Reaction of the nucleotide analogue 2-[(4-bromo-2,3-dioxobutyl) thio]adenosine 2′,5′-bisphosphate at the coenzyme site of wild-type and mutant NADP+-specific glutamate dehydrogenases from Salmonella typhimurium
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference33 articles.
1. Affinity labeling of a glutamyl peptide in the coenzyme binding site of NADP+-specific glutamate dehydrogenase of Salmonella typhimurium by 2-[(4-bromo-2,3-dioxobutyl)thio]-1,N6-ethenoadenosine 2′,5′-bisphosphate
2. Cloning and characterization of gdhA, the structural gene for glutamate dehydrogenase of Salmonella typhimurium
3. Interaction of pyrophosphate moieties with .alpha.-helixes in dinucleotide-binding proteins
4. AFFINITY LABELING OF PURINE NUCLEOTIDE SITES IN PROTEINS
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2. Affinity Labeling and Related Approaches to Targeting Specific Enzyme Sites;Subcellular Biochemistry;1995
3. Targeting enzyme sites in pyruvate kinase, glutamate dehydrogenase and glutathione S-transferase;Pure and Applied Chemistry;1994-01-01
4. Importance of lysine-286 at the NADP site of glutamate dehydrogenase from Salmonella typhimurium;Biochemistry;1992-09
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