کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10537085 | 962666 | 2009 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Biochemical characterization of Alr1529, a novel SGNH hydrolase variant from Anabaena sp. PCC 7120
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Biochemical characterization of Alr1529, a novel SGNH hydrolase variant from Anabaena sp. PCC 7120 Biochemical characterization of Alr1529, a novel SGNH hydrolase variant from Anabaena sp. PCC 7120](/preview/png/10537085.png)
چکیده انگلیسی
Alr1529, a serine hydrolase from the cyanobacteria Anabaena sp. strain PCC 7120 is a member of the SGNH hydrolase superfamily. Biochemical characterization of the purified enzyme revealed that the protein is a dimer in solution and is specific for aryl esters of short chain carboxylic acids. The enzyme was regio-selective for α-naphthyl esters with maximum activity at pH 7.5 and has a broad optimal temperature range (25-45 °C). A structure based comparison of Alr1529 with other superfamily members confirmed the presence of the catalytic triad (Ser17-Asp179-His182) and oxyanion hole (Ser17-Arg54-Asn87) residues. Alr1529 exhibits a previously undescribed variation in the active site wherein a conserved Gly, a proton donor making up the oxyanion hole in the SGNH hydrolases, is substituted by Arg54. Site-directed mutagenesis studies suggest that Arg54 is crucial for substrate binding and catalytic activity. Ser17 plays a very crucial role in catalysis as evident from the 50-fold lower activity of the S17A mutant.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1794, Issue 2, February 2009, Pages 324-334
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1794, Issue 2, February 2009, Pages 324-334
نویسندگان
Kiranmayee Bakshy, Sathyanarayana N. Gummadi, Narayanan Manoj,