Modulation of the activity of mitochondrial aspartate aminotransferase H352C by the redox state of the engineered interdomain disulfide bond.-Reference-Cited by-同舟云学术

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Modulation of the activity of mitochondrial aspartate aminotransferase H352C by the redox state of the engineered interdomain disulfide bond.

Published:1994-10 Issue:41 Volume:269 Page:25432-25436
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Pan P,Jakob C A,Sandmeier E,Christen P,Gehring H

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference21 articles.

1. in Methods of Biochemical Analysis;Christen,1982

2. Tissue sulfhydryl groups

3. Syncatalytic conformational changes in mitochondrial aspartate aminotransferases. Evidence from modification and demodification of Cys 166 in the enzyme from chicken and pig.

4. Crystalline mitochondrial aspartate aminotransferase exists in only two conformations

5. Biochemistry of the SH Group;Jocelyn,1972

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Engineered control of enzyme structural dynamics and function;Protein Science;2018-02-16

2. Recombinant expression of twelve evolutionarily diverse subfamily Iα aminotransferases;Protein Expression and Purification;2008-01

3. Molecular-Dynamics Simulation of Domain Movements in Aspartate Aminotransferase;European Journal of Biochemistry;1996-09-15

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