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Literature summary for 4.6.1.18 extracted from

  • Chatani, E.; Hayashi, R.; Moriyama, H.; Ueki, T.
    Conformational strictness required for maximum activity and stability of bovine pancreatic ribonuclease A as revealed by crystallographic study of three Phe120 mutants at 1.4 A resolution (2002), Protein Sci., 11, 72-81.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor-diffusion method Bos taurus

Protein Variants

Protein Variants Comment Organism
F120A mutant with decreased activity Bos taurus
F120G mutant with decreased activity Bos taurus
F120W mutant with decreased activity Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P61823 bovine
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Reaction

Reaction Comment Organism Reaction ID
an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA] His12, His119 and Lys41 comprise the catalytic site, and several other amino acid residues serve as substrate binding subsites. The mutagenic replacement of Phe120 causes a positional change in His119 and that is a major cause in decreasing the activity of the enzyme. Phe120 is important in fixing the proper spatial position of His119 near the C-terminal region for efficient activity. Phe120 interacts not directly with His119, but with the hydrophobic core Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
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Bos taurus
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