Knowledge

Nuclease S1

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Aspergillus nuclease S1 is a monomeric protein of a molecular weight of 38 kilodalton. It requires Zn as a cofactor and is relatively stable against denaturing agents like urea, SDS, or formaldehyde. The optimum pH for its activity lies between 4-4.5. Aspergillus nuclease S1 is known to be inhibited
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Alternative names include endonuclease S1 (Aspergillus), single-stranded-nucleate endonuclease, deoxyribonuclease S1, deoxyribonuclease S1, Aspergillus nuclease S1, Neurospora crassa single-strand specific endonuclease, S1 nuclease, single-strand endodeoxyribonuclease, single-stranded DNA specific
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These requirements and distinguishing features are responsible for function efficacy. It is an enzyme and these four features are needed for enzyme functionality. The three zinc ions are vital for catalysis. The first two zincs activate the attacking water in hydrolysis whilst the third zinc ion
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Although its primary substrate is single-stranded, it can also occasionally introduce single-stranded breaks in double-stranded DNA or RNA, or DNA-RNA hybrids. The enzyme hydrolyses single stranded region in duplex DNA such as loops or gaps. It also cleaves a strand opposite a nick on the
734:. In molecular biology, it is used in removing single stranded tails from DNA molecules to create blunt ended molecules and opening hairpin loops generated during synthesis of double stranded cDNA. 859:
Romier C, Dominguez R, Lahm A, Dahl O, Suck D (September 1998). "Recognition of single-stranded DNA by nuclease P1: high resolution crystal structures of complexes with substrate analogs".
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Yang X, Pu F, Ren J, Qu X (July 2011). "DNA-templated ensemble for label-free and real-time fluorescence turn-on detection of enzymatic/oxidative cleavage of single-stranded DNA".
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Balabanova LA, Gafurov YM, Pivkin MV, Terentyeva NA, Likhatskaya GN, Rasskazov VA (February 2012). "An extracellular S1-type nuclease of marine fungus Penicillium melinii".
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located in the cavity in the active site and its backbone supports the action one of the zinc ions. Such mechanisms are essential to the catalytic function of the enzyme.
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Podzimek T, Matoušek J, Lipovová P, Poučková P, Spiwok V, Santrůček J (February 2011). "Biochemical properties of three plant nucleases with anticancer potential".
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extracellular, that is, outside of the cell. Their function and distinguishing features mean they have potential in being exploited in the field of
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somewhat by 50 ÎĽM ATP and nearly completely by 1 mM ATP. 50% inhibition has been shown at 85 ÎĽM dAMP and 1 ÎĽM dATP but uninhibited by cAMP.
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endonuclease, single-strand-specific endodeoxyribonuclease, single strand-specific DNase and Aspergillus oryzae S1 nuclease.
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and are thought to be associated in programmed cell death and also in tissue differentiation. Furthermore, they are
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Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products
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10.1002/(sici)1097-0134(19980901)32:4<414::aid-prot2>3.0.co;2-g
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Most nucleases with EC 3.1.30.1 activity are homologous to each other in a
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Aspergillus nuclease S1 is used in the laboratory as a reagent in
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groups from 3' nucleotides. Additionally, the side chain of
400:(ssDNA) and RNA into oligo- or mononucleotides. This enzyme 1519: 1396: 1389: 1333: 1328: 1069: 324: 258: 246: 108: 1919: 988:"Specificity of the S1 nuclease from Aspergillus oryzae" 710:
This zinc-dependent nuclease protein domain produces 5'
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This article incorporates text from the public domain
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complementary strand. It has no sequence specificity.
