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

doi:10.1021/ja068636z

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

Biotechnology Institute

Research output: Contribution to journal › Article › peer-review

32 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 language	English (US)
Pages (from-to)	4120-4121
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	129
Issue number	14
DOIs	https://doi.org/10.1021/ja068636z
State	Published - Apr 11 2007

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

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.",

author = "Bera, {Asim K.} and Polovnikova, {Lena S.} and Juliatek Roestamadji and Widlanski, {Theodore S.} and Kenyon, {George L.} and McLeish, {Michael J.} and Hasson, {Miriam S.}",

year = "2007",

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doi = "10.1021/ja068636z",

language = "English (US)",

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journal = "Journal of the American Chemical Society",

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T1 - Mechanism-based inactivation of benzoylformate decarboxylase, a thiamin diphosphate-dependent enzyme

AU - Bera, Asim K.

AU - Polovnikova, Lena S.

AU - Roestamadji, Juliatek

AU - Widlanski, Theodore S.

AU - Kenyon, George L.

AU - McLeish, Michael J.

AU - Hasson, Miriam S.

PY - 2007/4/11

Y1 - 2007/4/11

N2 - 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.

AB - 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.

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 14

ER -

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

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