| 词条 | Pancreatic ribonuclease |
| 释义 |
| Name = Pancreatic ribonuclease | EC_number = 3.1.27.5 | CAS_number = 9001-99-4 | IUBMB_EC_number = 3/1/27/5 | GO_code = 0004522 | image = RNase A.png | width = | caption = Structure of RNase A }}{{Pfam box |Symbol = RNaseA |Name = Pancreatic ribonuclease |Pfam = PF00074 |InterPro = IPR001427 |SMART = SM00092 |PROSITE = PDOC00118 |PDB = {{PDB|11ba}} {{PDB|11bg}} {{PDB|1a2w}} {{PDB|1a4y}} {{PDB|1a5p}} {{PDB|1a5q}} {{PDB|1afk}} {{PDB|1afl}} {{PDB|1afu}} {{PDB|1agi}} }}Pancreatic ribonucleases ({{EC number|3.1.27.5}}, RNase, RNase I, RNase A, pancreatic RNase, ribonuclease I, endoribonuclease I, ribonucleic phosphatase, alkaline ribonuclease, ribonuclease, gene S glycoproteins, Ceratitis capitata alkaline ribonuclease, SLSG glycoproteins, gene S locus-specific glycoproteins, S-genotype-assocd. glycoproteins, ribonucleate 3'-pyrimidino-oligonucleotidohydrolase) 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 RNA helix by complexing with single-stranded RNA; 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. Notable family membersBovine pancreatic ribonuclease is the best-studied member of the family and has served as a model system in work related to protein folding, disulfide bond formation, protein crystallography and spectroscopy, and protein dynamics.[2] Human genome contains 8 genes that share the structure and function with bovine pancreatic ribonuclease, with 5 additional pseudo-genes. These structure and dynamics of these enzymes are related to their diverse biological functions.[3]Other proteins belonging to the pancreatic ribonuclease superfamily include: bovine seminal vesicle and brain ribonucleases; kidney non-secretory ribonucleases;[4] liver-type ribonucleases;[5] angiogenin, which induces vascularisation of normal and malignant tissues; eosinophil cationic protein,[6] a cytotoxin and helminthotoxin with ribonuclease activity; and frog liver ribonuclease and frog sialic acid-binding lectin. The sequence of pancreatic ribonucleases contains four conserved disulfide bonds and three amino acid residues involved in the catalytic activity.[7] Human genesHuman genes encoding proteins containing this domain include:
CytotoxicitySome members of the pancreatic ribonuclease family have cytotoxic effects. Mammalian cells are protected from these effects due to their extremely high affinity for ribonuclease inhibitor (RI), which protects cellular RNA from degradation by pancreatic ribonucleases.[8] Pancreatic ribonucleases that are not inhibited by RI are approximately as toxic as alpha-sarcin, diphtheria toxin, or ricin.[9] Two pancreatic ribonucleases isolated from the oocytes of the Northern leopard frog - amphinase and ranpirnase - are not inhibited by RI and show differential cytotoxicity against tumor cells.[10] Ranpirnase was studied in a Phase III clinical trial as a treatment candidate for mesothelioma, but the trial did not demonstrate statistical significance against primary endpoints.[11] References1. ^{{cite journal | vauthors = Beintema JJ, van der Laan JM | title = Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases | journal = FEBS Lett. | volume = 194 | issue = 2 | pages = 338–343 | year = 1986 | pmid = 3940901 | doi = 10.1016/0014-5793(86)80113-2 }} {{InterPro content|IPR001427}}{{Esterases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}2. ^{{cite journal | vauthors = Marshall GR, Feng JA, Kuster DJ | title = Back to the future: ribonuclease A | journal = Biopolymers | volume = 90 | issue = 3 | pages = 259–77 | year = 2008 | pmid = 17868092 | doi = 10.1002/bip.20845 }} 3. ^{{cite journal | vauthors = Narayanan C, Bernard DN, Bafna K, Gagné D, Chennubhotla CS, Doucet N, Agarwal PK | title = Conservation of Dynamics Associated with Biological Function in an Enzyme Superfamily. | journal = Structure | volume = 26 | issue = 3 | pages = 426-436 | year = Mar 2018| pmid = 29478822 | pmc = 5842143 | doi = 10.1016/j.str.2018.01.015 }} 4. ^{{cite journal | vauthors = Rosenberg HF, Tenen DG, Ackerman SJ | title = Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 86 | issue = 12 | pages = 4460–4464 | year = 1989 | pmid = 2734298 | pmc = 287289 | doi = 10.1073/pnas.86.12.4460 }} 5. ^{{cite journal | vauthors = Hofsteenge J, Matthies R, Stone SR | title = Primary structure of a ribonuclease from porcine liver, a new member of the ribonuclease superfamily | journal = Biochemistry | volume = 28 | issue = 25 | pages = 9806–9813 | year = 1989 | pmid = 2611266 | doi = 10.1021/bi00451a040 }} 6. ^{{cite journal | vauthors = Rosenberg HF, Ackerman SJ, Tenen DG | title = Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity | journal = J. Exp. Med. | volume = 170 | issue = 1 | pages = 163–176 | year = 1989 | pmid = 2473157 | pmc = 2189377 | doi = 10.1084/jem.170.1.163 }} 7. ^{{cite journal | vauthors = Raines RT | title = Ribonuclease A | journal = Chem. Rev. | volume = 98 | issue = 3 | pages = 1045–1066 | year = 1998 | pmid = 11848924 | doi = 10.1021/cr960427h }} 8. ^{{cite journal|last1=Gaur|first1=D|last2=Swaminathan|first2=S|last3=Batra|first3=JK|title=Interaction of human pancreatic ribonuclease with human ribonuclease inhibitor. Generation of inhibitor-resistant cytotoxic variants.|journal=The Journal of Biological Chemistry|date=6 July 2001|volume=276|issue=27|pages=24978–84|pmid=11342552|doi=10.1074/jbc.m102440200}} 9. ^{{cite journal|last1=Saxena|first1=SK|last2=Rybak|first2=SM|last3=Winkler|first3=G|last4=Meade|first4=HM|last5=McGray|first5=P|last6=Youle|first6=RJ|last7=Ackerman|first7=EJ|title=Comparison of RNases and toxins upon injection into Xenopus oocytes.|journal=The Journal of Biological Chemistry|date=5 November 1991|volume=266|issue=31|pages=21208–14|pmid=1939163}} 10. ^{{cite journal | vauthors = Lee JE, Raines RT | title = Ribonucleases as novel chemotherapeutics : the ranpirnase example | journal = BioDrugs | volume = 22 | issue = 1 | pages = 53–58 | year = 2008 | pmid = 18215091 | pmc = 2802594 | doi = 10.2165/00063030-200822010-00006 }} 11. ^{{cite web|title=Alfacell Annual Report 2009|url=http://www.alfacell.com/annualreport2009.pdf|accessdate=2 February 2015}} 3 : Ribonucleases|EC 3.1.27|Protein domains |
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