Details
| Original language | English |
|---|---|
| Pages (from-to) | 587-596 |
| Number of pages | 10 |
| Journal | Chemistry and Biology |
| Volume | 13 |
| Issue number | 6 |
| Publication status | Published - 1 Jun 2006 |
| Externally published | Yes |
Abstract
Acyl carrier proteins (ACPs) play a fundamental role in directing intermediates among the enzyme active sites of fatty acid and polyketide synthases (PKSs). In this paper, we demonstrate that the Streptomyces coelicolor (S. coelicolor) actinorhodin (act) PKS ACP can catalyze transfer of malonate to type II S. coelicolor fatty acid synthase (FAS) and other PKS ACPs in vitro. The reciprocal transfer from S. coelicolor FAS ACP to a PKS ACP was not observed. Several mutations in both act ACP and S. coelicolor FAS ACP could be classified by their participation in either donation or acceptance of this malonyl group. These mutations indicated that self-malonylation and malonyl transfer could be completely decoupled, implying that they were separate processes and that a FAS ACP could be converted from a non-malonyl-transferring protein to one with malonyl transferase activity.
Keywords
- CHEMBIO
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Medicine
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Pharmacology, Toxicology and Pharmaceutics(all)
- Pharmacology
- Pharmacology, Toxicology and Pharmaceutics(all)
- Drug Discovery
- Biochemistry, Genetics and Molecular Biology(all)
- Clinical Biochemistry
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In: Chemistry and Biology, Vol. 13, No. 6, 01.06.2006, p. 587-596.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The Malonyl Transferase Activity of Type II Polyketide Synthase Acyl Carrier Proteins
AU - Arthur, Christopher J.
AU - Szafranska, Anna E.
AU - Long, Jed
AU - Mills, Jane
AU - Cox, Russell J.
AU - Findlow, Stuart C.
AU - Simpson, Thomas J.
AU - Crump, Matthew P.
AU - Crosby, John
N1 - Funding information: We thank the Wellcome Trust and the Higher Education Funding Council for England for equipment support for the 600 MHz spectrometer at Southampton University and Bristol University and the Biotechnology and Biological Sciences Research Council (7/B20055). We also thank the Engineering and Physical Sciences Research Council (C.J.A) and the Overseas Research Students Awards Scheme (A.E.S.) for studentships.
PY - 2006/6/1
Y1 - 2006/6/1
N2 - Acyl carrier proteins (ACPs) play a fundamental role in directing intermediates among the enzyme active sites of fatty acid and polyketide synthases (PKSs). In this paper, we demonstrate that the Streptomyces coelicolor (S. coelicolor) actinorhodin (act) PKS ACP can catalyze transfer of malonate to type II S. coelicolor fatty acid synthase (FAS) and other PKS ACPs in vitro. The reciprocal transfer from S. coelicolor FAS ACP to a PKS ACP was not observed. Several mutations in both act ACP and S. coelicolor FAS ACP could be classified by their participation in either donation or acceptance of this malonyl group. These mutations indicated that self-malonylation and malonyl transfer could be completely decoupled, implying that they were separate processes and that a FAS ACP could be converted from a non-malonyl-transferring protein to one with malonyl transferase activity.
AB - Acyl carrier proteins (ACPs) play a fundamental role in directing intermediates among the enzyme active sites of fatty acid and polyketide synthases (PKSs). In this paper, we demonstrate that the Streptomyces coelicolor (S. coelicolor) actinorhodin (act) PKS ACP can catalyze transfer of malonate to type II S. coelicolor fatty acid synthase (FAS) and other PKS ACPs in vitro. The reciprocal transfer from S. coelicolor FAS ACP to a PKS ACP was not observed. Several mutations in both act ACP and S. coelicolor FAS ACP could be classified by their participation in either donation or acceptance of this malonyl group. These mutations indicated that self-malonylation and malonyl transfer could be completely decoupled, implying that they were separate processes and that a FAS ACP could be converted from a non-malonyl-transferring protein to one with malonyl transferase activity.
KW - CHEMBIO
UR - http://www.scopus.com/inward/record.url?scp=33745205061&partnerID=8YFLogxK
U2 - 10.1016/j.chembiol.2006.03.010
DO - 10.1016/j.chembiol.2006.03.010
M3 - Article
C2 - 16793516
AN - SCOPUS:33745205061
VL - 13
SP - 587
EP - 596
JO - Chemistry and Biology
JF - Chemistry and Biology
SN - 1074-5521
IS - 6
ER -