2210: 985: 986:Wiegand RC, Godson GN, Radding CM (November 1975). 1407:Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase 1111: 475:Members of this family, including P1 and S1, are 2234: 435:. Members of the S1/P1 family are found in both 768: 766: 746:, similar activity but probably not homologous 227:P1 nuclease in complex with a substrate analog 1935: 1097: 479:with very distinguishing features, they are: 1031: 901: 817: 763: 1942: 1928: 1104: 1090: 852: 221: 1049: 1003: 962: 936: 419:Well-known versions include S1 found in 1297:Ubiquitin carboxy-terminal hydrolase L1 14: 2235: 1923: 1877:either deoxy- or ribo-     1085: 1458:Protein serine/threonine phosphatase 1032:Desai NA, Shankar V (January 2003). 1559:Cyclic nucleotide phosphodiesterase 1553:Clostridium perfringens alpha toxin 1354:Tartrate-resistant acid phosphatase 992:The Journal of Biological Chemistry 24: 1402:Pyruvate dehydrogenase phosphatase 1051:10.1111/j.1574-6976.2003.tb00626.x 1034:"Single-strand-specific nucleases" 1024: 483:a requirement for three zinc ions 25: 2274: 1302:4-hydroxybenzoyl-CoA thioesterase 937:Wrede P, Rich A (November 1979). 750:DNA/RNA non-specific endonuclease 2220: 1620:N-acetylglucosamine-6-sulfatase 1508:Sphingomyelin phosphodiesterase 454: 1429:Inositol-phosphate phosphatase 1292:Palmitoyl protein thioesterase 979: 930: 895: 838:10.1016/j.plantsci.2010.10.006 472:family called Nuclease S1/P1. 13: 1: 1792:RNA-induced silencing complex 1005:10.1016/S0021-9258(19)40751-5 756: 538: 319:Available protein structures: 1896:Serratia marcescens nuclease 1463:Dual-specificity phosphatase 1453:Protein tyrosine phosphatase 705: 463: 7: 1949: 1373:Fructose 1,6-bisphosphatase 737: 10: 2279: 1067: 732:nuclease protection assays 2106: 2098:Michaelis–Menten kinetics 2070: 2039: 2008: 1957: 1876: 1764: 1716: 1702: 1680: 1662: 1648: 1628: 1610:Galactosamine-6 sulfatase 1567: 1471: 1310: 1278: 1166:6-phosphogluconolactonase 1128: 1038:FEMS Microbiology Reviews 795:10.1007/s10126-011-9392-5 685: 675: 670: 666: 654: 646: 634: 629: 624: 606: 596: 591: 587: 575: 567: 555: 550: 545: 361: 341: 323: 318: 314: 302: 282: 270: 257: 245: 237: 232: 220: 215: 195: 183: 171: 166: 162: 143: 131: 119: 107: 95: 83: 71: 66: 54: 42: 37: 32: 1990:Diffusion-limited enzyme 1358:Purple acid phosphatases 904:Chemical Communications 725: 531:stabilizes the leaving 425:(yellow koji mold) and 1783:Microprocessor complex 1422:Beta-propeller phytase 943:Nucleic Acids Research 2083:Eadie–Hofstee diagram 2016:Allosteric regulation 1718:Endodeoxyribonuclease 1615:Iduronate-2-sulfatase 1368:Glucose 6-phosphatase 1154:Butyrylcholinesterase 2093:Lineweaver–Burk