Enzyme Catalytic Promiscuity: The Nonheme Fe 2+  Center of β‐Diketone‐Cleaving Dioxygenase Dke1 Promotes Hydrolysis of Activated Esters | Zendy

Leitgeb Stefan | Zendy; Nidetzky Bernd | Zendy

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Enzyme Catalytic Promiscuity: The Nonheme Fe 2+ Center of β‐Diketone‐Cleaving Dioxygenase Dke1 Promotes Hydrolysis of Activated Esters

Author(s) -

Leitgeb Stefan,

Nidetzky Bernd

Publication year - 2010

Publication title -

chembiochem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.05

H-Index - 126

eISSN - 1439-7633

pISSN - 1439-4227

DOI - 10.1002/cbic.200900688

Subject(s) - hydrolysis , chemistry , catalysis , dioxygenase , enzyme , stereochemistry , enzyme kinetics , diketone , cofactor , organic chemistry , active site

Trying new partners: The nonheme Fe 2+ center of β‐diketone‐cleaving dioxygenase in native (His62, His64, His104) and mutated (His62, His64, Glu104) form catalyzed hydrolysis of 4‐nitrophenyl esters of short‐chain (C 2 –C 4 ) alkanoic acids with turnover numbers ( k cat ) in the range 0.01–0.03 s −1 . Zn 2+ was not competent in the dioxygenase reaction, but replaced Fe 2+ as essential metal cofactor for ester hydrolysis.

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