Issue 11, 2012
From the journal:

Molecular BioSystems

The Botrytis cinerea type III polyketide synthase shows unprecedented high catalytic efficiency toward long chain acyl-CoAs†

Marimuthu Jeya,a   Tae-Su Kim,a   Manish Kumar Tiwari,a   Jinglin Li,a   Huimin Zhao*b  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 University of Illinois, Departments of Chemical and Biomolecular Engineering, Chemistry and Bioengineering, Institute for Genomic Biology, Center for Biophysics and Computational Biology, 600 South Mathews Avenue, Urbana, IL 61801, USA
E-mail: zhao5@illinois.edu
Fax: +1 217-333-5052

Abstract

BPKS from Botrytis cinerea is a novel type III polyketide synthase that accepts C4–C18 aliphatic acyl-CoAs and benzoyl-CoA as the starters to form pyrones, resorcylic acids and resorcinols through sequential condensation with malonyl-CoA. The catalytic efficiency (kcat/Km) of BPKS was 2.8 × 105 s−1 M−1 for palmitoyl-CoA, the highest ever reported. Substrate docking analyses addressed the unique features of BPKS such as its high activity and high specificity toward long chain acyl-CoAs.

Graphical abstract: The Botrytis cinerea type III polyketide synthase shows unprecedented high catalytic efficiency toward long chain acyl-CoAs

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Article information

DOI
https://doi.org/10.1039/C2MB25282A
Article type
Communication
Submitted
17 Jul 2012
Accepted
23 Aug 2012
First published
24 Aug 2012

Mol. BioSyst., 2012,8, 2864-2867

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The Botrytis cinerea type III polyketide synthase shows unprecedented high catalytic efficiency toward long chain acyl-CoAs

M. Jeya, T. Kim, M. K. Tiwari, J. Li, H. Zhao and J. Lee, Mol. BioSyst., 2012, 8, 2864 DOI: 10.1039/C2MB25282A

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