کد مقاله کد نشریه سال انتشار مقاله انگلیسی ترجمه فارسی نسخه تمام متن
1368536 981701 2016 3 صفحه PDF ندارد دانلود رایگان
عنوان انگلیسی مقاله
Characterization of three amidinotransferases involved in the biosynthesis of ketomemicins
ترجمه فارسی عنوان
خواص سه amidinotransferases درگیر در بیوسنتز ketomemicins
کلمات کلیدی
Amidinotransferase؛ بیوسنتز؛ Pseudopeptide؛ Ketomemicins
Amidinotransferase; Biosynthesis; Pseudopeptide; Ketomemicins
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آلی
چکیده انگلیسی

We recently reported a novel class of amide bond forming enzymes (peptide ligases) involved in the biosynthesis of pheganomycins, resorcinomycins and ketomemicins. This class of enzymes exclusively utilizes Nα-amidino amino acids as the N-terminal substrate. In this Letter, we characterized three new amidinotransferases involved in the biosynthesis of ketomemicins and showed that l-arginine was the amidino-acceptor of amidinotransferases in both the Micromonospora sp. and Streptomyces mobaraensis clusters, while the Salinispora tropica enzyme recognized l-valine. Unexpectedly, the S. tropica enzyme accepted several different amino acids as amidino acceptors in addition to l-valine. Accordingly, we re-investigated the specific metabolites governed by the gene cluster of S. tropica and identified several minor congeners of ketomemicin C with different N-terminal amidino-amino acids. These results indicate that the amidinotransferase of S. tropica is promiscuous and could be useful to generate new ketomemicin-type natural products.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 26, Issue 15, 1 August 2016, Pages 3662–3664
نویسندگان
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