Affinity Labeling of the Active Site of Rabbit Muscle Adenylosuccinate Lyase by 2-[(4-Bromo-2,3-Dioxobutyl)Thio]Adenosine 5‘-Monophosphate
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi952640y
Reference50 articles.
1. Cloning of a cDNA encoding adenylosuccinate lyase by functional complementation in Escherichia coli.
2. Isolation of the glutamyl peptide labeled by the nucleotide analogue 2-(4-bromo-2,3-dioxobutylthio)-1,N(6)-ethenoadenosine 2',5'-biphosphate in the active site of NADP+-specific isocitrate dehydrogenase.
3. Kinetic studies of mutant human adenylosuccinase
4. Affinity labeling of an allosteric ADP site of glutamate dehydrogenase by 2-(4-bromo-2,3-dioxobutylthio)adenosine 5'-monophosphate.
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2. Expression, purification, and characterization of stable, recombinant human adenylosuccinate lyase;Protein Expression and Purification;2007-02
3. Characterization of the NAD+ binding site of Candida boidinii formate dehydrogenase by affinity labelling and site-directed mutagenesis;European Journal of Biochemistry;2000-11
4. Succinylpurinemic autism: increased sensitivity of defective adenylosuccinate lyase towards 4-hydroxy-2-nonenal;Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease;2000-03
5. Implication of Arginine-131 and Arginine-303 in the Substrate Site of Adenylosuccinate Synthetase of Escherichia coli by Affinity Labeling with 6-(4-Bromo-2,3-dioxobutyl)thioadenosine 5‘-Monophosphate;Biochemistry;1999-04-15
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