PRESENCE, PRELIMINARY PROPERTIES AND PARTIAL-PURIFICATION OF 5-PHOSPHORIBOSYLPYROPHOSPHATE AMIDOTRANSFERASE FROM ARTEMIA SP

5′-Phosphoribosylpyrophosphate amidotransferase, which catalyzes the synthesis of phosphoribosylamine in the de novo synthesis of purine nucleotides, has been detected and partially purified approx . 800-fold from Artemia sp. nauplii. The apparent Km values for 5′-phosphoribosyl 1-pyrophosphate as substrate were 0.7 mM and 0.4 mM in the presence of glutamine and ammonia as nitrogenous sources, respectively, and the enzymatic activity was inhibited by purine 5′-ribonucleotide compounds and 5′, 5′″′-p1, p4-diguanosine tetraphosphate. © 1990.