نتایج جستجو برای: dfpase

تعداد نتایج: 24  

Journal: :Acta Crystallographica Section D Biological Crystallography 2010

Journal: :Acta Crystallographica Section F Structural Biology and Crystallization Communications 2010

Journal: :The Journal of biological chemistry 1958
F E BELL L A MOUNTER

Hog kidney Acylase I, an enzyme which hydrolyzes N-acetylL-amino acids, has been purified approximately 40-fold by Greenstein (1). During the course of the purification of hog kidney dialkylfluorophosphatase, it was consistently found that the protein fractions containing DFPasel activity also possessed very high Acylase I activity. Inasmuch as the DFPase and Acylase I activities were found to ...

Journal: :Acta Crystallographica Section F Structural Biology and Crystallization Communications 2006

Journal: :applied biotechnology reports 0
morteza mirzaei applied biotechnology research center, baqiyatallah university of medical sciences, tehran, iran ali mohammad latifi rahim jafari

efficiency of enzymes which are used in industrial or environmental applications is highly dependent on their thermal stability. in this study, the stability of dfpase has been evaluated after introducing disulfide bonds to the structure. the results obtained from a series of protein design software were subjected to molecular dynamics simulation at different temperature to test the performance...

Journal: :Biochimica et biophysica acta 2004
David T Yeung Denis Josse James D Nicholson Akhil Khanal Christopher W McAndrew Brian J Bahnson David E Lenz Douglas M Cerasoli

Human serum paraoxonase (HuPON1) is a calcium-dependent enzyme that hydrolyzes esters, including organophosphates and lactones, and exhibits anti-atherogenic properties. A few amino acids have been shown to be essential for the enzyme's arylesterase and organophosphatase activities. Until very recently, a three-dimensional model was not available for HuPON1, so functional roles have not been as...

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