scholarly journals A new dye-linked alcohol dehydrogenase (vanillyl alcohol dehydrogenase) from Rhodopseudomonas acidophila M402 purification, identification of reaction product and substrate specificity.

1983 ◽  
Vol 47 (10) ◽  
pp. 2173-2183 ◽  
Author(s):  
Kei YAMANAKA ◽  
Yasutaka TSUYUKI
Keyword(s):  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Vanillyl Alcohol ◽  
Rhodopseudomonas Acidophila

Investigation of Structural Determinants for the Substrate Specificity in the Zinc-Dependent Alcohol Dehydrogenase CPCR2 fromCandida parapsilosis

ChemBioChem ◽  
2015 ◽  
Vol 16 (10) ◽  
pp. 1512-1519 ◽  
Author(s):  
Christoph Loderer ◽  
Gaurao V. Dhoke ◽  
Mehdi D. Davari ◽  
Wolfgang Kroutil ◽  
Ulrich Schwaneberg ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Structural Determinants

Structural insights into substrate specificity and solvent tolerance in alcohol dehydrogenase ADH-‘A’ from Rhodococcus ruber DSM 44541

2010 ◽  
Vol 46 (34) ◽  
pp. 6314 ◽  
Author(s):  
Martin Karabec ◽  
Andrzej Łyskowski ◽  
Katharina C. Tauber ◽  
Georg Steinkellner ◽  
Wolfgang Kroutil ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Solvent Tolerance ◽  
Rhodococcus Ruber ◽  
Structural Insights

Substrate specificity of alcohol dehydrogenase from the yeastHansenyls polymorpha CBS 4732 andCandida utilis CBS 621

Yeast ◽  
1988 ◽  
Vol 4 (2) ◽  
pp. 143-148 ◽  
Author(s):  
Cornelis Verduyn ◽  
Guido J. Breedveld ◽  
W. Alexander Scheffers ◽  
Johnnes P. Van Dijken
Keyword(s):  
Alcohol Dehydrogenase ◽  
Substrate Specificity

Role of Tryptophan 95 in substrate specificity and structural stability of Sulfolobus solfataricus alcohol dehydrogenase

Extremophiles ◽  
2009 ◽  
Vol 13 (5) ◽  
pp. 751-761 ◽  
Author(s):  
Angela Pennacchio ◽  
Luciana Esposito ◽  
Adriana Zagari ◽  
Mosè Rossi ◽  
Carlo A. Raia
Keyword(s):  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Structural Stability ◽  
Sulfolobus Solfataricus

scholarly journals Structural aspects of the dye-linked alcohol dehydrogenase of Rhodopseudomonas acidophila

1979 ◽  
Vol 181 (3) ◽  
pp. 517-524 ◽  
Author(s):  
C W Bamforth ◽  
J R Quayle
Keyword(s):  
Alcohol Dehydrogenase ◽  
Paracoccus Denitrificans ◽  
Colorimetric Assay ◽  
Protein Band ◽  
Atomic Absorption Spectrophotometry ◽  
Biochemical Properties ◽  
Visible Absorption ◽  
Rhodopseudomonas Acidophila ◽  
Alcohol Dehydrogenase Activity ◽  
Alcohol Dehydrogenation

1. A dye-linked alcohol dehydrogenase was purified 60-fold from extracts of Rhodopseudomonas acidophila 10050 grown aerobically on ethanol. 2. The properties of this enzyme were identical with those of the alcohol dehydrogenase synthesized by this organism during growth on methanol anaerobically in the light, and they are judged to be the same enzyme. 3. The enzyme gave a single protein band, coincident with alcohol dehydrogenase activity, during electrophoresis on polyacrylamide gel. 4. The amino acid composition, ioselectric point, u.v. and visible absorption spectra of the enzyme were determined and compared with those of other similar enzymes. 5. The presence of 0.7–1.0 g-atom of non-haem, acidlabile iron/mol of enzyme was shown by atomic absorption spectrophotometry and colorimetric assay. The iron could not be dissociated from the enzyme by dialysis against chelating agents. 6. E.p.r. spectroscopy of the enzyme did not indicate any redox function for the iron during alcohol dehydrogenation, but showed a signal at g = 2.00 consistent with the presence of a protein-bound organic free radical. 8. Antisera were raised against alcohol (methanol) dehydrogenases purified from Rhodopseudomonas acidophila, Paracoccus denitrificans and Methylophilus methylotrophus. 9. The antiserum to the Rhodopseudomonas acidophila enzyme cross-reacted with neither of the two other antisera, nor with crude extracts of methanol-grown Hyphomicrobium X and Pseudomonas AM1, thus emphasizing its singular biochemical properties.

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