Inhibition of triosephosphate isomerase in boar spermatozoa by (S)-3-chlorolactaldehyde.
Mature epididymal boar spermatozoa converted fructose and glycerol to carbon dioxide but in the presence of 3-chloro-1-hydroxyacetone these oxidations were inhibited. When the substrate was fructose, there was an increase in the amounts of fructose 1,6-bisphosphate and dihydroxyacetone phosphate but these glycolytic intermediates did not accumulate when glycerol was the substrate. Examination of enzyme activities in mature boar spermatozoa incubated with 3-chloro-1-hydroxyacetone, which is metabolised in vitro to (S)-3-chlorolactaldehyde, confirmed that glyceraldehyde 3-phosphate dehydrogenase and triosephosphate isomerase were both inhibited to equivalent degrees by this metabolite.
D000447:Aldehydes / Q000494:pharmacology*; D000818:Animals; D002238:Carbohydrate Epimerases / Q000037:antagonists & inhibitors*; D005632:Fructose / Q000378:metabolism; D005990:Glycerol / Q000378:metabolism; D066298:In Vitro Techniques; D007700:Kinetics; D007773:Lactates / Q000378:metabolism; D008297:Male; D013094:Spermatozoa / Q000201:enzymology*; D013552:Swine; D014305:Triose-Phosphate Isomerase / Q000037:antagonists & inhibitors*
D000447:Aldehydes; D007773:Lactates; D005632:Fructose; C045799:3-chlorolactaldehyde; D002238:Carbohydrate Epimerases; D014305:Triose-Phosphate Isomerase; D005990:Glycerol