Skip NavigationSkip to Content

Contrasting behavior of conformationally locked carbocyclic nucleosides of adenosine and cytidine as substrates for deaminases

  1. Author:
    Marquez, V. E.
    Schroeder, G. K.
    Ludek, O. R.
    Siddiqui, M. A.
    Ezzitouni, A.
    Wolfenden, R.
  2. Author Address

    Laboratory of Medicinal Chemistry, Center for Cancer Research, National Cancer Institute at Frederick, National Institutes of Health, Frederick, Maryland, USA. marquezv@dc37a.nci.nih.gov
    1. Year: 2009
    2. Date: May
    3. Epub Date: 2/26/2010
  1. Journal: Nucleosides, nucleotides & nucleic acids
    1. 28
    2. 5
    3. Pages: 614-32
  2. Type of Article: Article
  3. ISSN: 1532-2335 (Electronic);1525-7770 (Linking)
  1. Abstract:

    In addition to the already known differences between adenosine deaminase (ADA) and cytidine deaminase (CDA) in terms of their tertiary structure, the sphere of Zn(+2) coordination, and their reverse stereochemical preference, we present evidence that the enzymes also differ significantly in terms of the North/South conformational preferences for their substrates and the extent to which the lack of the O(4') oxygen affects the kinetics of the enzymatic deamination of carbocyclic substrates. The carbocyclic nucleoside substrates used in this study have either a flexible cyclopentane ring or a rigid bicyclo[3.1.0]hexane scaffold.

    See More

External Sources

  1. DOI: 10.1080/15257770903091904
  2. PMID: 20183605
  3. PMCID: PMC2910114
  4. NIHMSID: Nihms217050

Library Notes

  1. Fiscal Year: FY2008-2009
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel