NAD-dependent aromatic alcohol dehydrogenase in wheats (Triticum L.) and goatgrasses (Aegilops L.): evolutionary genetics

1984 ◽  
Vol 67 (6) ◽  
pp. 535-540 ◽  
Author(s):  
Vello Jaaska
Keyword(s):  
Alcohol Dehydrogenase ◽  
Evolutionary Genetics ◽  
Aromatic Alcohol ◽  
Aromatic Alcohol Dehydrogenase

Inheritance and phenotype expression of functional and null alleles of aromatic alcohol dehydrogenase (CAD) in diploid wheats

2014 ◽  
Vol 50 (11) ◽  
pp. 1161-1168 ◽  
Author(s):  
A. A. Konovalov ◽  
I. K. Shundrina ◽  
E. V. Karpova ◽  
A. A. Nefedov ◽  
N. P. Goncharov
Keyword(s):  
Alcohol Dehydrogenase ◽  
Null Alleles ◽  
Aromatic Alcohol ◽  
Aromatic Alcohol Dehydrogenase ◽  
Phenotype Expression

Aromatic alcohol dehydrogenase from potato tubers

1973 ◽  
Vol 12 (3) ◽  
pp. 531-536 ◽  
Author(s):  
D.D. Davies ◽  
E.N. Ugochukwu ◽  
K.D. Patil ◽  
G.H.N. Towers
Keyword(s):  
Alcohol Dehydrogenase ◽  
Potato Tubers ◽  
Aromatic Alcohol ◽  
Aromatic Alcohol Dehydrogenase

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.

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