trans-o-Hydroxybenzylidenepyruvate hydratase-aldolase as a biocatalyst.
The hydratase-aldolase-catalyzed conversion of trans-o-hydroxybenzylidenepyruvate to salicylaldehyde and pyruvate is an intermediate reaction in the conversion of naphthalene to salicylate by bacteria. Here, a variety of aromatic aldehydes and some nonaromatic aldehydes together with pyruvate have been shown to be substrates for aldol condensations catalyzed by this enzyme in extracts of the recombinant strain Escherichia coli JM109(pRE701). Some of the products of these reactions were also compared as substrates in the opposite (hydration-aldol cleavage) reaction.
Eaton
R W
RW
Gulf Ecology Division, National Health and Environmental Effects Research Laboratory, U.S. Environmental Protection Agency, Gulf Breeze, Florida 32561, USA. eaton.richard@epa.gov
D000447:Aldehydes / Q000737:chemistry / Q000378:metabolism*; D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D008401:Gas Chromatography-Mass Spectrometry; D006836:Hydro-Lyases / Q000235:genetics / Q000378:metabolism*; D009281:Naphthalenes / Q000378:metabolism; D011773:Pyruvates / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D013237:Stereoisomerism
D000447:Aldehydes; D009281:Naphthalenes; D011773:Pyruvates; D011994:Recombinant Proteins; C031721:naphthalene; D006836:Hydro-Lyases; C078380:trans-2-hydroxybenzylidenepyruvate hydratase-aldolase