Oxidation of aromatic aldehydes and aliphatic secondary alcohols by Hyphomicrobium spp.

1982 ◽  
Vol 28 (1) ◽  
pp. 65-72 ◽  
Author(s):  
Jürgen Köhler ◽  
Arnold C. Schwartz
Keyword(s):  
Oxygen Consumption ◽  
Aldehyde Dehydrogenase ◽  
Secondary Alcohol ◽  
Aromatic Aldehydes ◽  
Polyacrylamide Gel ◽  
Secondary Alcohols ◽  
Multiple Forms ◽  
Aldehyde Dehydrogenases ◽  
Enzyme Substrate ◽  
Secondary Alcohol Dehydrogenase

Two of six tested strains of Hyphomicrobium respired on benzaldehyde with higher rates than on formaldehyde, and three strains with equal or lower rates, whereas one strain, Hyphomicrobium X, showed almost negligible respiration on benzaldehyde. Various substituted benzaldehydes stimulated oxygen consumption to lower rates than benzaldehyde itself in active strains. All strains contained multiple forms of dye-linked aldehyde dehydrogenase, as evident from polyacrylamide gel electropherograms of cell-free extracts and activity tests on the gels with nitroblue tetrazolium. All bands of this enzyme reacted more strongly with benzaldehyde than with formaldehyde in all strains. On gels of some strains additional bands appeared with benzaldehyde as the enzyme substrate. Hyphomicrobium X again displayed the lowest activity of this enzyme on the gels. A new band of this enzyme appeared on gels of strain ZV 580 after growth on methylamine, when tested in this respect. NAD-dependent secondary alcohol dehydrogenase was present on gels of three strains, which respired on 2-propanol.Difference spectra and observation of the degree of reduction of ubiquinone and cytochromes b and c of two strains indicated that the electrons from benzaldehyde oxidation were transferred to cytochrome c.The results are discussed with regard to the significance of dye-linked aldehyde dehydrogenases with broad substrate specificity for the catabolism and oligocarbophilic growth of Hyphomicrobium and the taxonomic relevance of the aldehyde dehydrogenase pattern observed on polyacrylamide gel electropherograms.

Racemization of enantiopure secondary alcohols by Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase

2013 ◽  
Vol 11 (17) ◽  
pp. 2911 ◽  
Author(s):  
Musa M. Musa ◽  
Robert S. Phillips ◽  
Maris Laivenieks ◽  
Claire Vieille ◽  
Masateru Takahashi ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Secondary Alcohol ◽  
Secondary Alcohols ◽  
Thermoanaerobacter Ethanolicus ◽  
Secondary Alcohol Dehydrogenase

Studies of NADP+-preferred secondary alcohol dehydrogenase from Thermoanaerobium brockii

1990 ◽  
Vol 68 (6) ◽  
pp. 907-913 ◽  
Author(s):  
Loola S. Al-Kassim ◽  
C. Stan Tsai
Keyword(s):  
Alcohol Dehydrogenase ◽  
Turnover Rate ◽  
Dissociation Constants ◽  
Secondary Alcohol ◽  
Kinetic Studies ◽  
Enzymic Activity ◽  
Secondary Alcohols ◽  
High Turnover ◽  
Subunit Molecular Weight ◽  
Secondary Alcohol Dehydrogenase

Alcohol dehydrogenase has been purified from the cell-free preparation of Thermoanaerobium brockii to homogeneity, employing combined DEAE, Sephadex, and affinity chromatographic procedures. The enzyme is tetrameric having subunit molecular weight of 40.4 × 103. The purified alcohol dehydrogenase is capable of utilizing either NAD+ or NADP+ to oxidize primary and secondary alcohols, although it prefers NADP+ as the coenzyme and secondary alcohols as substrates. Inactivation of the enzymic activity by sensitized photooxidation and carboxymethylation implicates the presence of catalytically important histidine and cysteine residues. Kinetic studies indicate that Thermoanaerobium alcohol dehydrogenase catalyzes NADP+-linked oxidations of secondary alcohols by an ordered bi-bi mechanism with NADP+ as the leading reactant. The preference of the Thermoanaerobium enzyme for NADP+ is correlated with its low dissociation constants (KA and KiA) and high turnover rate (V/Et). The corresponding kinetic parameters also contribute to the preference of this enzyme for secondary alcohols.Key words: NADP+-preferred secondary alcohol dehydrogenase.

