@article{mbs:/content/journal/micro/10.1099/13500872-142-3-649, author = "Bramwell, Helena and Hunter, Lain S. and Coggins, John R. and Nimmo, Hugh G.", title = "Propionyl-CoA carboxylase from Streptomyces coelicolor A3(2) : cloning of the gene encoding the biotinlcontaining subunit", journal= "Microbiology", year = "1996", volume = "142", number = "3", pages = "649-655", doi = "https://doi.org/10.1099/13500872-142-3-649", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/13500872-142-3-649", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "Streptomyces coelicolor A3(2)", keywords = "acetyl-CoA carboxylase", keywords = "biotinylated proteins", keywords = "propionyl-CoA carboxylase", 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 β 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.", }