Literature summary for 3.2.2.8 extracted from

Lenz, S.A.P.; Wetmore, S.D.
Structural explanation for the tunable substrate specificity of an E. coli nucleoside hydrolase insights from molecular dynamics simulations (2018), J. Comput. Aided Mol. Des., 32, 1375-1388 .

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics simulation. Both in wild-type and mutant T223Y/Q227Y, inosine binding is facilitated by interactions of the ribose moiety with active site residues and Ca2+, and pi-interactions between residues His82 and His239 and the nucleobase. The lack of observed activity toward inosine for wild-type CU-NH is explained by no residue being correctly aligned to stabilize the departing nucleobase. A hydrogen-bonding network between hypoxanthine and a general acid Asp15 is present when the two Tyr mutations are engineered into the active site. This hydrogen-bonding network is only maintained when both Tyr mutations are present due to a pi-interaction between the residues	Escherichia coli

Crystallization (Comment)

Organism

molecular dynamics simulation. Both in wild-type and mutant T223Y/Q227Y, inosine binding is facilitated by interactions of the ribose moiety with active site residues and Ca2+, and pi-interactions between residues His82 and His239 and the nucleobase. The lack of observed activity toward inosine for wild-type CU-NH is explained by no residue being correctly aligned to stabilize the departing nucleobase. A hydrogen-bonding network between hypoxanthine and a general acid Asp15 is present when the two Tyr mutations are engineered into the active site. This hydrogen-bonding network is only maintained when both Tyr mutations are present due to a pi-interaction between the residues

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
T223Y/Q227Y	contrary to wild-type, mutant is able to process inosine	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P33022	-	-

Synonyms

Synonyms	Comment	Organism
CU-NH	-	Escherichia coli
cytidine-uridine nucleoside hydrolase	-	Escherichia coli
YeiK	-	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)