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Literature summary for 4.6.1.18 extracted from

  • Pous, J.; Canals, A.; Terzyan, S.S.; Guasch, A.; Benito, A.; Ribo, M.; Vilanova, M.; Coll, M.
    Three-dimensional structure of a human pancreatic ribonuclease variant, a step forward in the design of cytotoxic ribonucleases (2000), J. Mol. Biol., 303, 49-60.
    View publication on PubMed
Search for more literature for 4.6.1.18

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
vapor-diffusion technique Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA] protein of 128 amino acid residues, catalyses the cleavage of RNA specifically on the 3'-side of pyrimidine bases. The catalytic triad comprises His12, Lys41 and His119. The amino acid sequence of the enzyme is longer than that of its bovine counterpart, with four extra amino acid residues at the C-terminal region Homo sapiens
a

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the four extra amino acid residues in the C-terminal region of the enzyme are proposed to be responsible for a decrease in the ability to cleave poly(C) Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
HP-RNase
-
 Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 the four extra amino acid residues in the C-terminal region of the enzyme are proposed to be responsible for a decrease in thermal stability Homo sapiens