Activity-based protein profiling: From enzyme chemistry

被引：946

作者：

Cravatt, Benjamin F. ^{[1
,2
]}

Wright, Aaron T. ^{[1
,2
]}

Kozarich, John W. ^{[3
]}

机构：

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

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

[3] Activx Biosci, La Jolla, CA 92037 USA

来源：

ANNUAL REVIEW OF BIOCHEMISTRY | 2008年 / 77卷

关键词：

affinity label; mass spectrometry; proteomics;

D O I：

10.1146/annurev.biochem.75.101304.124125

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Genome sequencing projects have provided researchers with a complete inventory of the predicted proteins produced by eukaryotic and prokaryotic organisms. Assignment of functions to these proteins represents one of the principal challenges for the field of proteomics. Activity-based protein profiling (ABPP) has emerged as a powerful chemical proteomic strategy to characterize enzyme function directly in native biological systems on a global scale. Here, we review the basic technology of AMP, the enzyme classes addressable by this method, and the biological discoveries attributable to its application.

引用

页码：383 / 414

页数：32

共 154 条

[1] Mapping enzyme active sites in complex proteomes [J].

Adam, GC ;

Burbaum, J ;

Kozarich, JW ;

Patricelli, MP ;

Cravatt, BF .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2004, 126 (05) :1363-1368

[2] Trifunctional chemical probes for the consolidated detection and identification of enzyme activities from complex proteomes [J].

Adam, GC ;

Sorensen, EJ ;

Cravatt, BF .

MOLECULAR & CELLULAR PROTEOMICS, 2002, 1 (10) :828-835

[3] Proteomic profiling of mechanistically distinct enzyme classes using a common chemotype [J].

Adam, GC ;

Sorensen, EJ ;

Cravatt, BF .

NATURE BIOTECHNOLOGY, 2002, 20 (08) :805-809

[4] Profiling the specific reactivity of the proteome with non-directed activity-based probes [J].

Adam, GC ;

Cravatt, BF ;

Sorensen, EJ .

CHEMISTRY & BIOLOGY, 2001, 8 (01) :81-95

[5] Chemical strategies for functional proteomics [J].

Adam, GC ;

Sorensen, EJ ;

Cravatt, BF .

MOLECULAR & CELLULAR PROTEOMICS, 2002, 1 (10) :781-790

[6] Regulation of cytochrome P450 by posttranslational modification [J].

Aguiar, M ;

Masse, R ;

Gibbs, BF .

DRUG METABOLISM REVIEWS, 2005, 37 (02) :379-404

[7] Novel mechanistic class of fatty acid amide hydrolase inhibitors with remarkable selectivity [J].

Ahn, Kyunghye ;

Johnson, Douglas S. ;

Fitzgerald, Laura R. ;

Liimatta, Marya ;

Arendse, Andrea ;

Stevenson, Tracy ;

Lund, Eric. T. ;

Nugent, Richard A. ;

Nomanbhoy, Tyzoon K. ;

Alexander, Jessica P. ;

Cravatt, Benjamin F. .

BIOCHEMISTRY, 2007, 46 (45) :13019-13030

[8] The putative endocannabinoid transport blocker LY2183240 is a potent inhibitor of FAAH and several other brain serine hydrolases [J].

Alexander, Jessica P. ;

Cravatt, Benjamin F. .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2006, 128 (30) :9699-9704

[9] Mechanism of carbamate inactivation of FAAH: Implications for the design of covalent inhibitors and in vivo functional probes for enzymes [J].

Alexander, JP ;

Cravatt, BF .

CHEMISTRY & BIOLOGY, 2005, 12 (11) :1179-1187

[10] Density functional study of the mechanism of a tyrosine phosphatase: 1. Intermediate formation [J].

Asthagiri, D ;

Dillet, V ;

Liu, TQ ;

Noodleman, L ;

Van Etten, RL ;

Bashford, D .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2002, 124 (34) :10225-10235

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