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: A quinonoid is an intermediate of oxidative deamination reaction catalyzed by Dopa decarboxylase.
    Author: Bertoldi M, Cellini B, Maras B, Voltattorni CB.
    Journal: FEBS Lett; 2005 Sep 26; 579(23):5175-80. PubMed ID: 16150447.
    Abstract:
    The reactions of Dopa decarboxylase (DDC) with l- and d-enantiomers of tryptophan methyl ester are described. Although both the enantiomers bind to the active site of the enzyme with similar affinity, their binding modes are different. l-enantiomer binds in an unproductive mode, while d-enantiomer acts as an oxidative deamination substrate. For the first time a quinonoid has been detected as intermediate of this reaction. By using rapid-scanning stopped-flow kinetic technique rate constants for formation and decay of this species have been determined. All these data, besides validating the functional DDC active site model, represent an important step toward the elucidation of the catalytic pathway of oxidative deamination.
    [Abstract] [Full Text] [Related] [New Search]