plot 1901:Micrococcal nuclease 1736:Deoxyribonuclease IV 1731:Deoxyribonuclease II 1664:Exodeoxyribonuclease 1324:Alkaline phosphatase 1149:Acetylcholinesterase 955:10.1093/nar/7.6.1457 775:Marine Biotechnology 640:Penicillium citrinum 432:Penicillium citrinum 1756:UvrABC endonuclease 1726:Deoxyribonuclease I 1449:Protein phosphatase 1385:Protein phosphatase 1183:Bile salt-dependent 1171:PAF acetylhydrolase 787:2012MarBt..14...87B 497:requires an acidic 398:single-stranded DNA 2052:Enzyme superfamily 1985:Enzyme promiscuity 1889:Mung bean nuclease 1748:Restriction enzyme 1741:Restriction enzyme 916:10.1039/c1cc12216a 744:Mung bean nuclease 561:Aspergillus oryzae 520:Disulphide bridges 490:containing common 422:Aspergillus oryzae 2208: 2207: 1917: 1916: 1913: 1912: 1909: 1908: 1698: 1697: 1690:Oligonucleotidase 1635:deoxyribonuclease 1603:Steroid sulfatase 1478:Phosphodiesterase 1207:Hormone-sensitive 699: 698: 695: 694: 620: 619: 616: 615: 406:chemical reaction 377: 376: 373: 372: 368:structure summary 211: 210: 207: 206: 126:metabolic pathway 16:(Redirected from 2270: 2263:Protein families 2225: 2224: 2216: 2088:Hanes–Woolf plot 2031:Enzyme activator 2026:Enzyme inhibitor 2000:Enzyme catalysis 1944: 1937: 1930: 1921: 1920: 1766:Endoribonuclease 1752: 1746: 1714: 1713: 1660: 1659: 1646: 1645: 1346:Acid phosphatase 1227:Monoacylglycerol 1137:ester hydrolases 1106: 1099: 1092: 1083: 1082: 1063: 1053: 1018: 1017: 1007: 983: 977: 976: 966: 934: 928: 927: 899: 893: 892: 856: 850: 849: 821: 815: 814: 770: 668: 667: 642: 622: 621: 589: 588: 563: 543: 542: 316: 315: 225: 213: 212: 164: 163: 30: 29: 27:Class of enzymes 21: 2278: 2277: 2273: 2272: 2271: 2269: 2268: 2267: 2258:Protein domains 2233: 2232: 2231: 2219: 2211: 2209: 2204: 2116:Oxidoreductases 2102: 2078:Enzyme kinetics 2066: 2062:List of enzymes 2035: 2004: 1975:Catalytic triad 1953: 1948: 1918: 1905: 1872: 1760: 1750: 1744: 1707: 1694: 1682:Exoribonuclease 1676: 1653: 1637: 1633: 1624: 1598:Arylsulfatase L 1593:Arylsulfatase B 1588:Arylsulfatase A 1563: 1476: 1467: 1306: 1274: 1136: 1124: 1110: 1080: 1066: 1027: 1025:Further reading 1022: 1021: 998:(22): 8848–55. 984: 980: 935: 931: 900: 896: 857: 853: 822: 818: 771: 764: 759: 740: 728: 708: 638: 559: 541: 514:N-glycosylation 512:asparagine via 504:contains three 466: 457: 228: 28: 23: 22: 15: 12: 11: 5: 2276: 2266: 2265: 2260: 2255: 2250: 2245: 2230: 2229: 2206: 2205: 2203: 2202: 2189: 2176: 2163: 2150: 2137: 2124: 2110: 2108: 2104: 2103: 2101: 2100: 2095: 2090: 2085: 2080: 2074: 2072: 2068: 2067: 2065: 2064: 2059: 2054: 2049: 2043: 2041: 2040:Classification 2037: 2036: 2034: 2033: 2028: 2023: 2018: 