کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9882335 | 1536554 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification, characterization cloning, and sequencing of metalloendopeptidase from Streptomyces septatus TH-2
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Streptomyces septatus TH-2 secretes a large amount of a protease when cultured on a medium containing K2HPO4 and glucose. The enzyme was purified to homogeneity by a three-step procedure. This enzyme had a molecular mass of approximately 35Â kDa, and was particularly inhibited by EDTA and phosphoramidon. Its substrate specificity was investigated using novel fluorescence energy transfer combinatorial libraries. The protease was found to prefer Phe and Tyr at the P1 position, a hydrophobic or basic residue at the P2 position, and a basic or small residue at the P3 position. Its gene was cloned and sequenced, and its deduced amino acid sequence contained an HEXXH consensus sequence for zinc binding, confirming that it encodes metalloendopeptidase. The primary structure of the enzyme showed 40 and 69% identities with that of thermolysin from Bacillus thermoproteolyticus and that of a metalloendopeptidase from Streptomyces griseus, respectively.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 434, Issue 2, 15 February 2005, Pages 289-298
Journal: Archives of Biochemistry and Biophysics - Volume 434, Issue 2, 15 February 2005, Pages 289-298
نویسندگان
Tadashi Hatanaka, Jiro Arima Yoshiko Uesugi, Masaki Iwabuchi,