-
Je něco špatně v tomto záznamu ?
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
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články, Research Support, N.I.H., Extramural, práce podpořená grantem
NLK
Free Medical Journals
od 2005 do Před 1 rokem
Medline Complete (EBSCOhost)
od 2005-01-01 do Před 1 rokem
Wiley Online Library (archiv)
od 1967-01-01 do 2012-12-31
Wiley Free Content
od 2005 do Před 1 rokem
- MeSH
- 2-propanol metabolismus MeSH
- aceton metabolismus MeSH
- alkoholoxidoreduktasy genetika metabolismus MeSH
- biologické modely MeSH
- DNA primery genetika MeSH
- energetický metabolismus MeSH
- fylogeografie MeSH
- interakce hostitele a parazita MeSH
- katalýza MeSH
- kinetika MeSH
- lidé MeSH
- oxidace-redukce MeSH
- protozoální proteiny genetika metabolismus MeSH
- sekvence nukleotidů MeSH
- stabilita enzymů MeSH
- Trichomonas vaginalis enzymologie genetika patogenita MeSH
- železo metabolismus MeSH
- Check Tag
- lidé MeSH
- mužské pohlaví MeSH
- ženské pohlaví MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem 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
Citace poskytuje Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc12034452
- 003
- CZ-PrNML
- 005
- 20160626100439.0
- 007
- ta
- 008
- 121023s2012 enk f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1111/j.1742-4658.2012.08661.x $2 doi
- 035 __
- $a (PubMed)22686835
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a enk
- 100 1_
- $a Sutak, Robert $u Department of Parasitology, Faculty of Science, Charles University in Prague, Vinicna 7, Prague, Czech Republic
- 245 10
- $a Secondary alcohol dehydrogenase catalyzes the reduction of exogenous acetone to 2-propanol in Trichomonas vaginalis / $c R. Sutak, I. Hrdy, P. Dolezal, R. Cabala, M. Sedinová, J. Lewin, K. Harant, M. Müller, J. Tachezy
- 520 9_
- $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.
- 650 _2
- $a 2-propanol $x metabolismus $7 D019840
- 650 _2
- $a aceton $x metabolismus $7 D000096
- 650 _2
- $a alkoholoxidoreduktasy $x genetika $x metabolismus $7 D000429
- 650 _2
- $a sekvence nukleotidů $7 D001483
- 650 _2
- $a katalýza $7 D002384
- 650 _2
- $a DNA primery $x genetika $7 D017931
- 650 _2
- $a energetický metabolismus $7 D004734
- 650 _2
- $a stabilita enzymů $7 D004795
- 650 _2
- $a ženské pohlaví $7 D005260
- 650 _2
- $a interakce hostitele a parazita $7 D006790
- 650 _2
- $a lidé $7 D006801
- 650 _2
- $a železo $x metabolismus $7 D007501
- 650 _2
- $a kinetika $7 D007700
- 650 _2
- $a mužské pohlaví $7 D008297
- 650 _2
- $a biologické modely $7 D008954
- 650 _2
- $a oxidace-redukce $7 D010084
- 650 _2
- $a fylogeografie $7 D058974
- 650 _2
- $a protozoální proteiny $x genetika $x metabolismus $7 D015800
- 650 _2
- $a Trichomonas vaginalis $x enzymologie $x genetika $x patogenita $7 D014246
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a Research Support, N.I.H., Extramural $7 D052061
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Hrdy, Ivan $u Department of Parasitology, Faculty of Science, Charles University in Prague, Czech Republic
- 700 1_
- $a Doležal, Pavel, $d 1975- $7 xx0257242 $u Department of Parasitology, Faculty of Science, Charles University in Prague, Czech Republic
- 700 1_
- $a Čabala, Radomír, $d 1965- $7 uk2007300494 $u Department of Analytical Chemistry, Faculty of Science, Charles University in Prague, Czech Republic
- 700 1_
- $a Šedinová, Miroslava $7 xx0215602 $u Department of Parasitology, Faculty of Science, Charles University in Prague, Czech Republic
- 700 1_
- $a Lewin, Joern $u Laboratory of Biochemical Parasitology, The Rockefeller University, New York, NY, USA
- 700 1_
- $a Harant, Karel $u Department of Genetics and Microbiology, Faculty of Science, Charles University in Prague, Czech Republic
- 700 1_
- $a Müller, Miklos $u Laboratory of Biochemical Parasitology, The Rockefeller University, New York, NY, USA
- 700 1_
- $a Tachezy, Jan, $d 1958- $7 mzk2008442769 $u Department of Parasitology, Faculty of Science, Charles University in Prague, Czech Republic
- 773 0_
- $w MED00008414 $t The FEBS journal $x 1742-4658 $g Roč. 279, č. 15 (2012), s. 2768-2780
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/22686835 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y p $z 0
- 990 __
- $a 20121023 $b ABA008
- 991 __
- $a 20160626100623 $b ABA008
- 999 __
- $a ok $b bmc $g 956462 $s 791949
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2012 $b 279 $c 15 $d 2768-2780 $i 1742-4658 $m The FEBS journal $n FEBS J $x MED00008414
- LZP __
- $b NLK122 $a Pubmed-20121023
