Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 89, Issue 3, Pages 739-746Publisher
SPRINGER
DOI: 10.1007/s00253-010-2924-5
Keywords
Rhodococcus erythropolis; Aminoalcohol dehydrogenase; Aminoalcohol metabolism; GntR family transcriptional regulator
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Funding
- Japan Society for the Promotion of Science (JSPS) [20380051]
- Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan
- Grants-in-Aid for Scientific Research [20380051] Funding Source: KAKEN
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NADP(+)-dependent aminoalcohol dehydrogenase (AADH) of Rhodococcus erythropolis MAK154 catalyzes the reduction of (S)-1-phenyl-1-keto-2-methylaminopropane ((S)-MAK) to d-pseudoephedrine, which is used as a pharmaceutical. AADH is suggested to participate in aminoalcohol or aminoketone metabolism in this organism because it is induced by the addition of several aminoalcohols, such as 1-amino-2-propanol. Genetic analysis of around the aadh gene showed that some open reading frames (ORFs) are involved in this metabolic pathway. Four of these ORFs might form a carboxysome-like polyhedral organelle, and others are predicted to encode aminotransferase, aldehyde dehydrogenase, phosphotransferase, and regulator protein. OrfE, a homologous ORF of the FadR subfamily of GntR transcriptional regulators, lies downstream from aadh. To investigate whether or not orfE plays a role in the regulation of aadh expression, the gene disruption mutant of R. erythropolis MAK154 was constructed. The Delta orfE strain showed higher AADH activity than wild-type strain. In addition, a transformed strain, which harbored multi-orfE, showed no AADH activity even in the induced condition with 1-amino-2-propanol. These results suggest that OrfE is a negative regulator that represses aadh expression in the absence of 1-amino-2-propanol.
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