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.
Departmento de Bioquímica, Facultad de Medicina, Universidad Autónoma de Madrid, Spain.
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Liras
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Argomaniz
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Llorente
D000582:Amidophosphoribosyltransferase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D000641:Ammonia / Q000494:pharmacology; D000818:Animals; D001156:Artemia / Q000201:enzymology* / Q000254:growth & development; D002845:Chromatography; D005973:Glutamine / Q000494:pharmacology; D007700:Kinetics; D010430:Pentosyltransferases / Q000378:metabolism*; D010754:Phosphoribosyl Pyrophosphate / Q000378:metabolism; D011685:Purine Nucleotides / Q000494:pharmacology
D011685:Purine Nucleotides; D005973:Glutamine; D010754:Phosphoribosyl Pyrophosphate; D000641:Ammonia; D010430:Pentosyltransferases; D000582:Amidophosphoribosyltransferase