Enzymic synthesis and cofactor activity of 3'-pyrophosphocoenzyme A.
The 3'-pyrophosphate derivative of CoA was synthesized by using the excreted 5'-to-3' pyrophosphoryl-transferring enzyme from Streptomyces adephospholyticus and ATP as donor and dephospho-CoA as acceptor. Cofactor activity of this new coenzyme A derivative was tested with Clostridium kluyveri phosphotransacetylase and hog heart succinic thiokinase. With the phosphotransacetylase, 3'-pyrophospho-CoA was found to be twice as active as CoA whereas dephospho-CoA was inactive. However, succinic thiokinase utilized all three types of CoA equally well. Adenosine 5'-monophosphate 3'-pyrophosphate also was synthesized and used as an analog of adenosine 5'-monophosphate 3'-monophosphate in the dog liver's sulfotransferase-catalyzed sulfate transfer from p-nitrophenyl sulfate to phenol. In contrast to the pyrophospho derivative of coenzyme A, adenosine 5'-monophosphate 3'-pyrophosphate was inactive as a cofactor.
D000818:Animals; D003065:Coenzyme A / Q000031:analogs & derivatives* / Q000378:metabolism; D007700:Kinetics; D010709:Phosphate Acetyltransferase / Q000378:metabolism; D010766:Phosphorylation; D013329:Structure-Activity Relationship; D013389:Succinate-CoA Ligases / Q000378:metabolism; D013552:Swine
C038113:3'-pyrophosphoryl-coenzyme A; D010709:Phosphate Acetyltransferase; D013389:Succinate-CoA Ligases; D003065:Coenzyme A