کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10880233 | 1076944 | 2005 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Cloning and biochemical characterization of APIT, a new l-amino acid oxidase from Aplysia punctata
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوشیمی، ژنتیک و زیست شناسی مولکولی (عمومی)
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Cloning and biochemical characterization of APIT, a new l-amino acid oxidase from Aplysia punctata Cloning and biochemical characterization of APIT, a new l-amino acid oxidase from Aplysia punctata](/preview/png/10880233.png)
چکیده انگلیسی
The purple ink of the sea hare Aplysia punctata contains a 60 kDa protein with tumoricidal activity. This A. punctata ink toxin (APIT) kills tumor cells within 6-8 h in an apoptosis independent manner by the production of high amounts of hydrogen peroxide which induce a necrotic form of oxidative stress. Here, we describe the biochemical features of APIT associated with its anti-tumor activity. APIT is a weakly glycosylated FAD-binding l-amino acid oxidase that catalyzes the oxidative deamination of l-lysine and l-arginine and thereby produces hydrogen peroxide (H2O2), ammonia (NH4+) and the corresponding α-keto acids. The tumoricidal effect is completely abrogated in the absence of the amino acids l-lysine and l-arginine. The enzyme is stable at temperatures from 0 to 50 °C. Similar to other FAD-binding enzymes, it is resistant against tryptic digest. Even digest with proteinase K fails to degrade the enzyme. Cloning of the APIT gene and subsequent sequencing revealed a FAD-binding domain followed by a so-called GG-motif, which is typical for l-amino acid oxidases. Strongest homology exists to escapin, aplysianin A precursor, the cyplasins L and S and achacin.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Toxicon - Volume 46, Issue 5, October 2005, Pages 479-489
Journal: Toxicon - Volume 46, Issue 5, October 2005, Pages 479-489
نویسندگان
Daniel Butzke, Robert Hurwitz, Bernd Thiede, Sigrid Goedert, Thomas Rudel,