کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2020529 | 1069186 | 2013 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Kinetic characterization of arginine deiminase and carbamate kinase from Streptococcus pyogenes M49
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Kinetic characterization of arginine deiminase and carbamate kinase from Streptococcus pyogenes M49 Kinetic characterization of arginine deiminase and carbamate kinase from Streptococcus pyogenes M49](/preview/png/2020529.png)
چکیده انگلیسی
Streptococcus pyogenes (group A Streptococcus, GAS) is an important human pathogen causing mild superficial infections of skin and mucous membranes, but also life-threatening systemic diseases. S. pyogenes and other prokaryotic organisms use the arginine deiminase system (ADS) for survival in acidic environments. In this study, the arginine deiminase (AD), and carbamate kinase (CK) from S. pyogenes M49 strain 591 were heterologously expressed in Escherichia coli DH5α, purified, and kinetically characterized. AD and CK from S. pyogenes M49 share high amino acid sequence similarity with the respective enzymes from Lactococcus lactis subsp. lactis IL1403 (45.6% and 53.5% identical amino acids) and Enterococcus faecalis V583 (66.8% and 66.8% identical amino acids). We found that the arginine deiminase of S. pyogenes is not allosterically regulated by the intermediates and products of the arginine degradation (e.g., ATP, citrulline, carbamoyl phosphate). The Km and Vmax values for arginine were 1.13 ± 0.12 mM (mean ± SD) and 1.51 ± 0.07 μmol/min/mg protein. The carbamate kinase is inhibited by ATP but unaffected by arginine and citrulline. The Km and Vmax values for ADP were 0.72 ± 0.08 mM and 1.10 ± 0.10 μmol/min/mg protein and the Km for carbamoyl phosphate was 0.65 ± 0.07 mM. The optimum pH and temperature for both enzymes were 6.5 and 37 °C, respectively.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 91, Issue 1, September 2013, Pages 61-68
Journal: Protein Expression and Purification - Volume 91, Issue 1, September 2013, Pages 61-68
نویسندگان
Silvio Hering, Antje Sieg, Bernd Kreikemeyer, Tomas Fiedler,