scholarly journals Multiple induction of dye-linked aromatic alcohol dehydrogenases by n-propanol and n-butanol in Rhodopseudomonas acidophila M402.

1983 ◽  
Vol 47 (9) ◽  
pp. 2107-2108
Author(s):  
Kei YAMANAKA ◽  
Yasutaka TSUYUKI
Keyword(s):  
Alcohol Dehydrogenases ◽  
Aromatic Alcohol ◽  
Rhodopseudomonas Acidophila

scholarly journals The aromatic alcohol dehydrogenases in Pseudomonas putida N.C.I.B. 9869 grown on 3,5-xylenol and p-cresol

1978 ◽  
Vol 175 (2) ◽  
pp. 659-667 ◽  
Author(s):  
M J Keat ◽  
D J Hopper
Keyword(s):  
Alcohol Dehydrogenase ◽  
Pseudomonas Putida ◽  
The Other ◽  
Alcohol Dehydrogenases ◽  
Whole Cells ◽  
Aromatic Alcohol ◽  
Aromatic Alcohols ◽  
Hydroxybenzyl Alcohol

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.

scholarly journals Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.

1987 ◽  
Vol 262 (8) ◽  
pp. 3754-3761
Author(s):  
A.J. Ganzhorn ◽  
D.W. Green ◽  
A.D. Hershey ◽  
R.M. Gould ◽  
B.V. Plapp
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Amino Acid Residue ◽  
Kinetic Characterization ◽  
Alcohol Dehydrogenases
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