Abstract
Methionine ?-lyase [EC 4.4.1.11] participates in a methionine catabolism at a number of bacteria and protozoa eukaryotes, including pathogenic microorganisms. Lack of this enzyme at mammals allows consider it as a perspective target for rational antibacterial drug design. Currently in medical practice there are no the preparations based on an inhibition of methionine ?-lyase activity. We present results of the search of potential inhibitors of the enzyme using the NMR screening techniques based on identification of compounds, which able to bind specifically to their biological target. Study included a stage of in silico virtual screening of the library of commercially available compounds and subsequent experimental selection of the leading compounds, capable to interact with enzyme. Identification of binding was carried out by means of saturation transfer difference (STD) spectroscopy and WaterLOGSY technique. At the final stage the experimental assessment of inhibiting ability of the selected compounds in the reaction of ?-elimination of L-methionine catalyzed by methionine ?-lyase was carried out. Binding constants of two leading compounds were determined using the WaterLOGSY method. The research expands structural group of potential inhibitors of methionine ?-lyase and allows approach to the design of the inhibitors with higher efficacy.
[NMR paper] High-resolution screening combined with HPLC-HRMS-SPE-NMR for identification of fungal plasma membrane H(+)-ATPase inhibitors from plants.
High-resolution screening combined with HPLC-HRMS-SPE-NMR for identification of fungal plasma membrane H(+)-ATPase inhibitors from plants.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles High-resolution screening combined with HPLC-HRMS-SPE-NMR for identification of fungal plasma membrane H(+)-ATPase inhibitors from plants.
J Agric Food Chem. 2014 Jun 18;62(24):5595-602
Authors: Kongstad KT, Wubshet SG, Johannesen A, Kjellerup L, Winther AM, Jäger AK, Staerk D
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[NMR paper] Defining the Potential of Aglycone Modifications for Affinity/Selectivity Enhancement against Medically Relevant Lectins: Synthesis, Activity Screening, and HSQC-Based NMR Analysis.
Defining the Potential of Aglycone Modifications for Affinity/Selectivity Enhancement against Medically Relevant Lectins: Synthesis, Activity Screening, and HSQC-Based NMR Analysis.
Related Articles Defining the Potential of Aglycone Modifications for Affinity/Selectivity Enhancement against Medically Relevant Lectins: Synthesis, Activity Screening, and HSQC-Based NMR Analysis.
Chembiochem. 2014 Nov 18;
Authors: Rauthu SR, Shiao TC, André S, Miller MC, Madej E, Mayo KH, Gabius HJ, Roy R
Abstract
The emerging significance of...
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11-20-2014 08:40 PM
[NMR paper] Synthesis, 2D-NMR and molecular modelling studies of pentacycloundecane lactam-peptides and peptoids as potential HIV-1 wild type C-SA protease inhibitors.
Synthesis, 2D-NMR and molecular modelling studies of pentacycloundecane lactam-peptides and peptoids as potential HIV-1 wild type C-SA protease inhibitors.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--informahealthcare.com-userimages-ContentEditor-1258375244362-ihc-linkout.gif Related Articles Synthesis, 2D-NMR and molecular modelling studies of pentacycloundecane lactam-peptides and peptoids as potential HIV-1 wild type C-SA protease inhibitors.
J Enzyme Inhib Med Chem. 2013 Feb;28(1):78-88
Authors: Makatini MM, Petzold K, Alves...
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[NMR paper] Rapid screening and identification of ?-glucosidase inhibitors from mulberry leaves using enzyme-immobilized magnetic beads coupled with HPLC/MS and NMR.
Rapid screening and identification of ?-glucosidase inhibitors from mulberry leaves using enzyme-immobilized magnetic beads coupled with HPLC/MS and NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Rapid screening and identification of ?-glucosidase inhibitors from mulberry leaves using enzyme-immobilized magnetic beads coupled with HPLC/MS and NMR.
Biomed Chromatogr. 2013 Feb;27(2):148-55
Authors: Tao Y, Zhang Y, Cheng Y, Wang Y
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[NMR paper] NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme
NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains.
Related Articles NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains.
J Mol Biol. 2003 Apr 4;327(4):833-42
Authors: Liepinsh E, Généreux C, Dehareng D, Joris B, Otting G
AmpD is a bacterial amidase involved in the recycling of cell-wall fragments in Gram-negative bacteria. Inactivation of AmpD leads to derepression of beta-lactamase expression, presenting a major...
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11-24-2010 09:01 PM
Conformational dependence of 13C shielding and coupling constants for methionine
Abstract Methionine residues fulfill a broad range of roles in protein function related to conformational plasticity, ligand binding, and sensing/mediating the effects of oxidative stress. A high degree of internal mobility, intrinsic detection sensitivity of the methyl group, and low copy number have made methionine labeling a popular approach for NMR investigation of selectively labeled protein macromolecules. However, selective labeling approaches are subject to more limited information content. In order to optimize the information available from such studies, we have performed DFT...
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08-25-2010 03:51 PM
[NMR paper] NMR studies of the methionine methyl groups in calmodulin.
NMR studies of the methionine methyl groups in calmodulin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of the methionine methyl groups in calmodulin.
FEBS Lett. 1995 Jun 12;366(2-3):104-8
Authors: Siivari K, Zhang M, Palmer AG, Vogel HJ
Calmodulin (CaM) is a ubiquitous Ca(2+)-binding protein that can regulate a wide variety of cellular events. The protein contains 9 Met out of a total of 148 amino acid residues. The binding of Ca2+ to CaM induces...
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[NMR paper] Localisation of methionine residues in bacteriorhodopsin by carbonyl 13C-NMR with seq
Localisation of methionine residues in bacteriorhodopsin by carbonyl 13C-NMR with sequence-specific assignments.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Localisation of methionine residues in bacteriorhodopsin by carbonyl 13C-NMR with sequence-specific assignments.
FEBS Lett. 1993 Jul 19;327(1):7-12
Authors: Seigneuret M, Kainosho M
High-resolution 13C-NMR experiments have been performed on bacteriorhodopsin biosynthetically labeled with carbonyl-13C amino...
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[NMR screening of potential inhibitors of Citrobacter freundii methionine].
Linear Mode
