Literature DB >> 4730466

On calculation of rate and dissociation constants from kinetic constants for the Ordered Bi Bi mechanism of liver alcohol dehydrogenase.

B V Plapp.   

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Year:  1973        PMID： 4730466     DOI： 10.1016/0003-9861(73)90347-0

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN： 0003-9861            Impact factor:   4.013


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  9 in total

1.  Inhibition by ethanol, acetaldehyde and trifluoroethanol of reactions catalysed by yeast and horse liver alcohol dehydrogenases.

Authors:  C J Dickenson; F M Dickinson
Journal:  Biochem J       Date:  1978-06-01       Impact factor: 3.857

2.  A kinetic analysis of enzyme systems involving four substrates.

Authors:  K R Elliott; K F Tipton
Journal:  Biochem J       Date:  1974-09       Impact factor: 3.857

3.  A study of the ionic properties of the essential histidine residue of yeast alcohol dehydrogenase in complexes of the enzyme with its coenzymes and substrates.

Authors:  C J Dickenson; F M Dickinson
Journal:  Biochem J       Date:  1977-01-01       Impact factor: 3.857

4.  The rate-determining steps of aldo-keto reductases (AKRs), a study on human steroid 5β-reductase (AKR1D1).

Authors:  Mo Chen; Yi Jin; Trevor M Penning
Journal:  Chem Biol Interact       Date:  2014-12-11       Impact factor: 5.192

5.  Inversion of substrate stereoselectivity of horse liver alcohol dehydrogenase by substitutions of Ser-48 and Phe-93.

Authors:  Keehyuk Kim; Bryce V Plapp
Journal:  Chem Biol Interact       Date:  2016-12-23       Impact factor: 5.192

6.  Macroscopic rate constants involved in the formation and interconversion of the two central enzyme--substrate complexes of the lactate dehydrogenase turnover.

Authors:  J Südi
Journal:  Biochem J       Date:  1974-04       Impact factor: 3.857

7.  In-Depth Dissection of the P133R Mutation in Steroid 5β-Reductase (AKR1D1): A Molecular Basis of Bile Acid Deficiency.

Authors:  Mo Chen; Yi Jin; Trevor M Penning
Journal:  Biochemistry       Date:  2015-10-06       Impact factor: 3.162

8.  Rate of steroid double-bond reduction catalysed by the human steroid 5β-reductase (AKR1D1) is sensitive to steroid structure: implications for steroid metabolism and bile acid synthesis.

Authors:  Yi Jin; Mo Chen; Trevor M Penning
Journal:  Biochem J       Date:  2014-08-15       Impact factor: 3.857

9.  Kinetic studies of the mechanism of pig kidney aldehyde reductase.

Authors:  F F Morpeth; F M Dickinson
Journal:  Biochem J       Date:  1981-02-01       Impact factor: 3.857
  9 in total

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