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Secondary alcohol dehydrogenase catalyzes the reduction of exogenous acetone to 2-propanol in Trichomonas vaginalis
R. Sutak, I. Hrdy, P. Dolezal, R. Cabala, M. Sedinová, J. Lewin, K. Harant, M. Müller, J. Tachezy
Language English Country England, Great Britain
Document type Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't
NLK
Free Medical Journals
from 2005 to 1 year ago
Medline Complete (EBSCOhost)
from 2005-01-01 to 1 year ago
Wiley Online Library (archiv)
from 1967-01-01 to 2012-12-31
Wiley Free Content
from 2005 to 1 year ago
- MeSH
- 2-Propanol metabolism MeSH
- Acetone metabolism MeSH
- Alcohol Oxidoreductases genetics metabolism MeSH
- Models, Biological MeSH
- DNA Primers genetics MeSH
- Energy Metabolism MeSH
- Phylogeography MeSH
- Host-Parasite Interactions MeSH
- Catalysis MeSH
- Kinetics MeSH
- Humans MeSH
- Oxidation-Reduction MeSH
- Protozoan Proteins genetics metabolism MeSH
- Base Sequence MeSH
- Enzyme Stability MeSH
- Trichomonas vaginalis enzymology genetics pathogenicity MeSH
- Iron metabolism MeSH
- Check Tag
- Humans MeSH
- Male MeSH
- Female MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, N.I.H., Extramural MeSH
Secondary alcohols such as 2-propanol are readily produced by various anaerobic bacteria that possess secondary alcohol dehydrogenase (S-ADH), although production of 2-propanol is rare in eukaryotes. Specific bacterial-type S-ADH has been identified in a few unicellular eukaryotes, but its function is not known and the production of secondary alcohols has not been studied. We purified and characterized S-ADH from the human pathogen Trichomonas vaginalis. The kinetic properties and thermostability of T. vaginalis S-ADH were comparable with bacterial orthologues. The substantial activity of S-ADH in the parasite's cytosol was surprising, because only low amounts of ethanol and trace amounts of secondary alcohols were detected as metabolic end products. However, S-ADH provided the parasite with a high capacity to scavenge and reduce external acetone to 2-propanol. To maintain redox balance, the demand for reducing power to metabolize external acetone was compensated for by decreased cytosolic reduction of pyruvate to lactate and by hydrogenosomal metabolism of pyruvate. We speculate that hydrogen might be utilized to maintain cytosolic reducing power. The high activity of Tv-S-ADH together with the ability of T. vaginalis to modulate the metabolic fluxes indicate efficacious metabolic responsiveness that could be advantageous for rapid adaptation of the parasite to changes in the host environment.
Department of Analytical Chemistry Faculty of Science Charles University Prague Czech Republic
Department of Genetics and Microbiology Faculty of Science Charles University Prague Czech Republic
Department of Parasitology Faculty of Science Charles University Prague Czech Republic
Laboratory of Biochemical Parasitology The Rockefeller University New York NY USA
References provided by Crossref.org
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- $a Secondary alcohols such as 2-propanol are readily produced by various anaerobic bacteria that possess secondary alcohol dehydrogenase (S-ADH), although production of 2-propanol is rare in eukaryotes. Specific bacterial-type S-ADH has been identified in a few unicellular eukaryotes, but its function is not known and the production of secondary alcohols has not been studied. We purified and characterized S-ADH from the human pathogen Trichomonas vaginalis. The kinetic properties and thermostability of T. vaginalis S-ADH were comparable with bacterial orthologues. The substantial activity of S-ADH in the parasite's cytosol was surprising, because only low amounts of ethanol and trace amounts of secondary alcohols were detected as metabolic end products. However, S-ADH provided the parasite with a high capacity to scavenge and reduce external acetone to 2-propanol. To maintain redox balance, the demand for reducing power to metabolize external acetone was compensated for by decreased cytosolic reduction of pyruvate to lactate and by hydrogenosomal metabolism of pyruvate. We speculate that hydrogen might be utilized to maintain cytosolic reducing power. The high activity of Tv-S-ADH together with the ability of T. vaginalis to modulate the metabolic fluxes indicate efficacious metabolic responsiveness that could be advantageous for rapid adaptation of the parasite to changes in the host environment.
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