Human GMP synthetase.
The specific activity of GMP synthetase was measured in several human tissues and found to be highest in cultured skin fibroblasts, followed by bone marrow, leukocytes, erythrocytes, placenta, and liver. The enzyme from fibroblasts was purified approximately 50-fold by ammonium sulfate fractionation and gel filtration. The Km values were determined to be 4.9 microM for XMP, 270 microM for ATP, and 340 microM for glutamine. Ammonium sulfate could replace glutamine as the amino donor but was much less efficient. The enzyme was specific for ATP as the energy source. Unlike the calf thymus enzyme, the human enzyme has no requirement for a reduced sulfhydryl compound. Human GMP synthetase is inhibited by ATP, dATP, azaserine, and hydroxylamine.[1]References
- Human GMP synthetase. Page, T., Bakay, B., Nyhan, W.L. Int. J. Biochem. (1984) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg