Evidence for an arginine residue at the substrate binding site of Escherichia coli adenylosuccinate synthetase as studied by chemical modification and site-directed mutagenesis
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference28 articles.
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1. Convergent evolution of nitrogen-adding enzymes in the purine nucleotide biosynthetic pathway, based on structural analysis of adenylosuccinate synthetase (PurA);The Journal of General and Applied Microbiology;2023
2. A mathematical model for the adenylosuccinate synthetase reaction involved in purine biosynthesis;Theoretical Biology and Medical Modelling;2007-02-27
3. Adenylosuccinate Syntheatase: Recent Developments;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
4. Active site determination of yeast geranylgeranyl protein transferase type I expressed in Escherichia coli;European Journal of Biochemistry;1999-10
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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