Literature summary for 6.3.4.4 extracted from

Wang, W.; Gorrell, A.; Honzatko, R.B.; Fromm, H.J.
A study of Escherichia coli adenylosuccinate synthetase association states and the interface residues of the homodimer (1997), J. Biol. Chem., 272, 7078-7084.

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Protein Variants

Protein Variants	Comment	Organism
D231A	wild-type and mutant enzymes, R132K, R143L, and D231A exist as a mixture of monomers and dimers, with a majority of the enzyme in the monomeric state. In the presence of active site ligands, the wild-type enzyme exists almost exclusively as a dimer, whereas the mutant enzymes show only slightly decreased dissociation constants for the dimerization	Escherichia coli
R132L	wild-type and mutant enzymes, R132K, R143L, and D231A exist as a mixture of monomers and dimers, with a majority of the enzyme in the monomeric state. In the presence of active site ligands, the wild-type enzyme exists almost exclusively as a dimer, whereas the mutant enzymes show only slightly decreased dissociation constants for the dimerization	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	wild-type and mutant enzymes, R132K, R143L, and D231A	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
GTP + IMP + L-Asp	-	Escherichia coli	GDP + phosphate + adenylosuccinate	-	?

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Release 2023.1 (January 2023)