BIOMAT Database Logo BIOMAT Database Logo

Purification and characterization of two NAD-dependent alcohol dehydrogenases (ADHs) induced in the quinoprotein ADH-deficient mutant of Acetobacter pasteurianus SKU1108. 2003

Piyawan Chinnawirotpisan, and Kazunobu Matsushita, and Hirohide Toyama, and Osao Adachi, and Savitree Limtong, and Gunjana Theeragool
Department of Microbiology, Faculty of Science, Kasetsart University, Bangkok 10900, Thailand.

High NAD-dependent alcohol dehydrogenase (ADH) activity was found in the cytoplasm when a membrane-bound, quinoprotein, ADH-deficient mutant strain of Acetobacter pasteurianus SKU1108 was grown on ethanol. Two NAD-dependent ADHs were separated and purified from the supernatant fraction of the cells. One (ADH I) is a trimer, consisting of an identical subunit of 42 kDa, while the other (ADH II) is a homodimer, having a subunit of 31 kDa. One of the two ADHs, ADH II, easily lost the activity during the column chromatographies, which could be stabilized by the addition of DTT and MgCl2 in the column buffer. ADH I but not ADH II contained approximately one zinc atom per subunit. The N-terminal amino acid analysis indicated that ADH I and ADH II have homology to the long-chain and short-chain ADH families, respectively. ADH I showed a preference for primary alcohols, while ADH II had a preference for secondary alcohols. The two ADHs showed clear difference in their kinetics on ethanol, acetaldehyde, NAD, and NADH. The physiological function of both ADH I and ADH II are also discussed.

UI MeSH Term Description Entries
D007527 Isoenzymes Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics. Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008670 Metals Electropositive chemical elements characterized by ductility, malleability, luster, and conductance of heat and electricity. They can replace the hydrogen of an acid and form bases with hydroxyl radicals. (Grant & Hackh's Chemical Dictionary, 5th ed) Metal
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D009243 NAD A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed) Coenzyme I,DPN,Diphosphopyridine Nucleotide,Nadide,Nicotinamide-Adenine Dinucleotide,Dihydronicotinamide Adenine Dinucleotide,NADH,Adenine Dinucleotide, Dihydronicotinamide,Dinucleotide, Dihydronicotinamide Adenine,Dinucleotide, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide,Nucleotide, Diphosphopyridine
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D000091 Acetobacter A species of gram-negative bacteria of the family ACETOBACTERACEAE found in FLOWERS and FRUIT. Cells are ellipsoidal to rod-shaped and straight or slightly curved.
D000426 Alcohol Dehydrogenase A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen. Alcohol Dehydrogenase (NAD+),Alcohol Dehydrogenase I,Alcohol Dehydrogenase II,Alcohol-NAD+ Oxidoreductase,Yeast Alcohol Dehydrogenase,Alcohol Dehydrogenase, Yeast,Alcohol NAD+ Oxidoreductase,Dehydrogenase, Alcohol,Dehydrogenase, Yeast Alcohol,Oxidoreductase, Alcohol-NAD+

Related Publications

Piyawan Chinnawirotpisan, and Kazunobu Matsushita, and Hirohide Toyama, and Osao Adachi, and Savitree Limtong, and Gunjana Theeragool
Molecular cloning and characterization of two inducible NAD⁺-adh genes encoding NAD⁺-dependent alcohol dehydrogenases from Acetobacter pasteurianus SKU1108.
November 2011, Journal of bioscience and bioengineering,
Piyawan Chinnawirotpisan, and Kazunobu Matsushita, and Hirohide Toyama, and Osao Adachi, and Savitree Limtong, and Gunjana Theeragool
Cloning and functional analysis of adhS gene encoding quinoprotein alcohol dehydrogenase subunit III from Acetobacter pasteurianus SKU1108.
March 2010, International journal of food microbiology,
Piyawan Chinnawirotpisan, and Kazunobu Matsushita, and Hirohide Toyama, and Osao Adachi, and Savitree Limtong, and Gunjana Theeragool
Characterization of thermotolerant Acetobacter pasteurianus strains and their quinoprotein alcohol dehydrogenases.
January 2010, Applied microbiology and biotechnology,
Piyawan Chinnawirotpisan, and Kazunobu Matsushita, and Hirohide Toyama, and Osao Adachi, and Savitree Limtong, and Gunjana Theeragool
Crystallization and preliminary diffraction studies of two quinoprotein alcohol dehydrogenases (ADHs): a soluble monomeric ADH from Pseudomonas putida HK5 (ADH-IIB) and a heterotrimeric membrane-bound ADH from Gluconobacter suboxydans (ADH-GS).
November 1999, Acta crystallographica. Section D, Biological crystallography,
Piyawan Chinnawirotpisan, and Kazunobu Matsushita, and Hirohide Toyama, and Osao Adachi, and Savitree Limtong, and Gunjana Theeragool
Alcohol dehydrogenase (ADH) in yeasts. II. NAD+-and NADP+-dependent alcohol dehydrogenases in Saccharomycopsis lipolytica.
January 1979, Zeitschrift fur allgemeine Mikrobiologie,
Piyawan Chinnawirotpisan, and Kazunobu Matsushita, and Hirohide Toyama, and Osao Adachi, and Savitree Limtong, and Gunjana Theeragool
Characterization of rpoH in Acetobacter pasteurianus NBRC3283.
April 2011, Journal of bioscience and bioengineering,
Piyawan Chinnawirotpisan, and Kazunobu Matsushita, and Hirohide Toyama, and Osao Adachi, and Savitree Limtong, and Gunjana Theeragool
[Demonstration of several alcohol dehydrogenases bound to NAD and NADP respectively in Acetobacter mesoxydans].
January 1972, Comptes rendus hebdomadaires des seances de l'Academie des sciences. Serie D: Sciences naturelles,
Piyawan Chinnawirotpisan, and Kazunobu Matsushita, and Hirohide Toyama, and Osao Adachi, and Savitree Limtong, and Gunjana Theeragool
Role of a membrane-bound aldehyde dehydrogenase complex AldFGH in acetic acid fermentation with Acetobacter pasteurianus SKU1108.
May 2018, Applied microbiology and biotechnology,
Piyawan Chinnawirotpisan, and Kazunobu Matsushita, and Hirohide Toyama, and Osao Adachi, and Savitree Limtong, and Gunjana Theeragool
Purification and characterization of the NAD-preferring glucose 6-phosphate dehydrogenase from Acetobacter hansenii (Acetobacter xylinum).
May 1994, Archives of biochemistry and biophysics,
Piyawan Chinnawirotpisan, and Kazunobu Matsushita, and Hirohide Toyama, and Osao Adachi, and Savitree Limtong, and Gunjana Theeragool
Induction by ethanol of alcohol dehydrogenase activity in Acetobacter pasteurianus.
November 1993, Journal of bacteriology,
Copied contents to your clipboard!