A monomeric mutant of Clostridium symbiosum glutamate dehydrogenase: Comparison with a structured monomeric intermediate obtained during refolding-Reference-Cited by-同舟云学术

A monomeric mutant of Clostridium symbiosum glutamate dehydrogenase: Comparison with a structured monomeric intermediate obtained during refolding

Published:1998-04 Issue:4 Volume:7 Page:966-974
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Millevoi Stefania,Chiaraluce Roberta,Consalvi Valerio,Giangiacomo Laura,Pasquo Alessandra,Linda Britton K.,Stillman Timothy J.,Rice David W.,Engel Paul C.

Funder

Universitl & Ricerca Scientifica & Tecnologica

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560070414/fullpdf

Reference28 articles.

1. Urea-induced inactivation and denaturation of clostridial glutamate dehydrogenase: The absence of stable dimeric and trimeric intermediates;Aghajanian;Biochem J,1995

2. Subunit assembly and active site location in the structure of glutamate dehydrogenase;Baker;Proteins Struct Funct Genet,1992

3. Catalytic activity of bovine glutamate dehydrogenase requires a hexamer structure;Bell;Biochem J,1984

4. Britton KL 1992 High resolution structure of glutamate dehydrogenase

5. Refolding pathway and association intermediates of glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus;Consalvi;Eur J Biochem,1996

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