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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
4.6.1.18 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
4.6.1.18 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

EC Number Inhibitors Comment Organism Structure
4.6.1.18 3'-CMP strong binding by the wild-type enzyme, reduced binding by enzyme mutants T17A and T82A, kinetics, overview Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.18 Bos taurus
-
-
-

Purification (Commentary)

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

Synonyms

EC Number Synonyms Comment Organism
4.6.1.18 RNase A
-
 Bos taurus