Issue 12, 2012
From the journal:

Molecular BioSystems

A type III polyketide synthase from Rhizobium etli condenses malonyl CoAs to a heptaketide pyrone with unusually high catalytic efficiency†

Marimuthu Jeya,a   Tae-Su Kim,a   Manish Kumar Tiwari,a   Jinglin Li,a   Huimin Zhao*bcd  and  Jung-Kul Lee*a  

* Corresponding authors

a Department of Chemical Engineering, Konkuk University, Seoul 143-701, Korea
E-mail: jkrhee@konkuk.ac.kr
Fax: +82-2-458-3504

b Departments of Chemical and Biomolecular Engineering, Chemistry, and Bioengineering, University of Illinois, 600 South Mathews Avenue, Urbana, IL 61801, USA
E-mail: zhao5@illinois.edu
Fax: +1 217-333-5052

c Institute for Genomic Biology, University of Illinois, 600 South Mathews Avenue, Urbana, IL 61801, USA

d Center for Biophysics and Computational Biology, University of Illinois, 600 South Mathews Avenue, Urbana, IL 61801, USA

Abstract

A novel type III polyketide synthase (RePKS) from Rhizobium etli produced a heptaketide pyrone using acetyl-CoA and six molecules of malonyl-CoA. Its catalytic efficiency (kcat/Km = 5230 mM−1 min−1) for malonyl CoA was found to be the highest ever reported. Molecular dynamics studies revealed the unique features of RePKS.

Graphical abstract: A type III polyketide synthase from Rhizobium etli condenses malonyl CoAs to a heptaketide pyrone with unusually high catalytic efficiency

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Article information

DOI
https://doi.org/10.1039/C2MB25347J
Article type
Communication
Submitted
28 Aug 2012
Accepted
28 Sep 2012
First published
02 Oct 2012

Mol. BioSyst., 2012,8, 3103-3106

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A type III polyketide synthase from Rhizobium etli condenses malonyl CoAs to a heptaketide pyrone with unusually high catalytic efficiency

M. Jeya, T. Kim, M. Kumar Tiwari, J. Li, H. Zhao and J. Lee, Mol. BioSyst., 2012, 8, 3103 DOI: 10.1039/C2MB25347J

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