2012: 2010: 2006: 2005: 2003: 2002: 1997: 1992: 1987: 1982: 1977: 1972: 1967: 1961: 1959: 1955: 1954: 1947: 1946: 1939: 1932: 1924: 1915: 1914: 1911: 1910: 1907: 1906: 1904: 1903: 1898: 1893: 1892: 1891: 1880: 1878: 1874: 1873: 1871: 1870: 1865: 1864: 1863: 1858: 1853: 1848: 1838: 1833: 1828: 1823: 1822: 1821: 1816: 1811: 1806: 1796: 1795: 1794: 1785: 1770: 1768: 1762: 1761: 1759: 1758: 1753: 1738: 1733: 1728: 1722: 1720: 1711: 1700: 1699: 1696: 1695: 1693: 1692: 1686: 1684: 1678: 1677: 1675: 1674: 1668: 1666: 1657: 1643: 1626: 1625: 1623: 1622: 1617: 1612: 1607: 1606: 1605: 1600: 1595: 1590: 1577: 1575: 1565: 1564: 1562: 1561: 1556: 1546: 1541: 1532: 1527: 1522: 1517: 1516: 1515: 1505: 1504: 1503: 1498: 1488: 1482: 1480: 1469: 1468: 1466: 1465: 1460: 1455: 1446: 1445: 1444: 1426: 1425: 1424: 1414: 1409: 1404: 1399: 1394: 1393: 1392: 1382: 1381: 1380: 1370: 1365: 1360: 1343: 1342: 1341: 1336: 1331: 1320: 1318: 1308: 1307: 1305: 1304: 1299: 1294: 1288: 1286: 1276: 1275: 1273: 1272: 1267: 1261: 1260: 1259: 1258: 1253: 1248: 1237: 1236: 1235: 1234: 1232:Diacylglycerol 1229: 1224: 1219: 1214: 1209: 1204: 1199: 1194: 1185: 1174: 1173: 1168: 1163: 1161:Pectinesterase 1158: 1157: 1156: 1151: 1144:Cholinesterase 1140: 1138: 1126: 1125: 1109: 1108: 1101: 1094: 1086: 1065: 1064: 1028: 1026: 1023: 1020: 1019: 978: 949:(6): 1457–67. 929: 910:(28): 8133–5. 894: 851: 816: 761: 760: 758: 755: 754: 753: 747: 739: 736: 727: 724: 707: 704: 697: 696: 693: 692: 687: 683: 682: 677: 673: 672: 664: 663: 658: 652: 651: 648: 644: 643: 636: 632: 631: 627: 626: 618: 617: 614: 613: 608: 604: 603: 598: 594: 593: 585: 584: 579: 573: 572: 569: 565: 564: 557: 553: 552: 548: 547: 540: 537: 528: 527: 516: 502: 501:for catalysis. 495: 488: 470:protein domain 465: 462: 456: 453: 413: 412: 404:the following 375: 374: 371: 370: 365: 359: 358: 345: 339: 338: 328: 321: 320: 312: 311: 306: 300: 299: 286: 280: 279: 274: 268: 267: 262: 255: 254: 249: 243: 242: 241:S1-P1_nuclease 239: 235: 234: 230: 229: 226: 218: 217: 216:S1-P1 nuclease 209: 208: 205: 204: 199: 193: 192: 187: 181: 180: 175: 169: 168: 160: 159: 148: 141: 140: 135: 129: 128: 123: 117: 116: 111: 105: 104: 99: 93: 92: 87: 81: 80: 75: 69: 68: 64: 63: 58: 52: 51: 46: 40: 39: 35: 34: 26: 9: 6: 4: 3: 2: 2275: 2264: 2261: 2259: 2256: 2254: 2251: 2249: 2246: 2244: 2241: 2240: 2238: 2228: 2223: 2218: 2217: 2214: 2200: 2196: 2195: 2190: 2187: 2183: 2182: 2177: 2174: 2170: 2169: 2164: 2161: 2157: 2156: 2151: 2148: 2144: 2143: 2138: 2135: 2131: 2130: 2125: 2122: 2118: 2117: 2112: 2111: 2109: 2105: 2099: 2096: 2094: 2091: 2089: 2086: 2084: 2081: 2079: 2076: 2075: 2073: 2069: 2063: 2060: 2058: 