Epimerization and substrate gating by a TE domain in β-lactam antibiotic biosynthesis
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چکیده
منابع مشابه
Epimerization and substrate gating by a TE domain in β-lactam antibiotic biosynthesis
Nonribosomal peptide synthetases are versatile engines of bioactive natural product biosynthesis that function according to the multiple carrier thiotemplate mechanism. C-terminal thioesterase (TE) domains of these giant modular proteins typically catalyze product release by hydrolysis or macrocyclization. We now report an unprecedented, dual-function TE that is involved in the biosynthesis of ...
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Penicillins and cephalosporins are β-lactam antibiotics widely used in human medicine. The biosynthesis of these compounds starts by the condensation of the amino acids L-α-aminoadipic acid, L-cysteine and L-valine to form the tripeptide δ-L-α-aminoadipyl-l-cysteinyl-D-valine catalysed by the non-ribosomal peptide 'ACV synthetase'. Subsequently, this tripeptide is cyclized to isopenicillin N th...
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BACKGROUND Parallel to the increasing use of non-β-lactam (NBL) antibiotics, allergic reactions to this drug group seem to increase. Data about NBL antibiotic hypersensitivity in children are limited. The aim of this study is to evaluate characteristic reactions to NBL antibiotics in children. METHOD Patients with suspected NBL allergy were assessed between 2011 and 2015. Characteristics of t...
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ژورنال
عنوان ژورنال: Nature Chemical Biology
سال: 2014
ISSN: 1552-4450,1552-4469
DOI: 10.1038/nchembio.1456