Kinetics and Mechanism of the Citrate Synthase from the Thermophilic Archaeon Thermoplasma acidophilum-Reference-Cited by-同舟云学术

Kinetics and Mechanism of the Citrate Synthase from the Thermophilic Archaeon Thermoplasma acidophilum

Published:2000-02-12 Issue:9 Volume:39 Page:2283-2296
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kurz Linda C.¹,Drysdale George¹,Riley Marian¹,Tomar Maharaj Alejandro¹,Chen Judy¹,Russell Rupert J. M.¹,Danson Michael J.¹

Affiliation:

1. Department of Biochemistry and Molecular Biophysics, Division of Biology and Biomedical Sciences, Washington University School of Medicine, St. Louis, Missouri 63110, and Centre for Extremophile Research, Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, U.K.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi991982r

Reference74 articles.

1. Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and S-acetonyl-coenzyme A

2. Ligand-induced conformational changes of citrate synthase studied with the fluorescent probe 8-anilinonaphthalene 1-sulfonate

Cited by 24 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. Heteroexpression and biochemical characterization of thermostable citrate synthase from the cyanobacteria Anabaena sp. PCC7120;Protein Expression and Purification;2020-04

2. Acetyl Coenzyme A Analogues as Rationally Designed Inhibitors of Citrate Synthase;ChemBioChem;2019-03-29

3. An active site–tail interaction in the structure of hexahistidine-tagged Thermoplasma acidophilum citrate synthase;Acta Crystallographica Section F Structural Biology Communications;2015-09-23

4. Kinetic and Chemical Mechanism of Malate Synthase from Mycobacterium tuberculosis;Biochemistry;2011-07-18

5. Enzyme:Nanoparticle Bioconjugates with Two Sequential Enzymes: Stoichiometry and Activity of Malate Dehydrogenase and Citrate Synthase on Au Nanoparticles;Langmuir;2010-12-21