Literature summary for 4.6.1.18 extracted from

Simons, B.L.; Kaplan, H.; Fournier, S.M.; Cyr, T.; Hefford, M.A.
A novel cross-linked RNase A dimer with enhanced enzymatic properties (2007), Proteins, 66, 183-195.

Search for more literature for 4.6.1.18

Crystallization (Commentary)

Crystallization (Comment)	Organism
data of enzyme dimer composed of monomeric units covalently linked by a single amide bond between the side-chains of residues K66 and E9 by incubation of a lyophilized preparation of enzyme under vacuum at 85°C. Procedure does not induce a significant conformational change	Bos taurus

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of enzyme dimer composed of monomeric units covalently linked by a single amide bond between the side-chains of residues K66 and E9 by incubation of a lyophilized preparation of enzyme under vacuum at 85°C. Procedure does not induce a significant conformational change, dimer shows an 2fold increase in activity over monomeric enzyme and is not inhibited by the cellular ribonuclease inhibitor protein	Bos taurus

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	construction of enzyme dimer composed of monomeric units covalently linked by a single amide bond between the side-chains of residues K66 and E9 by incubation of a lyophilized preparation of enzyme under vacuum at 85°C. Dimer exhibits a twofold increase in activity over monomeric enzyme and is not inhibited by the cellular ribonuclease inhibitor protein	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Subunits

Subunits	Comment	Organism
More	construction of enzyme dimer composed of monomeric units covalently linked by a single amide bond between the side-chains of residues K66 and E9 by incubation of a lyophilized preparation of enzyme under vacuum at 85°C. Dimer exhibits a twofold increase in activity over monomeric enzyme and is not inhibited by the cellular ribonuclease inhibitor protein	Bos taurus

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Release 2023.1 (January 2023)