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- W1569362186 abstract "Abstract Information concerning the mechanism of action of formylglycinamide ribonucleotide (FGAR) amidotransferase from chicken liver has been obtained from initial rate studies of the reaction of the three substrates of the enzyme system. The data are consistent with the belief that the substrates add sequentially to form a quaternary complex with the enzyme before undergoing reaction with release of products, and that glutamine adds first to the enzyme with ATP and FGAR adding randomly thereafter (partially compulsory order mechanism). Further studies with competitive and product inhibitors have led to this same conclusion. It was observed that albizziin, a competitive inhibitor of glutamine, acted as a mixed type inhibitor of the enzyme with respect to the other substrates. β,γ-5'-Adenylyl methylene diphosphonate, a competitive antagonist of ATP, acted as an uncompetitive and noncompetitive inhibitor of the enzyme with respect to glutamine and FGAR, respectively. Similarly, ADP functions as a competitive product inhibitor of the enzyme with respect to ATP but shows uncompetitive and mixed type inhibition patterns relative to glutamine and FGAR, respectively." @default.
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- W1569362186 date "1971-08-01" @default.
- W1569362186 modified "2023-10-17" @default.
- W1569362186 title "Biosynthesis of the Purines" @default.
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- W1569362186 doi "https://doi.org/10.1016/s0021-9258(18)61994-5" @default.
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