scholarly journals Aldehyde dehydrogenase in 2-acetaminofluorene-induced rat hepatomas. Ontogeny and evidence that the new isoenzymes are not due to normal gene de-repression

1977 ◽  
Vol 164 (1) ◽  
pp. 119-123 ◽  
Author(s):  
Ronald Lindahl
Keyword(s):  
Rat Liver ◽  
Aldehyde Dehydrogenase ◽  
Double Diffusion ◽  
Normal Liver ◽  
Normal Adult ◽  
Sprague Dawley ◽  
Adult Liver ◽  
Aldehyde Dehydrogenases ◽  
Adult Rat ◽  
Liver Aldehyde Dehydrogenase

The pre- and post-natal ontogeny of Sprague–Dawley rat liver aldehyde dehydrogenase [aldehyde–NAD(P)+ oxidoreductase, EC 1.2.1.5] is described. At no time in its ontogenetic development does normal liver aldehyde dehydrogenase exhibit any of the characteristics of a series of unique aldehyde dehydrogenases that can be isolated from 2-acetamidofluorene-induced rat hepatomas. Enzyme activity is first detectable in 15-day foetal liver and gradually increases throughout pre- and post-natal development until adult activities are attained by day 49 after birth. Electrophoretically, normal aldehyde dehydrogenase, throughout its ontogeny, exists as the same single isoenzyme found in normal adult liver. Isoelectric points for two normal liver isoenzymes demonstrable by isoelectric focusing are pH5.9 and 6.0. The immunochemical properties of aldehyde dehydrogenase during its ontogeny are identical with those of normal adult liver aldehyde dehydrogenase when tested against anti-(hepatoma aldehyde dehydrogenase) serum in Ouchterlony double-diffusion tests. The results indicate that the hepatoma-specific aldehyde dehydrogenases are not the result of the de-repression of genes normally repressed in adult rat liver or in some other adult tissue.

scholarly journals OXIDATION OF BENZYLIC SECONDARY ALCOHOL WITH PYRIDINIUM CHLOROCHROMATE-ALUMINA (PCC-Al2O3)

2010 ◽  
Vol 8 (1) ◽  
pp. 91-93
Author(s):  
Hanoch J. Sohilait
Keyword(s):  
1H Nmr ◽  
Secondary Alcohol ◽  
Pyridinium Chlorochromate ◽  
Secondary Alcohols

In these studies, Pyridinium chlorochromate-Alumina was used for oxidation of secondary alcohols (safryl alcohol and methyleugenyl alcohol) to ketone.  The oxidation of safryl alcohol with PCC-Al2O3 followed by purification by potassium bisulfite yields safryl ketone (62,92%). The oxidation of methyleugenyl alcohol with PCC-Al2O3, followed by purification by potassium bisulfite  yields methyleugenyl ketone (68,04%). The elucidation of these products was analyzed by FTIR, 1H-NMR and MS.   Keywords : PCC-alumina, secondary alcohols, ketone

scholarly journals SYNTHESIS OF SECONDARY ALCOHOL COMPOUNDS FROM SAFROLE AND METHYLEUGENOL

2010 ◽  
Vol 3 (3) ◽  
pp. 176-178
Author(s):  
Hanoch J Sohilait ◽  
Hardjono Sastrohamidjojo ◽  
Sabirin Matsjeh
Keyword(s):  
1H Nmr ◽  
Sodium Borohydride ◽  
13C Nmr ◽  
Structure Elucidation ◽  
Mercuric Acetate ◽  
Secondary Alcohol ◽  
Secondary Alcohols ◽  
In Situ Reduction

