1887

Abstract

In 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 However, propionyl-CoA carboxylase (PCC) activity was detected at substantial levels. Fixation of CO by ACC and PCC occurs by covalent bonding of CO to a biotin-containing protein. Most bacteria have a single small biotinylated protein of approximately 22 kDa, but 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 () was cloned.

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/content/journal/micro/10.1099/13500872-142-3-649
1996-03-01
2019-10-18
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/13500872-142-3-649
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