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Wiley, Angewandte Chemie International Edition, 26(43), p. 3425-3429, 2004

DOI: 10.1002/anie.200453353

Wiley, Angewandte Chemie, 26(116), p. 3507-3511, 2004

DOI: 10.1002/ange.200453353

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Structural Analysis of 1-Aminocyclopropane-1-Carboxylate Deaminase: Observation of an Aminyl Intermediate and Identification of Tyr 294 as the Active-Site Nucleophile

Journal article published in 2004 by Subramanian Karthikeyan Dr, Subramanian Karthikeyan, Zongbao Zhao Dr, Zongbao Zhao ORCID, Chai-Lin Kao Dr, Chai-Lin Kao, Qingxian Zhou, Zhihua Tao, Hong Zhang Prof. Dr, Hong Zhang, Hung-Wen Liu Prof. Dr, Hung-Wen Liu
This paper is available in a repository.
This paper is available in a repository.

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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.