Literature DB >> 226360

Active-site-specific reconstituted cobalt(II) horse-liver alcohol dehydrogenase. Changes of the spectra of the substrate trans-4-(N,N-dimethylamino)-cinnamaldehyde and of the catalytic cobalt ion upon ternary complex formation with NADH and 1,4,5,6-tetrahydronicotinamide--adenine dinucleotide.

H Dietrich, W Maret, L Wallén, M Zeppezauer.   

Abstract

Entities:  

Mesh：

Substances：

Year:  1979        PMID： 226360     DOI： 10.1111/j.1432-1033.1979.tb02057.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN： 0014-2956


× No keyword cloud information.
  4 in total

1.  Inhibition of nicotinoprotein (NAD+-containing) alcohol dehydrogenase by trans-4-(N,N-dimethylamino)-cinnamaldehyde binding to the active site.

Authors:  Sander R Piersma; Annika Norin; Simon de Vries; Hans Jörnvall; Johannis A Duine
Journal:  J Protein Chem       Date:  2003-07

2.  Thermoanaerobacter brockii alcohol dehydrogenase: characterization of the active site metal and its ligand amino acids.

Authors:  O Bogin; M Peretz; Y Burstein
Journal:  Protein Sci       Date:  1997-02       Impact factor: 6.725

3.  Magnetic and optical properties of copper-substituted alcohol dehydrogenase: a bisthiolate copper (II) complex.

Authors:  J A Farrar; G Formicka; M Zeppezauer; A J Thomson
Journal:  Biochem J       Date:  1996-07-15       Impact factor: 3.857

4.  Horse Liver Alcohol Dehydrogenase: Zinc Coordination and Catalysis.

Authors:  Bryce V Plapp; Baskar Raj Savarimuthu; Daniel J Ferraro; Jon K Rubach; Eric N Brown; S Ramaswamy
Journal:  Biochemistry       Date:  2017-07-07       Impact factor: 3.162
  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.