Discovery of Mycobacterium Tuberculosis Protein Tyrosine Phosphatase A (MptpA) Inhibitors Based on Natural Products and a Fragment-Based Approach
Naturally inspired or fragment based. Mcyobacterium tuberculosis has two functional phosphatases, protein tyrosine phosphates A and B (MptpA and B), which are thought to mediate mycobacterial survival in the host. Here we describe the first inhibitors of MptpA (see scheme). Initial hits were identif...
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| Veröffentlicht in: | Chembiochem : a European journal of chemical biology 2005-10, Vol.6 (10), p.1749-1753 |
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| container_title | Chembiochem : a European journal of chemical biology |
| container_volume | 6 |
| creator | Manger, Michael Scheck, Michael Prinz, Heino von Kries, Jens Peter Langer, Thomas Saxena, Krishna Schwalbe, Harald Fürstner, Alois Rademann, Jörg Waldmann, Herbert |
| description | Naturally inspired or fragment based. Mcyobacterium tuberculosis has two functional phosphatases, protein tyrosine phosphates A and B (MptpA and B), which are thought to mediate mycobacterial survival in the host. Here we describe the first inhibitors of MptpA (see scheme). Initial hits were identified in screening collections that were inspired by natural products and composed by fragment‐based approach. |
| doi_str_mv | 10.1002/cbic.200500171 |
| format | Article |
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Mcyobacterium tuberculosis has two functional phosphatases, protein tyrosine phosphates A and B (MptpA and B), which are thought to mediate mycobacterial survival in the host. Here we describe the first inhibitors of MptpA (see scheme). 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Mcyobacterium tuberculosis has two functional phosphatases, protein tyrosine phosphates A and B (MptpA and B), which are thought to mediate mycobacterial survival in the host. Here we describe the first inhibitors of MptpA (see scheme). Initial hits were identified in screening collections that were inspired by natural products and composed by fragment‐based approach.</description><subject>Bacterial Proteins - antagonists & inhibitors</subject><subject>Bacterial Proteins - metabolism</subject><subject>Depsipeptides - chemical synthesis</subject><subject>Depsipeptides - chemistry</subject><subject>Depsipeptides - pharmacology</subject><subject>Enzyme Inhibitors - chemical synthesis</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>enzymes</subject><subject>Heterocyclic Compounds, 3-Ring - pharmacology</subject><subject>inhibitors</subject><subject>Molecular Structure</subject><subject>Mycobacterium tuberculosis</subject><subject>Mycobacterium tuberculosis - drug effects</subject><subject>Mycobacterium tuberculosis - enzymology</subject><subject>natural products</subject><subject>Peptide Library</subject><subject>phosphatases</subject><subject>Protein Tyrosine Phosphatases - antagonists & inhibitors</subject><subject>Protein Tyrosine Phosphatases - metabolism</subject><subject>Pyrroles - pharmacology</subject><subject>Recombinant Fusion Proteins - antagonists & inhibitors</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>stevastelins</subject><issn>1439-4227</issn><issn>1439-7633</issn><issn>1439-4227</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9v0zAYxiMEYmNw5Qg-ITik-E9s18e20FG0jgnKn5vlOG9WjzQOdgL0Y_CNcZVqcNvJtvx7fpbfJ8ueEjwhGNPXtnR2QjHmGBNJ7mWnpGAql4Kx-8d9Qak8yR7FeIMxVoKRh9kJEUQJTPFp9ueNi9b_hLBHvkbrvfWlsT0EN-zQZigh2KHx0UV0FXwPrkWbfUjnFtDV1sdua3oTAc3Qy3XXd7NXaNVuXel6HyKap5sK-RZdmn4IpjkoqsH2EZm2QgYtg7neQdvnIzjruuCN3T7OHtSmifDkuJ5lm-XbzeJdfvHhfLWYXeS2YILkUzBKGauMYRXnhaQGCFAQUpVKMcolZVwyxrFg6dtVUZVTU4kUqDGvAdhZ9mLUpld_DBB7vUuTgKYxLfghajEVghac3wkSyaaEcJrAyQjaNKEYoNZdcDsT9ppgfShLH8rSt2WlwLOjeSh3UP3Dj-0kQI3AL9fA_g6dXsxXi__l-Zh1sYfft1kTvmshmeT66-W5_rhU39SX93O9Tvzzka-N1-Y6uKg_f6KYMExUQQsp2V8km7pW</recordid><startdate>20051001</startdate><enddate>20051001</enddate><creator>Manger, Michael</creator><creator>Scheck, Michael</creator><creator>Prinz, Heino</creator><creator>von Kries, Jens Peter</creator><creator>Langer, Thomas</creator><creator>Saxena, Krishna</creator><creator>Schwalbe, Harald</creator><creator>Fürstner, Alois</creator><creator>Rademann, Jörg</creator><creator>Waldmann, Herbert</creator><general>Wiley-VCH Verlag</general><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><scope>FBQ</scope><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20051001</creationdate><title>Discovery of Mycobacterium Tuberculosis Protein Tyrosine Phosphatase A (MptpA) Inhibitors Based on Natural Products and a Fragment-Based Approach</title><author>Manger, Michael ; 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Mcyobacterium tuberculosis has two functional phosphatases, protein tyrosine phosphates A and B (MptpA and B), which are thought to mediate mycobacterial survival in the host. Here we describe the first inhibitors of MptpA (see scheme). Initial hits were identified in screening collections that were inspired by natural products and composed by fragment‐based approach.</abstract><cop>Weinheim</cop><pub>Wiley-VCH Verlag</pub><pmid>16196020</pmid><doi>10.1002/cbic.200500171</doi><tpages>5</tpages></addata></record> |
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| subjects | Bacterial Proteins - antagonists & inhibitors Bacterial Proteins - metabolism Depsipeptides - chemical synthesis Depsipeptides - chemistry Depsipeptides - pharmacology Enzyme Inhibitors - chemical synthesis Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology enzymes Heterocyclic Compounds, 3-Ring - pharmacology inhibitors Molecular Structure Mycobacterium tuberculosis Mycobacterium tuberculosis - drug effects Mycobacterium tuberculosis - enzymology natural products Peptide Library phosphatases Protein Tyrosine Phosphatases - antagonists & inhibitors Protein Tyrosine Phosphatases - metabolism Pyrroles - pharmacology Recombinant Fusion Proteins - antagonists & inhibitors Recombinant Fusion Proteins - metabolism stevastelins |
| title | Discovery of Mycobacterium Tuberculosis Protein Tyrosine Phosphatase A (MptpA) Inhibitors Based on Natural Products and a Fragment-Based Approach |
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