Conformationally important histidine residue in glutamate dehydrogenase from Neurospora crassa
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(80)80397-8/fullpdf
Reference13 articles.
1. Studies of Glutamate Dehydrogenase. Methionine-169: the Preferentially Carboxymethylated Residue
2. Mutational amino acid replacements in Neurospora crassa NADP-specific glutamate dehydrogenase
3. Studies of Glutamate Dehydrogenase. Regulation of Glutamate Dehydrogenase from Candida utilis by a pH and Temperature-Dependent Conformational Transition
4. The coenzyme-binding domains of glutamate dehydrogenases
5. Studies on the Reactivity towards Pyridoxal 5′-Phosphate of a Neurospora Glutamate Dehydrogenase
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1. Studies of Glutamate Dehydrogenase;European Journal of Biochemistry;2005-03-03
2. Catalytic site studies on tuna (Thunnus albacares) pyloric caeca aminopeptidase;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1995-09
3. NAD-glutamate dehydrogenase from Halobacterium halobium: pH and chemical modification studies;International Journal of Biochemistry;1993-07
4. A circular dichroism study of the pH-dependent activation/inactivation equilibrium in the glutamate dehydrogenase of Clostridium symbiosum;FEBS Letters;1990-03-26
5. Essential lysine residue(s) in the coenzyme non-specific glutamate dehydrogenase from Chlorella pyrenoidosa 82T is responsible for irreversible inactivation by diethyl pyrocarbonate and unspecific inhibition by 4-chloromercuribenzoate;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1989-02
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