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Presence, preliminary properties and partial purification of 5-phosphoribosylpyrophosphate amidotransferase fromArtemiasp.

Authors
Journal
Biochimica et Biophysica Acta (BBA) - General Subjects
0304-4165
Publisher
Elsevier
Publication Date
Volume
1033
Issue
1
Identifiers
DOI: 10.1016/0304-4165(90)90203-9
Keywords
  • Phosphoribosylpyrophosphate Amidotransferase
  • Purine
  • (Artemia)

Abstract

Abstract 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 K m 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′″′-p 1, p 4-diguanosine tetraphosphate.

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