Article thumbnail

The protonated form of 1-N6-etheno-[erythro-9-(2-hydroxy-3-nonyl)] adenine is identified at the active site of adenosine deaminase

By Valeria R. Caiolfa, David Gill and Abraham H. Parola

Abstract

AbstractA novel fluorescent competitive inhibitor of adenosine deaminase (EC 3.5.4.4) (ADA), 1-N6-etheno-[erythro-9-(2-hydroxy-3-nonyl)] adenine (ϵ-EHNA), is protonated at the active site of the enzyme. In ϵ-EHNA [K1 = (4.06 ± 1.00) 10−6 M] part of the competive inhibition of EHNA is combined with spectroscopic properties of etheno-adenines. Computer subtraction of the fluorescence excitation spectrum of ADA from that of its equimolar complex with ϵ-EHNA yielded the corrected excitation spectrum of ϵ-EHNA at the active site of the enzyme. This spectrum mimics that of ϵ-EHNA at pH 5.5 in buffer solution and is suggested to indicate a shift in protonation equilibrium at the active site

Publisher: Published by Elsevier B.V.
Year: 1990
DOI identifier: 10.1016/0014-5793(90)80055-N
OAI identifier:

Suggested articles


To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.