2057:Enzyme family 2055: 2053: 2050: 2048: 2045: 2044: 2042: 2038: 2032: 2029: 2027: 2024: 2022: 2021:Cooperativity 2019: 2017: 2014: 2013: 2011: 2007: 2001: 1998: 1996: 1993: 1991: 1988: 1986: 1983: 1981: 1980:Oxyanion hole 1978: 1976: 1973: 1971: 1968: 1966: 1963: 1962: 1960: 1956: 1952: 1945: 1940: 1938: 1933: 1931: 1926: 1925: 1922: 1902: 1899: 1897: 1894: 1890: 1887: 1886: 1885: 1882: 1881: 1879: 1875: 1869: 1866: 1862: 1859: 1857: 1854: 1852: 1849: 1847: 1844: 1843: 1842: 1839: 1837: 1834: 1832: 1829: 1827: 1824: 1820: 1817: 1815: 1812: 1810: 1807: 1805: 1802: 1801: 1800: 1797: 1793: 1789: 1786: 1784: 1780: 1777: 1776: 1775: 1772: 1771: 1769: 1767: 1763: 1757: 1754: 1749: 1742: 1739: 1737: 1734: 1732: 1729: 1727: 1724: 1723: 1721: 1719: 1715: 1712: 1710: 1705: 1701: 1691: 1688: 1687: 1685: 1683: 1679: 1673: 1670: 1669: 1667: 1665: 1661: 1658: 1656: 1651: 1647: 1644: 1641: 1636: 1631: 1627: 1621: 1618: 1616: 1613: 1611: 1608: 1604: 1601: 1599: 1596: 1594: 1591: 1589: 1586: 1585: 1584: 1583: 1582:arylsulfatase 1579: 1578: 1576: 1574: 1570: 1566: 1560: 1557: 1554: 1550: 1547: 1545: 1542: 1540: 1536: 1533: 1531: 1528: 1526: 1523: 1521: 1518: 1514: 1511: 1510: 1509: 1506: 1502: 1499: 1497: 1494: 1493: 1492: 1491:Phospholipase 1489: 1487: 1484: 1483: 1481: 1479: 1474: 1470: 1464: 1461: 1459: 1456: 1454: 1450: 1447: 1443: 1439: 1435: 1432: 1431: 1430: 1427: 1423: 1420: 1419: 1418: 1415: 1413: 1410: 1408: 1405: 1403: 1400: 1398: 1395: 1391: 1388: 1387: 1386: 1383: 1379: 1376: 1375: 1374: 1371: 1369: 1366: 1364: 1361: 1359: 1355: 1351: 1347: 1344: 1340: 1337: 1335: 1332: 1330: 1327: 1326: 1325: 1322: 1321: 1319: 1317: 1313: 1309: 1303: 1300: 1298: 1295: 1293: 1290: 1289: 1287: 1285: 1281: 1277: 1271: 1268: 1266: 1263: 1262: 1257: 1254: 1252: 1249: 1247: 1244: 1243: 1242: 1241:Phospholipase 1239: 1238: 1233: 1230: 1228: 1225: 1223: 1220: 1218: 1215: 1213: 1210: 1208: 1205: 1203: 1200: 1198: 1195: 1193: 1189: 1186: 1184: 1181: 1180: 1179: 1176: 1175: 1172: 1169: 1167: 1164: 1162: 1159: 1155: 1152: 1150: 1147: 1146: 1145: 1142: 1141: 1139: 1135: 1131: 1127: 1122: 1118: 1114: 1107: 1102: 1100: 1095: 1093: 1088: 1087: 1084: 1079: 1075: 1071: 1061: 1057: 1052: 1047: 1044:(5): 457–91. 1043: 1039: 1035: 1030: 1029: 1015: 1011: 1006: 1001: 997: 993: 989: 982: 974: 970: 965: 960: 956: 952: 948: 944: 940: 933: 925: 921: 917: 913: 909: 905: 898: 890: 886: 882: 878: 874: 870: 867:(4): 414–24. 866: 862: 855: 847: 843: 839: 835: 832:(2): 343–51. 