5,5′-Dithiobis-(2-Nitrobenzoic Acid) as a Probe for a Non-Essential Cysteine Residue at the Medium Chain Acyl-Coenzyme a Dehydrogenase Binding Site of the Human ‘Electron Transferring Flavoprotein’ (ETF)-Reference-Cited by-同舟云学术

5,5′-Dithiobis-(2-Nitrobenzoic Acid) as a Probe for a Non-Essential Cysteine Residue at the Medium Chain Acyl-Coenzyme a Dehydrogenase Binding Site of the Human ‘Electron Transferring Flavoprotein’ (ETF)

Published:1999-01 Issue:5 Volume:14 Page:381-390
ISSN:8755-5093
Container-title:Journal of Enzyme Inhibition
language:en
Short-container-title:Journal of Enzyme Inhibition

Author:

Parker Antony,Engel Paul C.

Publisher

Informa UK Limited

Subject

Molecular Medicine,Biochemistry

Link

http://www.tandfonline.com/doi/pdf/10.3109/14756369909030330

Reference23 articles.

1. Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution

2. ON THE MECHANISM OF DEHYDROGENATION OF FATTY ACYL DERIVATIVES OF COENZYME A

3. Beinert H. The Enzymes, P. D. Boyer, H. Lardy, K. Myrback. Academic Press, NY 1963; Vol. 7: 447–466, part A

4. Purification and characterization of isovaleryl coenzyme A dehydrogenase from rat liver mitochondria.

5. The purification and characterization of glutaryl-coenzyme A dehydrogenase from porcine and human liver.

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1. Binding of the Human “Electron Transferring Flavoprotein” (ETF) to the Medium Chain Acyl-CoA Dehydrogenase (MCAD) Involves an Arginine and Histidine Residue;Journal of Enzyme Inhibition and Medicinal Chemistry;2003-10

2. A single arginine residue is required for the interaction of the electron transferring flavoprotein (ETF) with three of its dehydrogenase partners;Molecular and Cellular Biochemistry;2003