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THE MECHANISM AND SPECIFICITY OF GUANINE DEAMINASE

descriptionPublicationkeyboard_double_arrow_right Article 01 Aug 1967 English Publisher:Canadian Science PublishingJournal:Canadian Journal of Biochemistry, volume 45, pages 1,263-1,269 (issn: 0008-4018,

Authors: Joan E. Roy; Kenneth L. Roy;

doi: 10.1139/o67-147

pmid: 6067951

THE MECHANISM AND SPECIFICITY OF GUANINE DEAMINASE

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Abstract

Guanine deaminase from lingcod muscle has been found to remove chlorine from 2-chloro-6-hydroxypurine, hydrazine from 2-hydrazino-6-hydroxypurine, and methylamine from 2-methylamino-6-hydroxypurine, with xanthine as the product in all cases. Methylation of guanine on nitrogen atoms other than N-1 and substitutions at C-6 eliminate susceptibility to guanine deaminase. Kinetic data for the reaction of guanine deaminase with five substrates are presented and the results of a survey of possible inhibitors of the enzyme are given. The results tend to support a requirement by guanine deaminase for the lactam tautomeric form of the substrate.

Keywords

Guanine, Chemical Phenomena, Azaguanine, Chemistry, Organic, Fishes, Enzymes, Organic Chemistry Phenomena, Chemistry, Kinetics, Hydrazines, Aminohydrolases, Purines, Spectrophotometry, Animals, Chlorine

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