These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: The enzymatic conversion of dihydroneopterin triphosphate to tripolyphosphate and 6-pyruvoyl-tetrahydropterin, an intermediate in the biosynthesis of other pterins in Drosophila melanogaster.
    Author: Switchenko AC, Brown GM.
    Journal: J Biol Chem; 1985 Mar 10; 260(5):2945-51. PubMed ID: 3919013.
    Abstract:
    The enzyme, previously called "sepiapterin synthase A," has been purified by approximately 700-fold from the heads of Drosophila melanogaster. This enzyme catalyzes the Mg2+-dependent conversion of 2-amino-4-oxo-6-(D-erythro-1',2',3'-trihydroxypropyl)-7,8-dihydrop teridine triphosphate (dihydroneopterin triphosphate or H2-NTP) to two products, one of which we have identified as tripolyphosphate. The other product is a phosphate-free, unstable compound which is an intermediate in the biosynthesis of several other naturally occurring pterins in Drosophila. This product is stable enough under anaerobic conditions to allow it to be characterized as 6-pyruvoyl-5,6,7,8-tetrahydropterin (6-pyruvoyl-H4-pterin). The 3-carbon side chain was identified as a pyruvoyl group on the basis of the susceptibility of the enzymatic product to reduction with tritiated sodium borohydride and the determination of the amounts and the sites of incorporation of tritium resulting from this reduction. From these observations, we suggest that this enzyme be renamed "6-pyruvoyl-H4-pterin synthase."
    [Abstract] [Full Text] [Related] [New Search]