Literature DB >> 4348442

Conformational studies on lipoamide dehydrogenase from pig heart. 4. The binding of NAD + to non-equivalent sites.

H v Muiswinkel-Voetberg, C Veeger.   

Abstract

Entities:  

Mesh：

Substances：

Year:  1973        PMID： 4348442     DOI： 10.1111/j.1432-1033.1973.tb02682.x

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


× No keyword cloud information.
  4 in total

1.  A pH-dependent kinetic model of dihydrolipoamide dehydrogenase from multiple organisms.

Authors:  Michael A Moxley; Daniel A Beard; Jason N Bazil
Journal:  Biophys J       Date:  2014-12-16       Impact factor: 4.033

2.  Global Kinetic Analysis of Mammalian E3 Reveals pH-dependent NAD+/NADH Regulation, Physiological Kinetic Reversibility, and Catalytic Optimum.

Authors:  Michael A Moxley; Daniel A Beard; Jason N Bazil
Journal:  J Biol Chem       Date:  2015-12-07       Impact factor: 5.157

3.  The mechanism of the quinone reductase reaction of pig heart lipoamide dehydrogenase.

Authors:  J Vienozinskis; A Butkus; N Cenas; J Kulys
Journal:  Biochem J       Date:  1990-07-01       Impact factor: 3.857

4.  Isolation of a specific lipoamide dehydrogenase for a branched-chain keto acid dehydrogenase from Pseudomonas putida.

Authors:  J R Sokatch; V McCully; J Gebrosky; D J Sokatch
Journal:  J Bacteriol       Date:  1981-11       Impact factor: 3.490
  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.