831: 827: 826:Plant Science 820: 812: 808: 804: 800: 796: 792: 788: 784: 780: 776: 769: 767: 762: 751: 748: 745: 742: 741: 735: 733: 723: 721: 717: 713: 703: 691: 688: 684: 681: 678: 674: 669: 665: 662: 659: 657: 653: 649: 645: 641: 637: 633: 628: 623: 612: 609: 605: 602: 599: 595: 590: 586: 583: 580: 578: 574: 570: 566: 562: 558: 554: 549: 544: 536: 534: 525: 521: 517: 515: 511: 508:bound to the 507: 503: 500: 496: 493: 489: 486: 482: 481: 480: 478: 477:glycoproteins 473: 471: 461: 452: 450: 449:biotechnology 446: 442: 438: 434: 433: 428: 424: 423: 417: 410: 409: 408: 407: 403: 399: 395: 392: 388: 385: 381: 369: 366: 364: 360: 357: 353: 349: 346: 344: 340: 336: 332: 329: 326: 322: 317: 313: 310: 307: 305: 301: 298: 294: 290: 287: 285: 281: 278: 275: 273: 269: 266: 263: 260: 256: 253: 250: 248: 244: 240: 236: 231: 224: 219: 214: 203: 200: 198: 194: 191: 188: 186: 182: 179: 176: 174: 170: 165: 161: 158: 155: 152: 149: 146: 142: 139: 136: 134: 130: 127: 124: 122: 118: 115: 112: 110: 106: 103: 102:NiceZyme view 100: 98: 94: 91: 88: 86: 82: 79: 76: 74: 70: 65: 62: 59: 57: 53: 50: 47: 45: 41: 36: 31: 19: 2243:Zinc enzymes 2194:Translocases 2191: 2178: 2165: 2152: 2139: 2129:Transferases 2126: 2113: 1970:Binding site 1883: 1751:}} 1745:{{ 1709:Endonuclease 1640:ribonuclease 1580: 1363:Nucleotidase 1284:Thioesterase 1041: 1037: 995: 991: 981: 946: 942: 932: 907: 903: 897: 864: 860: 854: 829: 825: 819: 781:(1): 87–95. 778: 774: 729: 714:and cleaves 709: 700: 529: 474: 467: 458: 455:Nomenclature 430: 426: 420: 418: 414: 396:that splits 391:endonuclease 379: 378: 90:BRENDA entry 1965:Active site 1884:Nuclease S1 1655:Exonuclease 1549:Lecithinase 1378:Calcineurin 1316:Phosphatase 1222:Lipoprotein 1212:Endothelial 712:nucleotides 680:Swiss-model 630:Identifiers 625:Nuclease P1 601:Swiss-model 551:Identifiers 546:Nuclease S1 492:active site 437:prokaryotes 427:Nuclease P1 380:Nuclease S1 233:Identifiers 78:IntEnz view 61:37288-25-8 38:Identifiers 33:Nuclease S1 18:P1 nuclease 2237:Categories 2168:Isomerases 2142:Hydrolases 2009:Regulation 1197:Pancreatic 1134:Carboxylic 757:References 720:tryptophan 676:Structures 671:Search for 597:Structures 592:Search for 539:Properties 510:amino acid 494:motifs and 441:eukaryotes 331:structures 147:structures 114:KEGG entry 2253:Nucleases 2248:EC 3.1.30 2047:EC number 1774:RNase III 1632:(includes 1573:Sulfatase 1486:Autotaxin 1350:Prostatic 1202:Lysosomal 1117:esterases 1113:Hydrolase 1078:IPR003154 716:phosphate 706:Mechanism 526:residues. 