Pancreatic ribonuclease

Pancreatic ribonuclease
Identifiers
Symbol RNaseA
Pfam PF00074
InterPro IPR001427
SMART SM00092
PROSITE PDOC00118

Pancreatic ribonucleasea are pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and of some reptiles.[1]

Specifically, the enzymes are involved in endonucleolytic cleavage of 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates. Ribonuclease can unwind the DNA helix by complexing with single-stranded DNA; the complex arises by an extended multi-site cation-anion interaction between lysine and arginine residues of the enzyme and phosphate groups of the nucleotides.

Other proteins belonging to the pancreatic RNAse family include: bovine seminal vesicle and brain ribonucleases; kidney non-secretory ribonucleases;[2] liver-type ribonucleases;[3] angiogenin, which induces vascularisation of normal and malignant tissues; eosinophil cationic protein,[4] a cytotoxin and helminthotoxin with ribonuclease activity; and frog liver ribonuclease and frog sialic acid-binding lectin. The sequence of pancreatic RNases contains four conserved disulfide bonds and three amino acid residues involved in the catalytic activity.

Examples

Human genes encoding proteins containing this domain include:

References

  1. ^ van der Laan JM, Beintema JJ (1986). "Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases". FEBS Lett. 194 (2): 338–343. doi:10.1016/0014-5793(86)80113-2. PMID 3940901. 
  2. ^ Rosenberg HF, Ackerman SJ, Tenen DG (1989). "Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family". Proc. Natl. Acad. Sci. U.S.A. 86 (12): 4460–4464. doi:10.1073/pnas.86.12.4460. PMC 287289. PMID 2734298. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=287289. 
  3. ^ Stone SR, Hofsteenge J, Matthies R (1989). "Primary structure of a ribonuclease from porcine liver, a new member of the ribonuclease superfamily". Biochemistry 28 (25): 9806–9813. doi:10.1021/bi00451a040. PMID 2611266. 
  4. ^ Rosenberg HF, Ackerman SJ, Tenen DG (1989). "Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity". J. Exp. Med. 170 (1): 163–176. doi:10.1084/jem.170.1.163. PMC 2189377. PMID 2473157. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2189377. 

This article incorporates text from the public domain Pfam and InterPro IPR001427