The antibiotic CJ-15,801 is an antimetabolite that hijacks and then inhibits CoA biosynthesis. - Wikidata - wikimedia - TriplyDB

The antibiotic CJ-15,801 is an antimetabolite that hijacks and then inhibits CoA biosynthesis.

The antibiotic CJ-15,801 is an antimetabolite that hijacks and then inhibits CoA biosynthesis.

http://www.wikidata.org/entity/Q35992631

about

Whole-genome sequencing targets drug-resistant bacterial infections Evidence of Kinetic Cooperativity in Dimeric Ketopantoate Reductase from Staphylococcus aureus.Validation of CoaBC as a Bactericidal Target in the Coenzyme A Pathway of Mycobacterium tuberculosis.Speculative strategies for new antibacterials: all roads should not lead to Rome.Emerging trends in the discovery of natural product antibacterials.Recent advances in targeting coenzyme A biosynthesis and utilization for antimicrobial drug development.Exploiting the coenzyme A biosynthesis pathway for the identification of new antimalarial agents: the case for pantothenamides.Strategies for target identification of antimicrobial natural products.Novel pantothenate derivatives for anti-malarial chemotherapy.Antimicrobial activity of pantothenol against staphylococci possessing a prokaryotic type II pantothenate kinase.Mutations in the pantothenate kinase of Plasmodium falciparum confer diverse sensitivity profiles to antiplasmodial pantothenate analogues.Variation in pantothenate kinase type determines the pantothenamide mode of action and impacts on coenzyme A salvage biosynthesis.Role of prokaryotic type I and III pantothenate kinases in the coenzyme A biosynthetic pathway of Bacillus subtilis.

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P2860

The antibiotic CJ-15,801 is an antimetabolite that hijacks and then inhibits CoA biosynthesis.

http://www.wikidata.org/entity/Q35992631

description

2012 nî lūn-bûn

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P356

J.CHEMBIOL.2012.03.013

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Chemistry and Biology

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The antibiotic CJ-15,801 is an ...... hen inhibits CoA biosynthesis.

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Justin C Hammons

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Michael D Burkart

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Renier van der Westhuyzen

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Samira Dahesh

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Stephen C Pelly

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Wessel J A Moolman

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P2860

Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution

Structure of the Type III Pantothenate Kinase from Bacillus anthracis at 2.0 Å Resolution: Implications for Coenzyme A-Dependent Redox Biology † , ‡

Structural basis for substrate binding and the catalytic mechanism of type III pantothenate kinase

Substrate-assisted inhibition of ubiquitin-like protein-activating enzymes: the NEDD8 E1 inhibitor MLN4924 forms a NEDD8-AMP mimetic in situ

Inhibitors of pantothenate kinase: novel antibiotics for staphylococcal infections

Characterization of a new pantothenate kinase isoform from Helicobacter pylori

Crystal structure of a type III pantothenate kinase: insight into the mechanism of an essential coenzyme A biosynthetic enzyme universally distributed in bacteria

Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties

Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified coenzyme A biosynthetic enzyme in bacteria

Copper-mediated synthesis of N-acyl vinylogous carbamic acids and derivatives: synthesis of the antibiotic CJ-15,801.

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559-571

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