Structure-Based Site-Directed Mutagenesis of the UDP-MurNAc-Pentapeptide-Binding Cavity of the FemX Alanyl Transferase from Weissella viridescens [PDF]
, 2005 International audienceWeissella viridescens FemX (FemX(Wv)) belongs to the Fem family of nonribosomal peptidyl transferases that use aminoacyl-tRNA as the amino acid donor to synthesize the peptide cross-bridge found in the peptidoglycan of many species ...
Bouhss, Ahmed +8 more
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The npgA/cfwA gene encodes a putative 4′-phosphopantetheinyl transferase which is essential for penicillin biosynthesis in Aspergillus nidulans [PDF]
, 2003 Non-ribosomal peptide synthetases, polyketides and fatty acid synthetases have a modular organisation of multi-enzymatic activities. In all of them, the acyl or peptidyl carrier proteins have 4′-phosphopantetheine (P-pant) as an essential prosthetic ...
Price, Jacqueline +4 more
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Crystal structure of the surfactin synthetase-activating enzyme Sfp: a prototype of the 4 '-phosphopantetheinyl transferase superfamily [PDF]
, 1999 The Bacillus subtilis Sfp protein activates the peptidyl carrier protein (PCP) domains of surfactin synthetase by transferring the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to a serine residue conserved in all PCPs.
Reuter, K. +3 more
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Catalysed activation of cyanobacterial biosynthetic pathways by phosphopantetheinyl transferases [PDF]
, 2005 Cyanobacteria produce a diverse array of natural products with significant potential in many biotechnological, clinical and commercial applications.
Copp, Janine Naomi
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A Phosphopantetheinyl Transferase Homolog Is Essential for Photorhabdus luminescens To Support Growth and Reproduction of the Entomopathogenic Nematode Heterorhabditis bacteriophora [PDF]
, 2001 The bacterium Photorhabdus luminescens is a symbiont of the entomopathogenic nematode Heterorhabditis bacteriophora. The nematode requires the bacterium for infection of insect larvae and as a substrate for
Scott B. Bintrim +3 more
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Nonribosomal peptide synthesis in Aspergillus fumigatus and other fungi [PDF]
, 2007 In fungi, nonribosomal peptide synthetases (NRP synthetases) are large multi-functional enzymes containing adenylation, thiolation (or peptidyl carrier protein, PCP) and condensation domains. These enzymes are often encoded within gene clusters. Multiple
Stack, Deirdre +2 more
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Cloning and characterization of a phosphopantetheinyl transferase from Streptomyces verticillus ATCC15003, the producer of the hybrid peptide–polyketide antitumor drug bleomycin [PDF]
, 2001 Background: Phosphopantetheinyl transferases (PPTases) catalyze the posttranslational modification of carrier proteins by the covalent attachment of the 4′-phosphopantetheine (P-pant) moiety of coenzyme A to a conserved serine residue, a reaction ...
Liangcheng Du +9 more
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Quantification of the d‑Ala‑d‑Lac-Terminated Peptidoglycan Structure in Vancomycin-Resistant Enterococcus faecalis Using a Combined Solid-State Nuclear Magnetic Resonance and Mass Spectrometry Analysis [PDF]
, 2017 Induction of vancomycin resistance in vancomycin-resistant enterococci (VRE) involves replacement of the d-Ala-d-Ala terminus of peptidoglycan (PG) stems with d-Ala-d-Lac, dramatically reducing the binding affinity of vancomycin for lipid II.
James D. Chang (3637693) +3 more
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Synthesis of aminoacyl-tRNA analogues for the study and inhibition of Fem-transferases, new targets for the development of antimicrobials [PDF]
, 2016 En raison de leur nombreux rôles biologiques, les aminoacyl-ARNt font l'objet d'un intérêt croissant dans le domaine de la biologie des ARN. Parmi ces rôles, ils participent à la biosynthèse de la paroi bactérienne chez de nombreuses espèces Gram ...
Sakkas, Nicolas
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How structure guides function: ergothioneine anabolism and catabolism formylglycine generating enzyme methyl transferases [PDF]
, 2022 . A detailed understanding of the underlying mechanisms determining the chemistry of all involved enzymes is crucial to understand any biological system and eventually gives the opportunity to manipulate such systems. Macromolecular X-ray crystallography
Leisinger, Florian
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