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

35 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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10.1021/ja068636z

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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",

month = apr,

day = "11",

doi = "10.1021/ja068636z",

language = "English (US)",

volume = "129",

pages = "4120--4121",

journal = "Journal of the American Chemical Society",

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TY - JOUR

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.

UR - https://www.scopus.com/pages/publications/34247135506

UR - https://www.scopus.com/pages/publications/34247135506#tab=citedBy

U2 - 10.1021/ja068636z

DO - 10.1021/ja068636z

M3 - Article

C2 - 17367138

AN - SCOPUS:34247135506

SN - 0002-7863

VL - 129

SP - 4120

EP - 4121

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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