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Acyltransferases in plants: a good time to be BAHD
1Department of Biochemistry, Max Planck Institute for Chemical Ecology, Hans-Knöll Strasse 8, D-07745 Jena, Germany. dauria@ice.mpg.de
Current Opinion in Plant Biology
|April 18, 2006
Summary
Plant BAHD acyltransferases modify secondary metabolites, creating diverse compounds. New structural data aids in understanding these versatile enzymes and their evolutionary roles.
Area of Science:
- Biochemistry
- Plant Science
- Enzymology
Background:
- Acylation is a crucial biochemical modification of plant secondary metabolites.
- Plant BAHD acyltransferases are a large enzyme family utilizing acyl-CoA.
- Their products range from volatile esters to defense compounds like phytoalexins.
Purpose of the Study:
- To explore the functional predictions and evolutionary insights of plant BAHD acyltransferases.
- To leverage recent advances in genomics and structural biology for understanding BAHD enzyme function.
Main Methods:
- Analysis of recent genome sequencing data.
- Examination of the first crystal structure of a BAHD enzyme member.
Main Results:
- BAHD enzymes exhibit significant catalytic versatility, complicating functional prediction from sequence alone.
- Advances in sequencing and structural data offer new perspectives on BAHD enzyme evolution and function.
Conclusions:
- Understanding BAHD acyltransferase evolution and function is enhanced by new genomic and structural insights.
- The catalytic diversity of BAHD enzymes presents challenges but is becoming more decipherable with advanced data.
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