Structural analysis of 1-aminocyclopropane-1-carboxylate deaminase: Observation of an aminyl intermediate and identification of Tyr294 as the active-site nucleophile

Subramanian Karthikeyan, Zongbao Zhao, Chailin Kao, Qingxian Zhou, Zhihua Tao, Hong Zhang, Hung Wen Liu

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

Finding an angle of attack: Structural studies of 1-aminocyclopropane-1- carboxylate (ACC) deaminase complexed with the tight-binding inhibitor 1-amino-cyclopropanephosphonate (ACP, see picture) revealed the existence of an aminyl adduct intermediate. The crystal structure of the enzyme and mutation studies suggest that the ring cleavage of ACC is initiated by nucleophilic attack by Tyr294.

Original languageEnglish (US)
Pages (from-to)3425-3429
Number of pages5
JournalAngewandte Chemie - International Edition
Volume43
Issue number26
DOIs
StatePublished - Jun 28 2004

Keywords

  • Enzyme catalysis
  • Enzymes
  • Proteins
  • Reaction mechanisms
  • Structure elucidation

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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