Evaluation of the Active Site of PhenylalanineDehydrogenase Isolated from Bacillus badius usingHomology Based Modeling

سال انتشار: 1394
نوع سند: مقاله ژورنالی
زبان: انگلیسی
مشاهده: 492

متن کامل این مقاله منتشر نشده است و فقط به صورت چکیده یا چکیده مبسوط در پایگاه موجود می باشد.
توضیح: معمولا کلیه مقالاتی که کمتر از ۵ صفحه باشند در پایگاه سیویلیکا اصل مقاله (فول تکست) محسوب نمی شوند و فقط کاربران عضو بدون کسر اعتبار می توانند فایل آنها را دریافت نمایند.

استخراج به نرم افزارهای پژوهشی:

لینک ثابت به این مقاله:

شناسه ملی سند علمی:

JR_FOCS-1-1_002

تاریخ نمایه سازی: 28 شهریور 1395

چکیده مقاله:

Introduction: The enzyme, Phenylalanine dehydrogenase (L-phe DH; NADoxidoreductase, deaminating; EC 1.4.1.20) belongs to the amino acid dehydrogenasefamily of enzymes which catalyzes the reversible oxidative deamination reaction ofL-phenylalanine to their respective α- ketoacids. An assay technique with a high sensitivityfor blood L-phenylalanine level, an important marker for the screening of Phenylketonuria(PKU), has been established by means of PheDH. This enzyme is being used as acommercial and valuable biocatalyst in medical and pharmaceutical industries. Theenzymes of this family are closely related in structure and function.Methods: Swiss-Pdb Viewer used for analysis and Rhodococcus sp. M4 was chosen becauseof the availability of several crystal structures with bound substrates and its high specificactivity.Results: Rhodococcus sp. M4 and B. badius PheDHs are very different from each other ona sequence level, sharing only %32 identity and %50 similarity. Coming from the samestructural sub-family, they share a much stronger correlation in their folding motifs.Conclusions: Since there currently is no crystal structure available for the B. badiusPheDH, the sequence was folded over the 1BW9 crystal structure and superimposed overthe original scaffold using SuperPose.

نویسندگان

Farzad Yousefi

Department of Biochemistry, Faculty of Biological Sciences, Tarbiat ModaresUniversity, Tehran, Iran

Farangis Ataei

Department of Biochemistry, Faculty of Biological Sciences, Tarbiat ModaresUniversity, Tehran, Iran

Hamid Reza Samadikhah

Department of Nanobiotechnology, Faculty of Biological Sciences, Tarbiat ModaresUniversity, Tehran, Iran

Parisa Bahmani

DepartmentofBiochemistry, Faculty of Biological Sciences, Tarbiat ModaresUniversity, Tehran,Iran