Modulating the catalytic activity and the substrate specificity of alcohol dehydrogenases using cyclic ethers

2015 ◽  
Vol 5 (8) ◽  
pp. 3922-3925 ◽  
Author(s):  
Norifumi Kawakami ◽  
Yosuke Hara ◽  
Kenji Miyamoto
Keyword(s):  
Catalytic Activity ◽  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Cyclic Ethers ◽  
Alcohol Dehydrogenases

The catalytic activity of Thermoanaerobacter brockii alcohol dehydrogenase (Tbadh) is increased by the addition of 1,3-dioxolane, although it is inhibited by the addition of tetrahydrofuran .

Regulation of NAD-specific alcohol dehydrogenases in Neurospora crassa

1969 ◽  
Vol 15 (3) ◽  
pp. 265-271 ◽  
Author(s):  
M. W. Zink
Keyword(s):  
Carbon Source ◽  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Neurospora Crassa ◽  
Sole Source ◽  
Protein Band ◽  
Alcohol Dehydrogenases

Neurospora crassa is capable of synthesizing two different alcohol dehydrogenases. The synthesis of each depends upon the carbon source on which the mycelium is grown. The fermentative alcohol dehydrogenase, consisting of one electrophoretic protein band, is produced when the mycelium is grown on sucrose. The oxidative alcohol dehydrogenase, consisting of at least two isozymes, is synthesized when Neurospora crassa is grown on ethanol as a sole source of carbon. This latter enzyme is repressed by sugars such as glucose or sucrose. The two enzymes have been differentiated (1) electrophoretically, (2) by their substrate specificity, (3) by the ratio of the forward and reverse reactions, and (4) by their thermostability. Extracts from acetate-grown cells indicate a mixture of the two enzymes.

scholarly journals Quinoprotein alcohol dehydrogenase from ethanol-grown Pseudomonas aeruginosa

1984 ◽  
Vol 223 (3) ◽  
pp. 921-924 ◽  
Author(s):  
B Groen ◽  
J Frank ◽  
J A Duine
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Aromatic Amino Acid ◽  
Pyrroloquinoline Quinone ◽  
The Other ◽  
Enzyme Molecule ◽  
Alcohol Dehydrogenases ◽  
Suicide Substrate

Cell-free extracts of Pseudomonas aeruginosa strains, grown on ethanol, showed dye-linked alcohol dehydrogenase activities. The enzyme responsible for this activity was purified to homogeneity. It appeared to contain two molecules of pyrroloquinoline quinone per enzyme molecule. In many respects, it resembled other quinoprotein alcohol dehydrogenases (EC 1.1.99.8), having a substrate specificity intermediate between that of methanol dehydrogenases and ethanol dehydrogenases in this group. On the other hand, it also showed dissimilarities: the enzyme was found to be a monomer (Mr 101 000), to need only one molecule of the suicide substrate cyclopropanol to become fully inactivated, and to have a different aromatic amino acid composition.

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

scholarly journals An ADH toolbox for raspberry ketone production from natural resources via a biocatalytic cascade

2021 ◽  
Author(s):  
Aileen Becker ◽  
Dominique Böttcher ◽  
Werner Katzer ◽  
Karsten Siems ◽  
Lutz Müller-Kuhrt ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Genetically Modified Organisms ◽  
Optical Purity ◽  
High Yield ◽  
Alcohol Dehydrogenases ◽  
Flavor Compound ◽  
Raspberry Ketone ◽  
Cofactor Recycling ◽  
Cosmetic Industry ◽  
Key Points

Abstract Raspberry ketone is a widely used flavor compound in food and cosmetic industry. Several processes for its biocatalytic production have already been described, but either with the use of genetically modified organisms (GMOs) or incomplete conversion of the variety of precursors that are available in nature. Such natural precursors are rhododendrol glycosides with different proportions of (R)- and (S)-rhododendrol depending on the origin. After hydrolysis of these rhododendrol glycosides, the formed rhododendrol enantiomers have to be oxidized to obtain the final product raspberry ketone. To be able to achieve a high conversion with different starting material, we assembled an alcohol dehydrogenase toolbox that can be accessed depending on the optical purity of the intermediate rhododendrol. This is demonstrated by converting racemic rhododendrol using a combination of (R)- and (S)-selective alcohol dehydrogenases together with a universal cofactor recycling system. Furthermore, we conducted a biocatalytic cascade reaction starting from naturally derived rhododendrol glycosides by the use of a glucosidase and an alcohol dehydrogenase to produce raspberry ketone in high yield. Key points • LB-ADH, LK-ADH and LS-ADH oxidize (R)-rhododendrol • RR-ADH and ADH1E oxidize (S)-rhododendrol • Raspberry ketone production via glucosidase and alcohol dehydrogenases from a toolbox Graphical abstract

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

scholarly journals Deacetoxycephalosporin C synthase isozymes exhibit diverse catalytic activity and substrate specificity

2003 ◽  
Vol 218 (2) ◽  
pp. 251-257 ◽  
Author(s):  
Hong Soon Chin ◽  
Janet Sim ◽  
Keng Ing Seah ◽  
Tiow Suan Sim
Keyword(s):  
Catalytic Activity ◽  
Substrate Specificity

scholarly journals A new dopachrome-rearranging enzyme from the ejected ink of the cuttlefish Sepia officinalis.

1994 ◽  
Vol 299 (3) ◽  
pp. 839-844 ◽  
Author(s):  
A Palumbo ◽  
M d'Ischia ◽  
G Misuraca ◽  
L De Martino ◽  
G Prota
Keyword(s):  
Catalytic Activity ◽  
Methyl Ester ◽  
Substrate Specificity ◽  
Molecular Mass ◽  
Significant Inhibition ◽  
Single Band ◽  
Pigment Cells ◽  
Sepia Officinalis ◽  
High Substrate ◽  
Sds Page

A melanogenic enzyme catalysing the rearrangement of dopachrome has been identified in the ejected ink of the cuttlefish Sepia officinalis. This enzyme occurs as a heat-labile protein which co-migrates with tyrosinase under a variety of chromatographic and electrophoretic conditions. On SDS/PAGE it shows like a single band with an approx. molecular mass of 85 kDa. The enzyme possesses high substrate specificity, acting on L-dopachrome (Km = 1 mM at pH 6.8) and on L-alpha-methyl-dopachrome, but not on D-dopachrome, L-dopachrome methyl ester, dopaminochrome and adrenochrome. Significant inhibition of the catalytic activity was observed with tropolone and L-mimosine. H.p.1.c. analysis of the enzyme-catalysed rearrangement of L-dopachrome revealed the quantitative formation of the decarboxylated product, 5,6-dihydroxyindole. These results point to marked differences between melanogenesis in cephalopod pigment cells and in melanocytes, which may have important implications in relation to the use of sepiomelanin as a model for studies of mammalian melanins.

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