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Updated: Jul 15, 2026

Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli
Published on: August 3, 2017
A mutation causing constitutive synthesis of the pyruvate dehydrogenase complex in Escherichia coli is located within
D J Haydon1, M A Quail, J R Guest
1Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, UK.
Abstract:
The aceE-aceF-lpd genes encoding the pyruvate dehydrogenase (PDH) complex of Escherichia coli are preceded by a gene encoding a putative transcriptional regulator, PdhR (formerly designated GenA). Enzymological tests and studies with pdhR-lacZ and aceE-lacZ translational fusions have shown that a constitutive mutation (acec816), which increases PDH complex synthesis to the pyruvate-induced level in the absence of inducer, is recessive to the wild-type pdhR gene in trans. Sequence comparisons further showed that the acec816 mutation affects a single site in the pdhR gene leading to an Arg118 (CGU)-->Cys (UGU) substitution in the PdhR protein. The results support the view that synthesis of the PDH complex is regulated from the pdhR promoter of a pdhR-aceEF-lpd operon.
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