An examination of the oxidation of aldehydes by horse liver alcohol dehydrogenase.

نویسندگان

  • J A Hinson
  • R A Neal
چکیده

A lag phase in the spectrophotometric assay progress curve of aldehyde oxidation by HL-ADH was observed and characterised. The aldehyde oxidation and aldehyde dismutation reactions were shown to be related, and a mechanism to explain net aldehyde oxidation was proposed. The spectrophotometric assay was shown to be unsuitable for measurement of kinetic parameters for aldehyde oxidation by HL-ADH, and kinetic constants previously determined were shown to be in error. Existing data on the aldehyde dismutation reaction are insufficient to discount a role for HL-ADH in aldehyde transformation in vivo.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Highly efficient asymmetric reduction of arylpropionic aldehydes by horse liver alcohol dehydrogenase through dynamic kinetic resolution.

The enantioselective synthesis of (2S)-2-phenylpropanol and (2S)-2-(4-iso-butylphenyl)propanol ((S)-Ibuprofenol) has been achieved by means of Horse Liver Alcohol Dehydrogenase (HLADH) in buffered aqueous solution or buffered organic solvent mixtures; under the reaction conditions, a dynamic kinetic resolution (DKR) process was realized with good reaction yields and enantiomeric ratios.

متن کامل

Reversible Oxidation of Cyclic Secondary Alcohols by Liver Alcohol Dehydrogenase

During a study of cyclic alcohol oxidation by a partially purified rat liver enzyme system (l), it was noted that ethanol was also oxidized by this preparation. Since the ratio of the rate of ethanol oxidation to the rate of cyclohexanol oxidation remained constant during purification, the possibility arose that the activity with cyclic substrates was due to the conventional alcohol dehydrogena...

متن کامل

Chemoenzymatic synthesis of (2S)-2-arylpropanols through a dynamic kinetic resolution of 2-arylpropanals with alcohol dehydrogenases.

We applied Horse Liver Alcohol Dehydrogenase (HLADH) to the enantioselective synthesis of six (2S)-2-arylpropanols, useful intermediates in the synthesis of Profens. The influence of substrate structure and reaction conditions on yields and enantioselectivity were investigated. The high yields and high enantioselectivity towards the (S)-enantiomer obtained in the bioreduction of 2-arylpropionic...

متن کامل

A comparison of retinene reductase and alcohol dehydrogenase of rat liver.

Retinene reductase, an enzyme which catalyzes the diphosphopyridine nucleotide-dependent reduction of vitamin A aldehyde (retinene) to vitamin A alcohol, was first demonstrated with homogenates of frog and cattle retinas (1, 2). Because crude rabbit liver extracts (3) and crystalline horse liver alcohol dehydrogenase (4) catalyze the oxidation of vitamin A into retinene, the general involvement...

متن کامل

Stereospecific oxidation of secondary alcohols by human alcohol dehydrogenases.

The human liver alpha alpha alcohol dehydrogenase exhibits a different substrate specificity and stereospecificity for secondary alcohols than the human beta 1 beta 1, and gamma 1 gamma 1 or horse liver alcohol dehydrogenases. All of the enzymes efficiently oxidize primary alcohols, but alpha alpha oxidizes secondary alcohols far more efficiently than human beta 1 beta 1 and gamma 1 gamma 1 or ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Advances in experimental medicine and biology

دوره 328  شماره 

صفحات  -

تاریخ انتشار 1972