Mechanism-based inactivation of benzoylformate decarboxylase, a thiamin diphosphate-dependent enzyme

Asim K. Bera, Lena S. Polovnikova, Juliatek Roestamadji, Theodore S. Widlanski, George L. Kenyon, Michael J. McLeish, Miriam S. Hasson

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

Abstract

Benzoylformate decarboxylase (BFD) from Pseudomonas putida is a thiamin diphosphate-dependent enzyme that catalyzes the non-oxidative decarboxylation of benzoylformate. Here we report the discovery of a mechanism-based inhibitor of BFD that is unusual in that it covalently modifies the enzyme via active site phosphorylation. Incubation of BFD with benzoylphosphonate results in time- and concentration-dependent inactivation of the enzyme. X-ray crystallography reveals that the inactivation is due to the phosphorylation of an active site serine residue.

Original languageEnglish (US)
Pages (from-to)4120-4121
Number of pages2
JournalJournal of the American Chemical Society
Volume129
Issue number14
DOIs
StatePublished - Apr 11 2007

Fingerprint Dive into the research topics of 'Mechanism-based inactivation of benzoylformate decarboxylase, a thiamin diphosphate-dependent enzyme'. Together they form a unique fingerprint.

Cite this