Diethylaminobenzaldehyde Is a Covalent, Irreversible Inactivator of ALDH7A1 | Zendy

Min Luo | Zendy; Kent S. Gates | Zendy; Michael T. Henzl | Zendy; John J. Tanner | Zendy

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Diethylaminobenzaldehyde Is a Covalent, Irreversible Inactivator of ALDH7A1

Author(s) -

Min Luo,

Kent S. Gates,

Michael T. Henzl,

John J. Tanner

Publication year - 2015

Publication title -

acs chemical biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.899

H-Index - 111

eISSN - 1554-8937

pISSN - 1554-8929

DOI - 10.1021/cb500977q

Subject(s) - aldehyde dehydrogenase , covalent bond , aldehyde , chemistry , enzyme , aldh2 , covalent binding , dehydrogenase , biochemistry , biophysics , combinatorial chemistry , biology , catalysis , organic chemistry

There is growing interest in aldehyde dehydrogenases (ALDHs) because of their overexpression in cancer stem cells and the ability to mediate resistance to cancer drugs. Here, we report the first crystal structure of an aldehyde dehydrogenase complexed with the inhibitor 4-diethylaminobenzaldehyde (DEAB). Contrary to the widely held belief that DEAB is a reversible inhibitor of ALDHs, we show that DEAB irreversibly inactivates ALDH7A1 via formation of a stable, covalent acyl-enzyme species.

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