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: Enzyme-activated inhibition of bacterial D-amino acid transaminase by beta-cyano-D-alanine.
    Author: Ueno H, Soper TS, Manning JM.
    Journal: Biochem Biophys Res Commun; 1984 Jul 31; 122(2):485-91. PubMed ID: 6466323.
    Abstract:
    beta-Cyano-D-alanine is an efficient suicide substrate (Ki = 10 microM) of D-amino acid transaminase. This apparent inactivation is temperature dependent: it is irreversible at 10 degrees C or below and becomes progressively reversible at higher temperatures. Since at higher temperatures the apparent reactivation process predominates over the inactivation reaction, the reactivation process is considered to be endothermic. The nature of this reversibility suggests the formation of a heat labile bond between the inhibitor molecule and a nucleophilic group on the enzyme.
    [Abstract] [Full Text] [Related] [New Search]