Insight into the structural flexibility and function of Mycobacterium tuberculosis isocitrate lyase (original) (raw)
Activity loss by H46A mutation in Mycobacterium tuberculosis isocitrate lyase is due to decrease in structural plasticity and collective motions of the active site
Timir Tripathi
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Alterations in conformational topology and interaction dynamics caused by L418A mutation leads to activity loss of Mycobacterium tuberculosis isocitrate lyase
Amit Sonkar
Biochemical and biophysical research communications, 2017
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Distant Phe345 mutation compromises the stability and activity of Mycobacterium tuberculosis isocitrate lyase by modulating its structural flexibility
Amit Sonkar
Scientific Reports, 2017
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The Three-dimensional Structure of N-Succinyldiaminopimelate Aminotransferase from Mycobacterium tuberculosis
Simone Weyand
Journal of Molecular Biology, 2007
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Structures of free and inhibited forms of the L , D -transpeptidase Ldt Mt1 from Mycobacterium tuberculosis
Emilia Pedone
Acta Crystallographica Section D Biological Crystallography, 2013
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Structural basis for the inhibition of Mycobacterium tuberculosis L , D -transpeptidase by meropenem, a drug effective against extensively drug-resistant strains
Jiří Brynda
Acta Crystallographica Section D Biological Crystallography, 2013
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Site-directed Mutagenesis of Glutamate 166 in Two β-Lactamases
Bernard Joris
Journal of Biological Chemistry, 1997
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Moonlighting function of glutamate racemase from Mycobacterium tuberculosis: racemization and DNA gyrase inhibition are two independent activities of the enzyme
Soumitra Ghosh
Microbiology, 2008
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Two Crystal Structures of Escherichia coli N-Acetyl-l-Glutamate Kinase Demonstrate the Cycling between Open and Closed Conformations
Leonor Fernandez-murga
Journal of Molecular Biology, 2010
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Novel Insights into Eukaryotic -Glutamyltranspeptidase 1 from the Crystal Structure of the Glutamate-bound Human Enzyme
Blaine Mooers
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Exploitation of structural and regulatory diversity in glutamate racemases
Stewart Fisher
Nature, 2007
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The key DNA-binding residues in the C-terminal domain of Mycobacterium tuberculosis DNA gyrase A subunit (GyrA)
Zhiping Zhang
Nucleic Acids Research, 2006
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Structural insight into the inactivation of Mycobacterium tuberculosis non-classical transpeptidase LdtMt2 by biapenem and tebipenem
Leighanne Basta
BMC biochemistry, 2017
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Targeting the Cell Wall of Mycobacterium tuberculosis: Structure and Mechanism of L,D-Transpeptidase 2
Gert Kruger
Structure, 2012
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Structure of M. tuberculosis (3,3) L,D-Transpeptidase, LdtMt5. (Meropenen-adduct form)
Leighanne Basta
2015
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Quaternary structure is an essential component that contributes to the sophisticated allosteric regulation mechanism in a key enzyme from Mycobacterium tuberculosis
Dr. Ali Nazmi ÇORA
PLOS ONE, 2017
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Wild-type catalase peroxidase vs G279D mutant type: Molecular basis of Isoniazid drug resistance in Mycobacterium tuberculosis
Aishwarya Pratap Singh
Gene, 2018
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The B12-Binding Subunit of Glutamate Mutase from Clostridium tetanomorphum Traps the Nucleotide Moiety of Coenzyme B12
Robert Konrat
Journal of Molecular Biology, 2001
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Molecular dynamics at the root of expansion of function in the M69L inhibitor-resistant TEM beta-lactamase from Escherichia coli
P. Roblin, Laurent Maveyraud
Journal of the American Chemical Society, 2002
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Variations in the SDN Loop of Class A Beta-Lactamases: A Study of the Molecular Mechanism of BlaC (Mycobacterium tuberculosis) to Alter the Stability and Catalytic Activity Towards Antibiotic Resistance of MBIs
Saugata Hazra
Frontiers in Microbiology, 2021
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Site-directed Mutagenesis of Glutamate 166in Two beta -Lactamases. KINETIC AND MOLECULAR MODELING STUDIES
Marc Vanhove
Journal of Biological Chemistry, 1997
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Mutation of katG in a clinical isolate of Mycobacterium tuberculosis: effects on catalase-peroxidase for isoniazid activation
Defi Natalia
The Ukrainian Biochemical Journal
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Detection of novel coupled mutations in the katG gene (His276Met, Gln295His and Ser315Thr) in a multidrug-resistant Mycobacterium tuberculosis strain from Chennai, India, and insight into the molecular mechanism of isoniazid resistance using structural bioinformatics approaches
Parvathy Rajan
International Journal of Antimicrobial Agents, 2011
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Multicopy Crystallographic Refinement of a Relaxed Glutamine Synthetase from Mycobacterium tuberculosis Highlights Flexible Loops in the Enzymatic Mechanism and Its Regulation
Gaston Pfluegl
Biochemistry, 2002
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Human Gamma-Glutamyl Transpeptidase 1: Structures of the Free Enzyme, Inhibitor-Bound Tetrahedral Transition States and Glutamate-Bound Enzyme Reveal Novel Movement within the Active Site during Catalysis
Annie Heroux, Blaine Mooers, Marie H Hanigan, Blaine Mooers
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Changes in the free energy profile of glutamate mutase imparted by the mutation of an active site arginine residue to lysine
Anjali Patwardhan
Archives of Biochemistry and Biophysics, 2007
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Regulation of glutamate metabolism by protein kinases in mycobacteria
Rosario Durán
Molecular Microbiology, 2008
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Structure of Ldt Mt2 , an L , D -transpeptidase from Mycobacterium tuberculosis
Ylva Lindqvist
Acta Crystallographica Section D Biological Crystallography, 2013
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Structure-Guided Discovery of Antitubercular Agents That Target the Gyrase ATPase Domain
Rahul Vats
ChemMedChem, 2016
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Impact of Mutations at Arg220 and Thr237 in PER-2 β-Lactamase on Conformation, Activity, and Susceptibility to Inhibitors
Gabriel Gutkind
Antimicrobial Agents and Chemotherapy, 2017
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