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Structure Determination and Characterization of the Vitamin B6 Degradative Enzyme (E)-2-(Acetamidomethylene)succinate Hydrolase,

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§ Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853
Department of Chemistry, Texas A&M University, College Station, Texas 77842
*To whom correspondence should be addressed. Telephone: (607) 255-7961. Fax: (607) 255-1227. E-mail: [email protected]; [email protected]
Cite this: Biochemistry 2010, 49, 6, 1226–1235
Publication Date (Web):January 25, 2010
https://doi.org/10.1021/bi901812p
Copyright © 2010 American Chemical Society

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    Abstract

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    The gene identification and kinetic characterization of (E)-2-(acetamidomethylene)succinate (E-2AMS) hydrolase has recently been described. This enzyme catalyzes the final reaction in the degradation of vitamin B6 and produces succinic semialdehyde, acetate, ammonia, and carbon dioxide from E-2AMS. The structure of E-2AMS hydrolase was determined to 2.3 Å using SAD phasing. E-2AMS hydrolase is a member of the α/β hydrolase superfamily and utilizes a serine/histidine/aspartic acid catalytic triad. Mutation of either the nucleophilic serine or the aspartate resulted in inactive enzyme. Mutation of an additional serine residue in the active site causes the enzyme to be unstable and is likely structurally important. The structure also provides insight into the mechanism of hydrolysis of E-2AMS and identifies several potential catalytically important residues.

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