Abstract:
:Adenylosuccinate synthetase catalyzes the first committed step in the de novo biosynthesis of AMP, thermodynamically coupling the hydrolysis of GTP to the formation of adenylosuccinate from l-aspartate and IMP. The enzyme from Esherichia coli undergoes a ligand-induced dimerization, which leads to the assembly of a complete active site. The binding of IMP causes conformational changes over distances of 30 A, the end result of which is the activation of essential catalytic elements and the organization of the binding pocket for Mg(2+)-GTP. The enzyme promotes first a phosphoryl transfer from GTP to the 6-oxygen atom of IMP, by way of a transition state that has characteristics of both associative and dissociative reaction pathways. Following the formation of 6-phosphoryl-IMP, the enzyme then catalyzes the nucleophilic displacement of the 6-phosphoryl group by the alpha-amino group of l-aspartate in a transition state, which requires two metal cations.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Honzatko RB,Fromm HJdoi
10.1006/abbi.1999.1383subject
Has Abstractpub_date
1999-10-01 00:00:00pages
1-8issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(99)91383-8journal_volume
370pub_type
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