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1Divisions of Biochemistry & Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK
2Divisions of Molecular Genetics, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK
* Author for correspondence: Hugh G. Nimmo. Tel: +44 141 330 4721. Fax: +44 141 330 4447. e-mail: gbca39@udcf.gla.ac.uk
ABSTRACT
In Streptomyces coelicolor A3(2), polyketides are made from malonyl-CoA, which is presumed to be derived from acetyl-CoA by the action of acetyl-CoA carboxylase (ACC). No ACC activity was found in cell-free extracts of S. coelicolor. However, propionyl-CoA carboxylase (PCC) activity was detected at substantial levels. Fixation of CO2 by ACC and PCC occurs by covalent bonding of CO2 to a biotin-containing protein. Most bacteria have a single small biotinylated protein of approximately 22 kDa, but S. coelicolor contains three larger biotin-containing proteins (approximately 145, 88 and 70 kDa). To determine which biotinylated protein was associated with PCC activity, the enzyme was purified and shown to comprise an 
subunit (biotin-containing) of 88 kDa and a ß subunit of 66 kDa. The N-terminal sequences of these proteins were determined and, using an oligonucleotide probe, the gene for the subunit (pccA) was cloned.
Present address: Department of Bioscience & Biotechnology, University of Strathclyde, Glasgow G1 1QX, UK.
Present address: Department of Human Metabolism & Clinical Biochemistry, University of Sheffield Medical School, Beech Hill Road, Sheffield S10 2RX, UK.
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