Propionyl-CoA carboxylase from Streptomyces coelicolor A3(2): cloning of the gene encoding the biotin-containing subunit

Bramwell, H., Hunter, I. S., Coggins, J. R. and Nimmo, H. G. (1996) Propionyl-CoA carboxylase from Streptomyces coelicolor A3(2): cloning of the gene encoding the biotin-containing subunit. Microbiology, 142(3), pp. 649-655. (doi: 10.1099/13500872-142-3-649) (PMID:8868440)

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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 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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Nimmo, Professor Hugh and Coggins, Professor John
Authors: Bramwell, H., Hunter, I. S., Coggins, J. R., and Nimmo, H. G.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Microbiology
Publisher:Microbiology Society
ISSN:1350-0872
ISSN (Online):1465-2080

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