کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10880251 | 1076948 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Primary structure of brevilysin L4, an enzymatically active fragment of a disintegrin precursor from Gloydius halys brevicaudus venom
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کلمات کلیدی
TFAFTCPLA2SVMPAutoproteolysisLys-Cachromobacter protease Iphospholipase A2 - آنزیم فسفولیپاز A2 Trifluoroacetic acid - اسید TrifluoroaceticSnake venom - زهر مارPrimary structure - ساختار اولیهMatrix-assisted laser desorption ionization time-of-flight mass spectrometry - طیف سنجی جرمی یونیزاسیون یونیزاسیون لیزر جذب ماتریسMALDI-TOF-MS - مالدی TOF-MSMetalloprotease - متالوپروتئازMetalloproteinase - متالوپروتئیناز Snake venom metalloproteinase - متالوپروتئیناز زهر مار
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوشیمی، ژنتیک و زیست شناسی مولکولی (عمومی)
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چکیده انگلیسی
Brevilysin L4 (L4) is a non-hemorrhagic P-I class metalloprotease (MP) isolated from Gloydius halys brevicaudus venom. Its complete amino acid sequence has been determined. L4 is a single-chain polypeptide and highly homologous to those of other snake venom MPs. A zinc-binding motif, HExxHxxGxxH, is located at residues 142-152. A characteristic feature of L4 is the presence of a spacer sequence (LRTDTVS) at the C-terminal that links metalloprotease and disintegrin domains and is usually removed by post-translational proteolysis, suggesting that L4 is expressed together with a spacer region and a disintegrin domain at the C-terminal. The nucleotide sequence of a cDNA clone encoding L4 has revealed that L4 is a disintegrin precursor and produced as a P-II class MP. The disintegrin coded after L4 sequence was brevicaudin 1, a disintegrin previously isolated from the same venom. P-II class MPs have been suspected to undergo autoproteolysis to release disintegrins. Although being P-I class MP, L4 itself autocatalytically degrades with a half-life of 30 min at pH 8.5 and 37 °C in the absence of Ca2+. Sequence analysis of several fragment peptides produced during the autolysis of L4 indicated that more than 40 peptide bonds were split, and the cleavages of Ser60-Asn61, Thr99-Ala100, and Phe103-Asp104 bonds may trigger the autoproteolysis. Addition of Ca2+ completely suppressed the cleavage of these particular bonds, resulting in a marked prevention of autoproteolysis. Thus, L4 provides a good model for the investigation of autolysis of some MPs.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Toxicon - Volume 45, Issue 5, April 2005, Pages 571-580
Journal: Toxicon - Volume 45, Issue 5, April 2005, Pages 571-580
نویسندگان
Masanobu Deshimaru, Makoto Ichihara, Takahiro Hattori, Kumiko Koba, Shigeyuki Terada,