Literature summary for 4.6.1.18 extracted from

Doucet, N.; Khirich, G.; Kovrigin, E.L.; Loria, J.P.
Alteration of hydrogen bonding in the vicinity of histidine 48 disrupts millisecond motions in RNase A (2011), Biochemistry, 50, 1723-1730.

Search for more literature for 4.6.1.18

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes in Escherichia coli	Bos taurus

Protein Variants

Protein Variants	Comment	Organism
T17A	site-directed mutagenesis, the mutant shows reduced affinity and binding to inhibitor 3'-CMP compared to the wild-type enzyme, kinetics, and conformational exchange motions, overview	Bos taurus
T82A	site-directed mutagenesis, the mutant shows reduced affinity and binding to inhibitor 3'-CMP compared to the wild-type enzyme, kinetics, and conformational exchange motions, overview	Bos taurus

Inhibitors

Inhibitors	Comment	Organism	Structure
3'-CMP	strong binding by the wild-type enzyme, reduced binding by enzyme mutants T17A and T82A, kinetics, overview	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and mutant enzymes from Escherichia coli	Bos taurus

Synonyms

Synonyms	Comment	Organism
RNase A	-	Bos taurus

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Release 2023.1 (January 2023)