Hydrogenosomal succinate thiokinase in Tritrichomonas foetus and Trichomonas vaginalis.
Succinate thiokinase displays a diversity of nucleotide specificity and molecular size throughout Nature. Eukaryotes and Gram-positive bacteria possess distinct 'small' (dimeric) thiokinase enzymes which are specific for adenine (ADP) or guanine (GDP) nucleotides, whereas Gram-negative bacteria contain a single 'large' (tetrameric) enzyme which utilizes both nucleotides. Succinate thiokinase activities, both ADP- and GDP-dependent, were shown to be hydrogenosomal in Tritrichomonas foetus and Trichomonas vaginalis. Surprisingly, the 'small' enzyme was found in T. foetus whereas T. vaginalis contained a 'large' enzyme.
Jenkins
T M
TM
Rockefeller University, New York, NY 10021.
Gorrell
T E
TE
Müller
M
M
Weitzman
P D
PD
D000244:Adenosine Diphosphate / Q000378:metabolism; D000818:Animals; D002458:Cell Fractionation; D002500:Centrifugation, Isopycnic; D002850:Chromatography, Gel; D006153:Guanosine Diphosphate / Q000378:metabolism; D015388:Organelles / Q000201:enzymology*; D013379:Substrate Specificity; D013389:Succinate-CoA Ligases / Q000378:metabolism*; D014246:Trichomonas vaginalis / Q000201:enzymology*; D014318:Tritrichomonas / Q000201:enzymology*
D006153:Guanosine Diphosphate; D000244:Adenosine Diphosphate; D013389:Succinate-CoA Ligases