f Propionyl-CoA carboxylase from Streptomyces coelicolor A3(2): cloning of the gene encoding the biotin-containing subunit
- Authors: Helena Bramwell†, Lain S. Hunter‡, John R. Coggins, Hugh G. Nimmo*M
- *Author for correspondence: Hugh G. Nimmo. Tel: +44 141 330 4721. Fax: +44 141 330 4447. e-mail: firstname.lastname@example.org
- Microbiology, March 1996 142: 649-655, doi: 10.1099/13500872-142-3-649
- Subject: Biochemistry
- Published Online:
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 α 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 α 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.
- Keyword(s): propionyl-CoA carboxylase, Streptomyces coelicolor A3(2), acetyl-CoA carboxylase, biotinylated proteins
© Society for General Microbiology 1996 | Published by the Microbiology Society
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