485:cofactors 464:Structure 429:found in 402:catalyses 277:IPR003154 67:Databases 2071:Kinetics 1995:Cofactor 1958:Activity 1868:RNase T1 1630:Nuclease 1265:Cutinase 1074:InterPro 1060:12586391 924:21629944 889:24233161 861:Proteins 846:21421379 811:17856850 803:21647618 738:See also 690:InterPro 635:Organism 611:InterPro 556:Organism 533:oxyanion 524:cysteine 522:between 445:secreted 389:) is an 387:3.1.30.1 348:RCSB PDB 272:InterPro 202:proteins 190:articles 178:articles 151:RCSB PDB 49:3.1.30.1 2227:Biology 2181:Ligases 1951:Enzymes 1841:RNase E 1836:RNase Z 1831:RNase A 1826:RNase P 1799:RNase H 1417:Phytase 1217:Hepatic 1192:Lingual 1188:Gastric 881:9726413 783:Bibcode 686:Domains 656:UniProt 607:Domains 577:UniProt 506:glycans 309:cd11010 252:PF02265 138:profile 121:MetaCyc 56:CAS no. 2213:Portal 2155:Lyases 1779:Drosha 1704:3.1.21 1672:RecBCD 1650:3.1.11 1270:PETase 1178:Lipase 1058:  1014:171268 1012:  971:  964:342320 961:  922:  887:  879:  844:  809:  801:  661:P24289 647:Symbol 582:P24021 568:Symbol 394:enzyme 363:PDBsum 337:  327:  297:SUPFAM 265:CL0368 238:Symbol 185:PubMed 167:Search 157:PDBsum 97:ExPASy 85:BRENDA 73:IntEnz 44:EC no. 2107:Types 1788:Dicer 1743:;see 1569:3.1.6 1539:PDE4B 1535:PDE4A 1473:3.1.4 1442:IMPA3 1438:IMPA2 1434:IMPA1 1312:3.1.3 1280:3.1.2 1130:3.1.1 973:41223 885:S2CID 807:S2CID 293:SCOPe 284:SCOP2 133:PRIAM 2199:list 2192:EC7 2186:list 2179:EC6 2173:list 2166:EC5 2160:list 2153:EC4 2147:list 2140:EC3 2134:list 2127:EC2 2121:list 2114:EC1 1706:-31: 1652:-16: 1638:and 1544:PDE5 1530:PDE3 1525:PDE2 1520:PDE1 1412:PTEN 1397:OCRL 1390:PP2A 1339:ALPP 1334:ALPL 1329:ALPI 1123:3.1) 1072:and 1070:Pfam 1056:PMID 1010:PMID 969:PMID 920:PMID 877:PMID 842:PMID 799:PMID 726:Uses 650:NuP1 571:NucS 518:two 439:and 356:PDBj 352:PDBe 335:ECOD 325:Pfam 289:1ak0 261:clan 259:Pfam 247:Pfam 197:NCBI 154:PDBe 109:KEGG 1861:4/5 1046:doi 1000:doi 996:250 959:PMC 951:doi 912:doi 869:doi 834:doi 830:180 791:doi 343:PDB 304:CDD 173:PMC 145:PDB 2239:: 1819:2C 1814:2B 1809:2A 1790:: 1781:: 1571:: 1451:: 1440:, 1436:, 1352:)/ 1314:: 1282:: 1251:A2 1246:A1 1132:: 1121:EC 1115:: 1076:: 1054:. 1042:26 1040:. 1036:. 1008:. 994:. 990:. 967:. 957:. 945:. 941:. 918:. 908:47 906:. 883:. 875:. 865:32 863:. 840:. 828:. 805:. 797:. 789:. 779:14 777:. 765:^ 535:. 499:pH 451:. 384:EC 354:; 350:; 333:/ 295:/ 291:/ 2215:: 2201:) 2197:( 2188:) 2184:( 2175:) 2171:( 2162:) 2158:( 2149:) 2145:( 2136:) 2132:( 2123:) 2119:( 1943:e 1936:t 1929:v 1856:3 1851:2 1846:1 1804:1 1642:) 1555:) 1551:( 1537:/ 1513:1 1501:D 1496:C 1475:: 1356:/ 1348:( 1256:B 1190:/ 1119:( 1105:e 1098:t 1091:v 1062:. 1048:: 1016:. 1002:: 975:. 953:: 947:7 926:. 914:: 891:. 871:: 848:. 836:: 813:. 793:: 785:: 487:, 382:( 20:)

Index

P1 nuclease
EC no.
3.1.30.1
CAS no.
37288-25-8
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB
RCSB PDB
PDBe
PDBsum
PMC
articles
PubMed
articles
NCBI
proteins

Pfam
PF02265

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