دورية أكاديمية

Substrate specificity of the cypemycin decarboxylase CypD

التفاصيل البيبلوغرافية
العنوان: Substrate specificity of the cypemycin decarboxylase CypD
المؤلفون: Wei Ding, Tianlu Mo, Dhanaraju Mandalapu, Qi Zhang
المصدر: Synthetic and Systems Biotechnology, Vol 3, Iss 3, Pp 159-162 (2018)
بيانات النشر: KeAi Communications Co., Ltd., 2018.
سنة النشر: 2018
المجموعة: LCC:Biotechnology
LCC:Biology (General)
مصطلحات موضوعية: Biotechnology, TP248.13-248.65, Biology (General), QH301-705.5
الوصف: The linaridin antibiotic cypemycin is a ribosomal synthesized and post-translationally modified peptide (RiPP) that possesses potent activity against mouse leukemia cells. This peptide natural product contains an S-[(Z)-2-aminovinyl]-d-cysteine (AviCys) moiety in the C-terminus. Formation of AviCys moiety requires an oxidative decarboxylation of the C-terminal Cys of the precursor peptide CypA, and this process is catalyzed by a flavin-containing protein CypD. In this work, we tested CypD substrate specificity with a series of synthetic oligopeptides. We show that most of the N-terminal sequence of CypA is not required for CypD activity, and the C-terminal three residues serve as the minimal structural element for enzyme recognition. We also show that CypD tolerates various substrates with modified C-termini, allowing for the generation of four novel cypemycin variants with modified AviCys moiety by site direct mutagenesis of the precursor peptide CypA. Our study demonstrates the relaxed substrate specificity of CypD and lays a foundation for future bioengineering of AviCys-containing natural products.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2405-805X
Relation: http://www.sciencedirect.com/science/article/pii/S2405805X18300395; https://doaj.org/toc/2405-805X
DOI: 10.1016/j.synbio.2018.09.002
URL الوصول: https://doaj.org/article/54dcd34bcdff43a5a9bc51302cce743e
رقم الأكسشن: edsdoj.54dcd34bcdff43a5a9bc51302cce743e
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:2405805X
DOI:10.1016/j.synbio.2018.09.002