Dialkylglycine decarboxylase structure: Bifunctional active site and alkali metal sites

Michael D. Toney, Erhard Hohenester, Sandra W. Cowan, Johan N. Jansonius

Research output: Contribution to journalArticle

174 Scopus citations

Abstract

The structure of the bifunctional, pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase was determined to 2.1-angstrom resolution. Model building suggests that a single cleavage site catalyzes both decarboxylation and transamination by maximizing stereoelectronic advantages and providing electrostatic and general base catalysis. The enzyme contains two binding sites for alkali metal ions. One is located near the active site and accounts for the dependence of activity on potassium ions. The other is located at the carboxyl terminus of an a helix. These sites help show how proteins can specifically bind alkali metals and how these ions can exert functional effects.

Original languageEnglish (US)
Pages (from-to)756-759
Number of pages4
JournalScience
Volume261
Issue number5122
StatePublished - Aug 6 1993

ASJC Scopus subject areas

  • General

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    Toney, M. D., Hohenester, E., Cowan, S. W., & Jansonius, J. N. (1993). Dialkylglycine decarboxylase structure: Bifunctional active site and alkali metal sites. Science, 261(5122), 756-759.