Comparison of aspartate transcarbamoylase regulation in Pseudomonas alcaligenes and Pseudomonas mendocina.
The regulation of aspartate transcarbamoylase activity in cell extracts of Pseudomonas alcaligenes ATCC 14909 and Pseudomonas mendocina ATCC 25411 was compared. Under saturating substrate concentrations, pyrophosphate, CTP, UDP and ADP were highly inhibitory of the P. alcaligenes transcarbamoylase activity while pyrophosphate, UDP, ADP, ATP and GTP were the most effective inhibitors of the P. mendocina transcarbamoylase. By examining transcarbamoylase inhibition by ribonucleotide triphosphates, it was possible to differentiate these species assigned to different DNA homology groups and such an analysis might prove useful in the reclassification of Pseudomonas species.
Santiago
Manuel F
MF
Olson Biochemistry Laboratories, Department of Chemistry and Biochemistry, South Dakota State University, Brookings, SD 57007, USA.
West
Thomas P
TP
D001221:Aspartate Carbamoyltransferase / Q000378:metabolism*; D011756:Diphosphates / Q000378:metabolism; D009711:Nucleotides / Q000378:metabolism; D010710:Phosphates / Q000378:metabolism; D011549:Pseudomonas / Q000145:classification / Q000201:enzymology*
D011756:Diphosphates; D009711:Nucleotides; D010710:Phosphates; D001221:Aspartate Carbamoyltransferase