کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2047500 1073984 2015 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Binding of PDZ domains to the carboxy terminus of inducible nitric oxide synthase boosts electron transfer and NO synthesis
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Binding of PDZ domains to the carboxy terminus of inducible nitric oxide synthase boosts electron transfer and NO synthesis
چکیده انگلیسی
iNOS lacks any phosphorylatable residue at its C-terminus despite displaying a 25-residue extension known to block electron transfer and activity. We report that C-terminal deletions of iNOS increased the cytochrome c reduction rate. Moreover, the interaction of the iNOS C-terminus with the PDZ domains of EBP50 or CAP70 resulted not only in augmented reductase activity and greater NO synthesis but also anticipated the formation of the air-stable semiquinone generated after NADPH addition. Hence, the C-terminus of iNOS regulates the activity of the enzyme, albeit, unlike nNOS and eNOS, displacement of the autoinhibitory element occurs upon binding to proteins with PDZ domains.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 589, Issue 17, 4 August 2015, Pages 2207-2212
نویسندگان
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