This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kotowska, M.
Right arrow Articles by Kuczek, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kotowska, M.
Right arrow Articles by Kuczek, K.
Agricola
Right arrow Articles by Kotowska, M.
Right arrow Articles by Kuczek, K.

Next Article 

Applied and Environmental Microbiology, February 2009, p. 887-896, Vol. 75, No. 4
0099-2240/09/$08.00+0     doi:10.1128/AEM.01371-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Type II Thioesterase ScoT, Associated with Streptomyces coelicolor A3(2) Modular Polyketide Synthase Cpk, Hydrolyzes Acyl Residues and Has a Preference for Propionate{triangledown} ,{dagger}

Magdalena Kotowska,1* Krzysztof Pawlik,1 Aleksandra Smulczyk-Krawczyszyn ,1,{ddagger} Hubert Bartosz-Bechowski,2 and Katarzyna Kuczek1

Department of Microbiology, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, ul. Weigla 12, 53-114 Wroclaw, Poland,1 Faculty of Chemistry, University of Wroclaw, ul. F. Joliot-Curie 14, 50-383 Wroclaw, Poland2

Received 19 June 2008/ Accepted 2 December 2008

Type II thioesterases (TE IIs) were shown to maintain the efficiency of polyketide synthases (PKSs) by removing acyl residues blocking extension modules. However, the substrate specificity and kinetic parameters of these enzymes differ, which may have significant consequences when they are included in engineered hybrid systems for the production of novel compounds. Here we show that thioesterase ScoT associated with polyketide synthase Cpk from Streptomyces coelicolor A3(2) is able to hydrolyze acetyl, propionyl, and butyryl residues, which is consistent with its editing function. This enzyme clearly prefers propionate, in contrast to the TE IIs tested previously, and this indicates that it may have a role in control of the starter unit. We also determined activities of ScoT mutants and concluded that this enzyme is an {alpha} hydrolase with Ser90 and His224 in its active site.


* Corresponding author. Mailing address: Department of Microbiology, Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, ul. Weigla 12, 53-114 Wroclaw, Poland. Phone: 48 (71) 3371172, ext. 184. Fax: 48 (71) 3371382. E-mail: szulc{at}iitd.pan.wroc.pl

{triangledown} Published ahead of print on 12 December 2008.

{dagger} Supplemental material for this article may be found at http://aem.asm.org/.

{ddagger} Present address: MEDianus sp. z o.o., ul. Cystersow 13/2, 31-553 Krakow, Poland.


Applied and Environmental Microbiology, February 2009, p. 887-896, Vol. 75, No. 4
0099-2240/09/$08.00+0     doi:10.1128/AEM.01371-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.