Structural Basis for Substrate Specificity in ArnB. A Key Enzyme in the Polymyxin Resistance Pathway of Gram-Negative Bacteria - Test2 - elhamkhani - TriplyDB

Structural Basis for Substrate Specificity in ArnB. A Key Enzyme in the Polymyxin Resistance Pathway of Gram-Negative Bacteria

Structural Basis for Substrate Specificity in ArnB. A Key Enzyme in the Polymyxin Resistance Pathway of Gram-Negative Bacteria

http://www.wikidata.org/entity/Q27681447

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The structure of apo ArnA features an unexpected central binding pocket and provides an explanation for enzymatic cooperativity The yin and yang of bacterial resilience in the human gut microbiota.Structural characterization of AtmS13, a putative sugar aminotransferase involved in indolocarbazole AT2433 aminopentose biosynthesis Structural Basis for the Stereochemical Control of Amine Installation in Nucleotide Sugar Aminotransferases Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis.Characterization of Early Enzymes Involved in TDP-Aminodideoxypentose Biosynthesis en Route to Indolocarbazole AT2433.Structural and functional studies of Spr1654: an essential aminotransferase in teichoic acid biosynthesis in Streptococcus pneumoniae.

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Structural Basis for Substrate Specificity in ArnB. A Key Enzyme in the Polymyxin Resistance Pathway of Gram-Negative Bacteria

http://www.wikidata.org/entity/Q27681447

description

2014 nî lūn-bûn

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2014 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2014 թվականի փետրվարին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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Structural Basis for Substrate ...... hway of Gram-Negative Bacteria

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Marcelo C Sousa

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Myeongseon Lee

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P2860

Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K

Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S

Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis

Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance

Crystal structure of Escherichia coli ArnA (PmrI) decarboxylase domain. A key enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance

PHENIX: a comprehensive Python-based system for macromolecular structure solution

An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli

Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance

Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme

GDP-perosamine synthase: structural analysis and production of a novel trideoxysugar

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796-805

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scholarly article

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10.1021/BI4015677

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4

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53

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24460375

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Gram-negative bacteria

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3985747

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