مقاله انگلیسی شناسایی جهش های محدود کننده کاتالیزورهای خودکار فعال شونده

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مقاله انگلیسی شناسایی جهش های محدود کننده کاتالیزورهای خودکار فعال شونده
عنوان فارسی مقاله: شناسایی جهش های محدود کننده کاتالیزورهای خودکار فعال شونده ال-آسپارتیت و α-دکربوکسیلاز باکتریایی
عنوان انگلیسی مقاله: Identification of mutations restricting autocatalytic activation of bacterial l-aspartate α-decarboxylase
مجله/کنفرانس: Amino Acids
رشته های تحصیلی مرتبط: زیست شناسی
گرایش های تحصیلی مرتبط: زیست فناوری محیط و صنعت
کلمات کلیدی انگلیسی: l-Aspartate α-decarboxylase; Self-cleavage; Pyruvoyl group; Site-directed mutagenesis; Classification
نوع نگارش مقاله: Original paper
نمایه: scopus - master journals - JCR - medline
DOI: doi.org/10.1007/s00726-018-2620-9
ناشر: Springer
نوع ارائه مقاله: ژورنالی
نوع مقاله: ISI
سال انتشار مقاله: 2018
ایمپکت فاکتور(IF): 2.906(2017)
شاخص H_index: 98
SJR: 1.135
شناسه ISSN: 0939-4451
فرمت مقاله انگلیسی: PDF
تعداد صفحات مقاله انگلیسی: 8
کد محصول: EN51
فهرست انگلیسی مطالب
Abstract

Introduction

Materials and methods
-Chemicals, vectors, and strains
-Cloning of panD from various origins and culture conditions
-Expression and purification of PanDs
-Tricine–SDS‑PAGE assay
-Deletion of panZ gene in E. coli BL21 (DE3)
-Phylogenetic analysis and sequence alignment
-Enzyme activity assay
-Site‑directed mutagenesis of PanD

Results
-Cloning of panD genes from various origins
-Characterization of PanDs from various origins
-Phylogenetic analysis of PanD
-Site‑directed mutagenesis of PanD

Discussion

Conclusions

References
نمونه متن انگلیسی
Abstract

Bacterial l-aspartate α-decarboxylase (PanD) specifically catalyzes the decarboxylation of l-aspartic acid to β-alanine. It is translated as an inactive pro-protein, then processed by self-cleavage to form two small subunits with catalytic activity. There is a significant difference in the efficiency of this process among the reported PanDs, while the structural basis remains unclear. More PanDs with known sequences and characterized properties are needed to shed light on the molecular basis of the self-cleavage process. In this study, PanD genes from 33 selected origins were synthesized and expressed; using purified recombinant enzymes, their self-processing properties were characterized and classified. Three classes of PanDs were acquired based on their self-cleavage efficiency. Combined with the phylogenetic analysis and structure comparison, sited-directed mutagenesis was performed to investigate the effects of four mutants on self-processing. In comparison with the wild-type (96.4%), the self-cleavage efficiencies of mutants V23E, I26C, T27A, and E56S were decreased to 90.5, 83.6, 74.4 and 81.2%, respectively. The results indicated that residues of V23, I26, T27 and E56 were critical to the self-cleavage processing of PanDs. This work provided further understanding to the self-cleavage processing of PanDs, which may contribute to protein engineering of the enzyme.
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