Synthesis of secondary alcohols compound from safrole and methyleugenol has been achieved through conversion of allyl group to alcohol.The reaction of safrole and methyleugenol with mercuric acetate in aqueous tetrahydrofuran, followed by in situ reduction of the mercurial intermediate by alkaline sodium borohydride produced secondary alcohol namely safryl alcohol (71.25%) and methyleugenil alcohol (65.56%). The structure elucidation of these products were analyzed by FTIR, 1H-NMR, 13C-NMR and MS.   Keywords: Secondary alcohols; safrole; methyleugenol

scholarly journals Engineered Synthetic Pathway for Isopropanol Production in Escherichia coli

2007 ◽  
Vol 73 (24) ◽  
pp. 7814-7818 ◽  
Author(s):  
T. Hanai ◽  
S. Atsumi ◽  
J. C. Liao
Keyword(s):  
Escherichia Coli ◽  
Secondary Alcohol ◽  
Clostridium Beijerinckii ◽  
Synthetic Pathway ◽  
E Coli ◽  
Coa Transferase ◽  
Secondary Alcohol Dehydrogenase ◽  
Acetoacetate Decarboxylase ◽  
Shake Flasks ◽  
K 12

ABSTRACT A synthetic pathway was engineered in Escherichia coli to produce isopropanol by expressing various combinations of genes from Clostridium acetobutylicum ATCC 824, E. coli K-12 MG1655, Clostridium beijerinckii NRRL B593, and Thermoanaerobacter brockii HTD4. The strain with the combination of C. acetobutylicum thl (acetyl-coenzyme A [CoA] acetyltransferase), E. coli atoAD (acetoacetyl-CoA transferase), C. acetobutylicum adc (acetoacetate decarboxylase), and C. beijerinckii adh (secondary alcohol dehydrogenase) achieved the highest titer. This strain produced 81.6 mM isopropanol in shake flasks with a yield of 43.5% (mol/mol) in the production phase. To our knowledge, this work is the first to produce isopropanol in E. coli, and the titer exceeded that from the native producers.

Kinetic measurement of guanine deaminase in serum with a centrifugal analyzer.

1981 ◽  
Vol 27 (4) ◽  
pp. 560-561 ◽  
Author(s):  
Y Nishikawa ◽  
K Fukumoto
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Kinetic Method ◽  
Reference Interval ◽  
Healthy Humans ◽  
Automated Method ◽  
Enzyme Substrate ◽  
Guanine Deaminase ◽  
One Step ◽  
Lag Period ◽  
Method R

Abstract We describe an enzymic, one-step kinetic method for determination of guanine deaminase (guanase, EC 3.5.4.3) in serum with a centrifugal analyzer. A combined enzyme-substrate system consists of the enzymes xanthine oxidase, catalase, and aldehyde dehydrogenase, the coenzyme NAD+, the substrate guanine, and ethanol in tris(hydroxymethyl)methylamine buffer, with KCl added as activator for aldehyde dehydrogenase. The method requires only 40 microL of sample. Guanase activity in 28 samples can be determined within 10 min by setting a 4-min lag period. The increase in absorbance at 340 nm is linearly proportional to the activity of guanase to 60 U/L. Within-run precision (CV) was 1.32 to 4.50% over the range studied. Day-to-day precision corresponds to CVs of 4.8 to 7.2% over the same range of guanase activity. The reference interval, as calculated from data on 25 healthy humans, was 0 to 1.02 U/L. The enzymic automated method shows good correlation with Caraway's (Clin. Chem. 12: 187, 1966) method (r = 0.949).

Cofactor specificity engineering of a long-chain secondary alcohol dehydrogenase from Micrococcus luteus for redox-neutral biotransformation of fatty acids

2019 ◽  
Vol 55 (96) ◽  
pp. 14462-14465 ◽  
Author(s):  
Eun-Ji Seo ◽  
Hye-Ji Kim ◽  
Myeong-Ju Kim ◽  
Jeong-Sun Kim ◽  
Jin-Byung Park
Keyword(s):  
Fatty Acids ◽  
Alcohol Dehydrogenase ◽  
Micrococcus Luteus ◽  
Secondary Alcohol ◽  
Cofactor Specificity ◽  
Secondary Alcohol Dehydrogenase ◽  
Long Chain

Structure-based cofactor specificity engineering of an alcohol dehydrogenase (mLSADH) enables a redox-neutral biotransformation of C18 fatty acids into C9 fatty acids.

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