scholarly journals Purification and partial characterization of a rat retina alcohol dehydrogenase active with ethanol and retinol

1983 ◽  
Vol 213 (2) ◽  
pp. 547-550 ◽  
Author(s):  
P Julià ◽  
J Farrés ◽  
X Parés
Keyword(s):  
Alcohol Dehydrogenase ◽  
Partial Characterization ◽  
Visual Cycle ◽  
Rat Retina

Homogeneous alcohol dehydrogenase (ADH) from rat retina was obtained by chromatography on DEAE-Sepharose and AMP-hexane-Sepharose. The enzyme is a dimer of Mr congruent to 80000 and oxidizes ethanol using NAD+ as a cofactor. Careful activity determinations demonstrate unambiguously that rat retina ADH is active with retinol as a substrate. This result opens the question about the role of retina ADH in the visual cycle.

Isolation and partial characterization of two alcohol dehydrogenase isozymes from the medfly Ceratitis capitata

1994 ◽  
Vol 24 (1) ◽  
pp. 87-94 ◽  
Author(s):  
G. Gasperi ◽  
D. Kafetzopoulos ◽  
A. Christodoulidou ◽  
V. Bouriotis ◽  
C. Savakis
Keyword(s):  
Alcohol Dehydrogenase ◽  
Ceratitis Capitata ◽  
Partial Characterization

scholarly journals Production and Characterization of a Thermostable Alcohol Dehydrogenase That Belongs to the Aldo-Keto Reductase Superfamily

2006 ◽  
Vol 72 (1) ◽  
pp. 233-238 ◽  
Author(s):  
Ronnie Machielsen ◽  
Agustinus R. Uria ◽  
Servé W. M. Kengen ◽  
John van der Oost
Keyword(s):  
Alcohol Dehydrogenase ◽  
Pyrococcus Furiosus ◽  
Enantiomeric Excess ◽  
Physiological Role ◽  
Secondary Alcohols ◽  
Gene Encoding ◽  
Ph Optimum ◽  
Reduction Of Ketones

ABSTRACT The gene encoding a novel alcohol dehydrogenase that belongs to the aldo-keto reductase superfamily has been identified in the hyperthermophilic archaeon Pyrococcus furiosus. The gene, referred to as adhD, was functionally expressed in Escherichia coli and subsequently purified to homogeneity. The enzyme has a monomeric conformation with a molecular mass of 32 kDa. The catalytic activity of the enzyme increases up to 100°C, and a half-life value of 130 min at this temperature indicates its high thermostability. AdhD exhibits a broad substrate specificity with, in general, a preference for the reduction of ketones (pH optimum, 6.1) and the oxidation of secondary alcohols (pH optimum, 8.8). Maximal specific activities were detected with 2,3-butanediol (108.3 U/mg) and diacetyl-acetoin (22.5 U/mg) in the oxidative and reductive reactions, respectively. Gas chromatrography analysis indicated that AdhD produced mainly (S)-2-pentanol (enantiomeric excess, 89%) when 2-pentanone was used as substrate. The physiological role of AdhD is discussed.

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