The aromatic alcohol dehydrogenases in Pseudomonas putida N.C.I.B. 9869 grown on 3,5-xylenol and p-cresol.
Whole cells of Pseudomonas putida N.C.I.B 9869, when grown on either 3,5-xylenol or p-cresol, oxidized both m- and p-hydroxybenzyl alcohols. Two distinct NAD+-dependent m-hydroxybenzyl alcohol dehydrogenases were purified from cells grown on 3,5-xylenol. Each is active with a range of aromatic alcohols, including both m- and p-hydroxybenzyl alcohol, but differ in their relative rates with the various substrates. An NAD+-dependent alcohol dehydrogenase was also partially purified from p-cresol grown cells. This too was active with m- and p-hydroxybenzyl alcohol and other aromatic alcohols, but was not identical with either of the other two dehydrogenases. All three enzymes were unstable, but were stabilized by dithiothreitol and all were inhibited with p-chloromercuribenzoate. All were specific for NAD+ and each was shown to catalyse conversion of alcohol into aldehyde.
D000429:Alcohol Oxidoreductases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D001592:Benzyl Alcohols / Q000378:metabolism; D002729:Chloromercuribenzoates / Q000494:pharmacology; D003408:Cresols / Q000378:metabolism*; D007700:Kinetics; D010084:Oxidation-Reduction; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity; D014992:Xylenes / Q000378:metabolism*
D001592:Benzyl Alcohols; D002729:Chloromercuribenzoates; D003408:Cresols; D014992:Xylenes; D000429:Alcohol Oxidoreductases; C016834:3,5-xylenol