Pancreatic ribonucleases (EC 184.108.40.206) are pyrimidine-specific endonucleases
present in high quantity in the pancreas of a number of mammalian taxa and of
a few reptiles [1,2]. As shown in the following schematic representation of
the sequence of pancreatic RNases there are four conserved disulfide bonds and
three amino acid residues involved in the catalytic activity.
Angiogenin, which induces vascularization of normal and malignant tissues.
It abolishes protein synthesis by specifically hydrolyzing cellular tRNAs.
Eosinophil cationic protein (ECP) , a cytotoxin and helminthotoxin with
Frog liver ribonuclease and frog sialic acid-binding lectin .
The signature pattern we developed for these proteins includes five conserved
residues: a cysteine involved in a disulfide bond, a lysine involved in the
catalytic activity and three other residues important for substrate binding.
October 1993 / Text revised.
PROSITE method (with tools and information) covered by this documentation:
Beintema J.J. Schuller C. Irie M. Carsana A.
Molecular evolution of the ribonuclease superfamily.
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