Generating enzyme and radical-mediated bisubstrates as tools for investigating Gcn5-related N- acetyltransferases-Reference-Cited by-同舟云学术

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Generating enzyme and radical-mediated bisubstrates as tools for investigating Gcn5-related N- acetyltransferases

Published:2017-08 Issue:15 Volume:591 Page:2348-2361
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:FEBS Lett

Author:

Reidl Cory¹,Majorek Karolina A.²,Dang Joseph³,Tran David³,Jew Kristen³,Law Melissa³,Payne Yasmine¹,Minor Wladek²,Becker Daniel P.¹,Kuhn Misty L.³

Affiliation:

1. Department of Chemistry; Loyola University Chicago; IL USA

2. Department of Molecular Physiology and Biological Physics; University of Virginia; Charlottesville VA USA

3. Department of Chemistry and Biochemistry; San Francisco State University; CA USA

Funder

San Francisco State University

National Institute of Allergy and Infectious Diseases

National Institutes of Health

U.S. Department of Health and Human Services

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Reference39 articles.

1. Genomic-scale comparison of sequence- and structure-based methods of function prediction: does structure provide additional insight?;Fetrow;Protein Sci,2001

2. Structure and functions of the GNAT superfamily of acetyltransferases;Vetting;Arch Biochem Biophys,2005

3. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein;Neuwald;Trends Biochem Sci,1997

4. Activity-based substrate profiling for Gcn5-related N-acetyltransferases: the use of chloroacetyl-coenzyme A to identify protein substrates;Yu;J Am Chem Soc,2006

5. A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones;Vetting;Chem Biol,2004

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