کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5131884 1378780 2017 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Functional characterization and crystal structure of thermostable amylase from Thermotoga petrophila, reveals high thermostability and an unusual form of dimerization
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
Functional characterization and crystal structure of thermostable amylase from Thermotoga petrophila, reveals high thermostability and an unusual form of dimerization
چکیده انگلیسی


- Novel thermostable α-amylase cloned from T. petrophila is able to hydrolyze starch into dextrin at 90-100 °C.
- The crystal structure of Tp-AmyS determined at 1.7 Å resolution showed prototypical three domains of GH-13 family.
- The enzyme is unique as it is a dimer that resemble to salivary amylase.
- Residues of tunnel, formed by monomer, specify the role of the dimer in substrate binding and hydrolysis.

Thermostable α-amylases have many industrial applications and are therefore continuously explored from novel sources. We present the characterization of a novel putative α-amylase gene product (Tp-AmyS) cloned from Thermotoga petrophila. The purified recombinant enzyme is highly thermostable and able to hydrolyze starch into dextrin between 90 and 100 °C, with optimum activity at 98 °C and pH 8.5. The activity increased in the presence of Rb1 +, K1 + and Ca2 + ions, whereas other ions inhibited activity. The crystal structure of Tp-AmyS at 1.7 Å resolution showed common features of the GH-13 family, however was apparently found to be a dimer. Several residues from one monomer interacted with a docked acarbose, an inhibitor of Tp-AmyS, in the other monomer, suggesting catalytic cooperativity within the dimer. The most striking feature of the dimer was that it resembled the dimerization of salivary amylase from a previous crystal structure, and thus could be a functional feature of some amylases.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1865, Issue 10, October 2017, Pages 1237-1245
نویسندگان
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