Class assignment of sequence-unrelated members of enzyme superfamilies by activity-based protein profiling

被引：24

作者：

Jessani, N

Young, JA

Diaz, SL

Patricelli, MP

Varki, A

Cravatt, BF ^{[1
]}

机构：

[1] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA

[2] Scripps Res Inst, Dept Cell Biol, La Jolla, CA 92037 USA

[3] Scripps Res Inst, Dept Chem, La Jolla, CA 92037 USA

[4] Univ Calif San Diego, Glycobiol Res & Training Ctr, Dept Med, La Jolla, CA 92093 USA

[5] Univ Calif San Diego, Glycobiol Res & Training Ctr, Dept Cellular & Mol Med, La Jolla, CA 92093 USA

[6] Activx Biosci, La Jolla, CA 92038 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2005年 / 44卷 / 16期

关键词：

activity-based protein profiling; enzymes; proteomics; serine hydrolases;

D O I：

10.1002/anie.200463098

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Chemical Equation Presented) No longer in a class of its own: By using a gel-free platform for activity-based protein profiling (ABPP; see figure), it was shown that the enzyme sialic acid 9-O-acetylesterase (SAE), which shares no sequence homology with other enzymes, is a member of the serine hydrolase super-family. The site of fluorophosphonate labeling in SAE was identified as serine 127; this residue is essential for catalytic activity. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA.

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收藏

页码：2400 / 2403

页数：4

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