کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8384086 | 1543465 | 2006 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coli
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کلمات کلیدی
ORFACPDTNBGdn-HClProtein denaturation - denaturization پروتئینAcylphosphatase - آکیل فسفاتازEscherichia coli - اشریشیا کُلیcircular dichroism - رنگ تابی دورانیEnzyme activity - فعالیت آنزیمopen reading frame - قاب خواندن بازprokaryotes - پروکریوت هاDisulfide bridge - پل دی سولفیدGuanidine hydrochloride - گوانیدین هیدروکلراید
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coli The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coli](/preview/png/8384086.png)
چکیده انگلیسی
Acylphosphatase (AcP) activity in prokaryotes was classically attributed to some aspecific acid phosphatases. We identified an open reading frame for a putative AcP in the b0968 Escherichia coli gene and purified the recombinant enzyme after checking by RT-PCR that it was indeed expressed. EcoAcP has a predicted typical fold of the AcP family but displays a very low specific activity and a high structural stability differently from its mesophilic and similarly to its hyperthermophilic counterparts. Site directed mutagenesis suggests that, together with other structural features, the intrachain S-S bridge in EcoAcP is involved in a remarkable thermal and chemical stabilization of the protein without affecting its catalytic activity.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 580, Issue 30, 22 December 2006, Pages 6763-6768
Journal: FEBS Letters - Volume 580, Issue 30, 22 December 2006, Pages 6763-6768
نویسندگان
Matteo Ramazzotti, Claudia Parrini, Massimo Stefani, Giampaolo Manao, Donatella Degl'Innocenti,