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 Variation in the Direction of Selection Applied by Pentenol to the Alcohol Dehydrogenase Locus in Drosophila melanogaster

1977 ◽  
Vol 30 (3) ◽  
pp. 259 ◽  
Author(s):  
JG Oakeshott
Keyword(s):  
Drosophila Melanogaster ◽  
Alcohol Dehydrogenase ◽  
Null Allele ◽  
Developmental Time ◽  
The Other ◽  
Laboratory Population ◽  
Alcohol Dehydrogenases ◽  
Alcohol Dehydrogenase Activity ◽  
Active Alcohol ◽  
Selective Effects

This paper describes selective effects of pentenol-impregnated media on six genotypes at the alcohol dehydrogenase (Adh) locus in D. melanogaster. In the laboratory population studied, developmental times of pre-adults homozygous for an alcohol dehydrogenase 'null' allele increased with increasing pentenol concentrations. The developmental times of the other five genotypes, which produced active alcohol dehydrogenases, increased slightly at pentenol concentrations up to 0�0033%, but above this concentration they decreased markedly. In fact on 0�067% pentenol, the highest concentration tested, developmental times of these five genotypes were between 9 and 24 h less than their developmental times on media lacking penteno!. The magnitude of the reduction in developmental time differed significantly between genotypes and was positively correlated with alcohol dehydrogenase activity.

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 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.

Amino Acid Profile and Aromatic Amino Acid Concentration in Total Parenteral Nutrition: Effect on Growth, Protein Metabolism and Aromatic Amino Acid Metabolism in the Neonatal Piglet

1994 ◽  
Vol 87 (1) ◽  
pp. 75-84 ◽  
Author(s):  
Linda J. Wykes ◽  
James D. House ◽  
Ronald O. Ball ◽  
Paul B. Pencharz
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Parenteral Nutrition ◽  
Human Milk ◽  
Total Parenteral Nutrition ◽  
Aromatic Amino Acid ◽  
Nitrogen Retention ◽  
Aromatic Amino Acids ◽  
The Other ◽  
Constant Infusion

1. The protein and amino acid utilization of two commercially available amino acid solutions, one egg-patterned (Vamin), the other human-milk-patterned (Vaminolact), were studied in piglets receiving total parenteral nutrition. It was hypothesized that Vaminolact was deficient in total aromatic amino acids, so a third group received a human-milk-patterned amino acid solution with added phenylalanine. 2. The piglets were on total parenteral nutrition for 8 days from day 2 or 3 of life. They all received a total energy intake of 1040 kJ day−1 kg−1 with macro-nutrient intakes of 14.6g of amino acid, 27.4 g of glucose and 9.4 g of fat day−1 kg−1. 3. Nitrogen balances were performed on days 3-8 of total parenteral nutrition. On day 8 a primed constant infusion of (1-14C]-phenylalanine was given to measure phenylalanine flux and fractional conversion to tyrosine. Transamination catabolites of phenylalanine and tyrosine were measured in urine on day 7. 4. The piglets receiving Vaminolact gained significantly less weight (0.86 kg compared with 1.18 kg for Vamin and 1.20 kg for phenylalanine-supplemented Vaminolact; P < 0.02) and nitrogen (1435 mg day−1 kg−1 compared with 1601 mg and 1836 mg day−1 kg−1 for the other groups; P < 0.0001). 5. The piglets receiving Vamin had high plasma phenylalanine levels (2234 μmol/l compared with 156 μmol/l for Vaminolact and 399 μmol for phenylalanine-supplemented Vaminolact; P < 0.0001). Those receiving Vamin also had an elevated excretion of phenylalanine transamination metabolites and low plasma lysine levels. Phenylalanine flux was highest in the Vamin group, intermediate in the phenylalanine-supplemented Vaminolact group and lowest in the Vaminolact group. 6. We conclude that Vaminolact is limiting in aromatic amino acids and that the addition of phenylalanine to the level in Vamin significantly improves growth and nitrogen retention; however, increasing the phenylalanine content of total parenteral nutrition is not the most metabolically suitable way to provide aromatic amino acids in neonatal total parenteral nutrition.

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 .

scholarly journals Purification and preliminary characterization of alcohol dehydrogenase from Aspergillus nidulans

1985 ◽  
Vol 225 (2) ◽  
pp. 449-454 ◽  
Author(s):  
E H Creaser ◽  
R L Porter ◽  
K A Britt ◽  
J A Pateman ◽  
C H Doy
Keyword(s):  
Amino Acid ◽  
Alcohol Dehydrogenase ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Single Step ◽  
Activity Profile ◽  
Alcohol Dehydrogenases ◽  
Freeze Dried ◽  
Blue Sepharose

Aspergillus alcohol dehydrogenase is produced in response to growth in the presence of a wide variety of inducers, of which the most effective are short-chain alcohols and ketones, e.g. butan-2-one and propan-2-ol. The enzyme can be readily extracted from fresh or freeze-dried cells and purified to homogeneity on Blue Sepharose in a single step by using specific elution with NAD+ and pyrazole. The pure enzyme has Mr 290 000 by electrophoresis or gel filtration; it is a homopolymer with subunit Mr 37 500 by electrophoresis in sodium dodecyl sulphate; its amino acid composition corresponds to Mr 37 900, and the native enzyme contains one zinc atom per subunit. The enzyme is NAD-specific and has a wide substrate activity in the forward and reverse reactions; its activity profile is not identical with those of other alcohol dehydrogenases.

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