Literature summary for 4.6.1.18 extracted from

Lee, J.E.; Bae, E.; Bingman, C.A.; Phillips, G.N.; Raines, R.T.
Structural basis for catalysis by onconase (2008), J. Mol. Biol., 375, 165-177.

Crystallization (Commentary)

Crystallization (Comment)	Organism
wild-type in complex with oligonucleotide d(AUGA) at 1.9 A resolution, mutant T89N/E91A in complex with 5'-AMP at 1.65 A resolution. In wild-type, residue E91 forms two hydrogen bonds with the guanine nucleobase in d(AUGA), and T89 is in close proximity to that nucleobase. One nucleic acid molecule is bound to one enzyme molecule. In the mutant, four 5'-AMP molecules are bound to each enzyme molecule in a non-productive mode	Lithobates pipiens

Crystallization (Comment)

Organism

wild-type in complex with oligonucleotide d(AUGA) at 1.9 A resolution, mutant T89N/E91A in complex with 5'-AMP at 1.65 A resolution. In wild-type, residue E91 forms two hydrogen bonds with the guanine nucleobase in d(AUGA), and T89 is in close proximity to that nucleobase. One nucleic acid molecule is bound to one enzyme molecule. In the mutant, four 5'-AMP molecules are bound to each enzyme molecule in a non-productive mode

Lithobates pipiens

Protein Variants

Protein Variants	Comment	Organism
E91A	mutant prefers adenine over guanine	Lithobates pipiens
E91K	1.6-fold preference for UpA over UpG	Lithobates pipiens
E91N	mutant prefers adenine over guanine	Lithobates pipiens
E91Q	mutant prefers adenine over guanine	Lithobates pipiens
T89D	3fold increased in the value of kcat/KM for UpA cleavage	Lithobates pipiens
T89N/E91A	mutant prefers adenine over guanine 2.6fold, crystallization data of mutant in complex with 5'-AMP	Lithobates pipiens

Inhibitors

Inhibitors	Comment	Organism	Structure
5'-AMP	-	Lithobates pipiens
5'-GMP	-	Lithobates pipiens

Organism

Organism	UniProt	Comment	Textmining
Lithobates pipiens	P22069	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
6-carboxyfluorescein-dArUdAdA-6-carboxytetramethylrhodamine + H2O	-	Lithobates pipiens	?	-	?
6-carboxyfluorescein-dArUdGdA-6-carboxytetramethylrhodamine + H2O	-	Lithobates pipiens	?	-	?

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.0000037	-	5'-AMP	wild-type, pH 6.0	Lithobates pipiens
0.000067	-	5'-GMP	wild-type, pH 6.0	Lithobates pipiens