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Expression and Characterization of Phenacetaldehyde Dehydrogenase from the Styrene Catabolic Pathway
Author(s) -
NaseriJabari Maryam,
Emami Shahram,
Gassner George
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a45-a
Subject(s) - catabolism , enzyme , biochemistry , aldehyde dehydrogenase , chemistry , dehydrogenase , phenylacetaldehyde , histidine , carbon monoxide dehydrogenase , phenylacetic acid , stereochemistry , carbon monoxide , catalysis
The enzymatic interconversion of aldehydes and acids is central to an array of biosynthetic, catabolic, detoxifying, and light‐generating reactions in biochemistry. In bacterial catabolism, phenacetaldehyde dehydrogenases are integral components of the phenethylamine and styrene degradation pathways where they catalyzes the oxidation of phenacetaldehyde to phenylacetic acid. We have cloned the phenacetaldehyde dehydrogenase associated with the styrene catabolic pathway from genomic DNA isolated from Pseudomons putida (S12) and expressed, purified, and characterized it as an N‐terminally histidine‐tagged enzyme. Three‐ dimensional structure homology modeling suggests that this enzyme is closely related to the known structures of human, cod, sheep, and rat aldehyde dehydrogenases. The substrate specificity, pH, and metal ion dependence of the kinetic mechanism of this enzyme will be reported. (This work was supported by NIH GM052588)