Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Chemical Compound Review:

SureCN850803 [(2R,3S,4R)-5-amino-3,4- dihydroxy-oxolan-2...

Synonyms: CHEBI:17284, AC1MIY2J, 14050-66-9, Phosphoribosylamine, 5-O-phosphono-D-ribofuranosylamine

Holmes, E.W. et al., Bera, A.K. et al., Wang, W. et al., Rudolph, J. et al.

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on Phosphoribosylamine

These results indicate that glutamine P-Rib-P-P amidotransferase or ammonia P-Rib-P-P aminotransferase or both are important for phosphoribosylamine synthesis, but that ammonia ribose-5-phosphate aminotransferase activity probably does not play a significant role in this eukaryotic cell line [1].
Three enzyme reactions have been reported to catalyze the synthesis of phosphoribosylamine in eukaryotic cells [1].
The defect in purine biosynthesis in the mutant cell line was localized to the synthesis of phosphoribosylamine [1].
Glutamine is hydrolyzed to glutamate plus NH(3) at an N-terminal glutaminase site, and NH(3) is transferred through a 20-A hydrophobic channel to a distal PRPP site for synthesis of phosphoribosylamine [2].
Glycinamide ribonucleotide synthetase (GAR-syn) catalyzes the second step of the de novo purine biosynthetic pathway; the conversion of phosphoribosylamine, glycine, and ATP to glycinamide ribonucleotide (GAR), ADP, and Pi [3].

Biological context of Phosphoribosylamine

Binding of PRPP is required to activate the glutaminase site (termed interdomain signaling) to prevent the wasteful hydrolysis of glutamine in the absence of phosphoribosylamine synthesis [2].

Gene context of Phosphoribosylamine

Investigation of the mechanism of phosphoribosylamine transfer from glutamine phosphoribosylpyrophosphate amidotransferase to glycinamide ribonucleotide synthetase [4].

References

A purine auxotroph deficient in phosphoribosylpyrophosphate amidotransferase and phosphoribosylpyrophosphate aminotransferase activities with normal activity of ribose-5-phosphate aminotransferase. Holmes, E.W., King, G.L., Leyva, A., Singer, S.C. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
Dual role for the glutamine phosphoribosylpyrophosphate amidotransferase ammonia channel. Interdomain signaling and intermediate channeling. Bera, A.K., Smith, J.L., Zalkin, H. J. Biol. Chem. (2000) [Pubmed]
X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli. Wang, W., Kappock, T.J., Stubbe, J., Ealick, S.E. Biochemistry (1998) [Pubmed]
Investigation of the mechanism of phosphoribosylamine transfer from glutamine phosphoribosylpyrophosphate amidotransferase to glycinamide ribonucleotide synthetase. Rudolph, J., Stubbe, J. Biochemistry (1995) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.