Unknown

Dataset Information

0

Unexpected properties of NADP-dependent secondary alcohol dehydrogenase (ADH-1) in Trichomonas vaginalis and other microaerophilic parasites.


ABSTRACT: Our previous observation that NADP-dependent secondary alcohol dehydrogenase (ADH-1) is down-regulated in metronidazole-resistant Trichomonas vaginalis isolates prompted us to further characterise the enzyme. In addition to its canonical enzyme activity as a secondary alcohol dehydrogenase, a pronounced, so far unknown, background NADPH-oxidising activity in absence of any added substrate was observed when the recombinant enzyme or T. vaginalis extract were used. This activity was strongly enhanced at low oxygen concentrations. Unexpectedly, all functions of ADH-1 were efficiently inhibited by coenzyme A which is a cofactor of a number of key enzymes in T. vaginalis metabolism, i.e. pyruvate:ferredoxin oxidoreductase (PFOR). These observations could be extended to Entamoeba histolytica and Tritrichomonas foetus, both of which have a homologue of ADH-1, but not to Giardia lamblia which lacks an NADP-dependent secondary alcohol dehydrogenase. Although we could not identify the substrate of the observed background activity, we propose that ADH-1 functions as a major sink for NADPH in microaerophilic parasites at low oxygen tension.

SUBMITTER: Leitsch D 

PROVIDER: S-EPMC3682184 | BioStudies | 2013-01-01

REPOSITORIES: biostudies

Similar Datasets

1994-01-01 | S-EPMC1137204 | BioStudies
2012-01-01 | S-EPMC3536282 | BioStudies
2011-01-01 | S-EPMC3133181 | BioStudies
2017-01-01 | S-EPMC5624969 | BioStudies
1998-01-01 | S-EPMC1219401 | BioStudies
2015-01-01 | S-EPMC4542167 | BioStudies
1997-01-01 | S-EPMC1218725 | BioStudies
2015-01-01 | S-EPMC4518838 | BioStudies
1996-01-01 | S-EPMC1217309 | BioStudies
1968-01-01 | S-EPMC1198688 | BioStudies