacterium tuberculosis (Mtb) is the causative agent of tuberculosis. Access to iron in host macrophages depends on iron‐chelating siderophores called…”
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Advances in menaquinone biosynthesis: sublocalisation and allosteric regulation
Published in Current opinion in structural biology (01-12-2020)“…•Menaquinones (MKs) are involved in bacterial electron transport and adaptation.•The Men pathway is the most predominant of two bacterial pathways to make…”
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Unambiguous determination of isobaric histone modifications by reversed-phase retention time and high-mass accuracy
Published in Analytical biochemistry (01-01-2010)“…Methylation and acetylation of lysines are crucial posttranslational modifications that regulate gene transcription and have been shown to be misregulated in…”
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Synthesis and evaluation of M. tuberculosis salicylate synthase (MbtI) inhibitors designed to probe plasticity in the active site
Published in Organic & biomolecular chemistry (01-01-2012)“…Mycobacterium tuberculosis salicylate synthase (MbtI) catalyses the first committed step in the biosynthesis of mycobactin T, an iron-chelating siderophore…”
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Allosteric inhibition of Staphylococcus aureus MenD by 1,4-dihydroxy naphthoic acid: a feedback inhibition mechanism of the menaquinone biosynthesis pathway
Published in Philosophical transactions of the Royal Society of London. Series B. Biological sciences (27-02-2023)“…Menaquinones (MKs) are electron carriers in bacterial respiratory chains. In ( ), MKs are essential for aerobic and anaerobic respiration. As MKs are…”
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Allosteric regulation of menaquinone (vitamin K2) biosynthesis in the human pathogen Mycobacterium tuberculosis
Published in The Journal of biological chemistry (20-03-2020)“…Menaquinone (vitamin K2) plays a vital role in energy generation and environmental adaptation in many bacteria, including the human pathogen Mycobacterium…”
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Structure and inhibition of subunit I of the anthranilate synthase complex of Mycobacterium tuberculosis and expression of the active complex
Published in Acta crystallographica. Section D, Biological crystallography. (01-11-2015)“…The tryptophan‐biosynthesis pathway is essential for Mycobacterium tuberculosis (Mtb) to cause disease, but not all of the enzymes that catalyse this pathway…”
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