Evaluation of cysteine 283 and glutamic acid 284 in the coenzyme binding site of Salmonella typhimurium glutamate dehydrogenase by site-directed mutagenesis and reaction with the nucleotide analogue 2-[4-bromo-2,3-dioxobutyl)thio)-1,N6-ethenoadenosine 2‘,5‘-bisphosphate.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference23 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. Complete nucleotide sequence of the glutamate dehydrogenase gene from Escherichia coli K-12
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1. [16] Affinity labels for NAD(P)-specific sites;Methods in Enzymology;1997
2. Genetic map of Salmonella typhimurium, edition VIII;Microbiological Reviews;1995-06
3. The NADP-glutamate dehydrogenase of the cyanobacterium Synechocystis 6803: cloning, transcriptional analysis and disruption of the gdhA gene;Plant Molecular Biology;1995-04
4. Rat guanidinoacetate methyltransferase: Mutation of amino acids within a common sequence motif of mammalian methyltransferase does not affect catalytic activity but alters proteolytic susceptibility;International Journal of Biochemistry;1992-10
5. Importance of lysine-286 at the NADP site of glutamate dehydrogenase from Salmonella typhimurium;Biochemistry;1992-09
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