219:
1195:
low-molecular-weight inhibitors can make multiple favorable interactions and approachable methods of designing transition-state analogues in the hydrolysis of sialosides, the sialidase becomes more attractive anti-influenza drug target than the haemagglutinin. After the X-ray crystal structures of several influenza virus sialidases were available, the structure-based inhibitor design was applied to discover potent inhibitors of this enzyme.
2753:
1136:
1122:
1108:
231:
1214:
sialidase than Neu5Ac2en5 and 4-guanidino-Neu5Ac2en (Compound 2), known as
Zanamivir, which is now marketed for treatment of influenza virus as a drug, have been designed by von Itzstein and coworkers. A series of amide-linked C9 modified Neu5Ac2en have been reported by Megesh and colleagues as NEU1 inhibitors.
1153:
chair conformation (the lowest-energy form in solution) to a pseudoboat conformation when the sialoside binds to the sialidase. The second step leads to an oxocarbocation intermediate, the sialosyl cation. The third step is the formation of Neu5Ac initially as the α-anomer, and then mutarotation and
1033:
neuraminidase is a mushroom-shaped projection on the surface of the influenza virus. It has a head consisting of four co-planar and roughly spherical subunits, and a hydrophobic region that is embedded within the interior of the virus' membrane. It comprises a single polypeptide chain that is
1213:
Many Neu5Ac2en-based compounds have been synthesized and tested for their influenza virus sialidase inhibitory potential. For example: The 4-substituted Neu5Ac2en derivatives (Figure 3), 4-amino-Neu5Ac2en (Compound 1), which showed two orders of magnitude better inhibition of influenza virus
1194:
There are two major proteins on the surface of influenza virus particles. One is the lectin haemagglutinin protein with three relatively shallow sialic acid-binding sites and the other is enzyme sialidase with the active site in a pocket. Because of the relative deep active site in which
393:
neuraminidase are known; many occur only in various species of duck and chicken. Subtypes N1 and N2 have been positively linked to epidemics in humans, and strains with N3 or N7 subtypes have been identified in a number of isolated deaths.
1210:-acetylneuraminic acid (Neu5Ac2en), a sialosyl cation transition-state (Figure 2) analogue, is believed the most potent inhibitor core template. Structurally modified Neu5Ac2en derivatives may give more effective inhibitors.
1148:
The enzymatic mechanism of influenza virus sialidase has been studied by Taylor et al., shown in Figure 1. The enzyme catalysis process has four steps. The first step involves the distortion of the α-sialoside from a
1038:
antigen. The composition of the polypeptide is a single chain of six conserved polar amino acids, followed by hydrophilic, variable amino acids. β-Sheets predominate as the secondary level of protein conformation.
1841:
Magesh S, Moriya S, Suzuki T, Miyagi T, Ishida H, Kiso M (January 2008). "Design, synthesis, and biological evaluation of human sialidase inhibitors. Part 1: selective inhibitors of lysosomal sialidase (NEU1)".
377:
and from the host cell receptors. Sialidase activities include assistance in the mobility of virus particles through the respiratory tract mucus and in the elution of virion progeny from the infected cell.
274:
Hydrolysis of α-(2→3)-, α-(2→6)-, α-(2→8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates
2112:
413:
182:
1918:
1077:
neuraminidase through two separate artificial tetramerization domains that facilitate the formation of catalytically active neuraminidase homotetramers from
1682:
Taylor NR, von
Itzstein M (March 1994). "Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis".
1462:
Palese P, Tobita K, Ueda M, Compans RW (October 1974). "Characterization of temperature sensitive influenza virus mutants defective in neuraminidase".
899:
756:
613:
470:
2424:
1911:
201:
2057:
2090:
1904:
1281:: cloning, sequencing, expression in Escherichia coli and identification of conserved sequences in sialidases and other proteins".
310:
to the virus than others. Other homologues are found in mammalian cells, which have a range of functions. At least four mammalian
194:
904:
761:
618:
475:
2783:
1370:"Some questions and suggestions on the type references of the official nomenclature (IUB) for sialidase(s) and endosialidase"
1341:
145:
2778:
2773:
226:. An analog of its neuraminic acid substrate, used as an inhibitor drug, is the small white and red molecule in the center.
923:
780:
637:
494:
1890:
1073:) H274Y has emphasized the need for suitable expression systems to obtain large quantities of highly pure and stable,
2803:
2472:
1786:
1734:
911:
768:
625:
482:
1557:
2788:
2354:
139:
2083:
291:
121:
1893:, Robert B. Couch, UTMB. Article includes a good clear line drawing of a neuraminidase on an influenza virus.
2628:
2366:
1896:
1499:"Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding"
1223:
417:
409:
405:
126:
1184:
916:
290:
infection. Viral neuraminidase was the first neuraminidase to be identified. It was discovered in 1957 by
2213:
773:
630:
487:
206:
114:
2743:
1584:"The crystal structure of an intramolecular trans-sialidase with a NeuAc alpha2-->3Gal specificity"
306:
found on the surface of the influenza virus. Some variants of the influenza neuraminidase confer more
2729:
2716:
2703:
2690:
2677:
2664:
2651:
2613:
2076:
1962:
1233:
1035:
49:
1625:"A generic system for the expression and purification of soluble and stable influenza neuraminidase"
2623:
2577:
2520:
2103:
1884:
1802:
von
Itzstein M, Wu WY, Jin B (June 1994). "The synthesis of 2,3-didehydro-2,4-dideoxy-4-guanidinyl-
1228:
1163:
354:
244:
142:
32:
350:
Exo hydrolysis of α-(2→3)-, α-(2→6)-, α-(2→8)-glycosidic linkages of terminal sialic acid residues
66:
2525:
2276:
2012:
1931:
1168:
432:
234:
1726:
2439:
2184:
389:
lists 137 types of neuraminidase from various species as of
October 18, 2006. Nine subtypes of
303:
1545:
1113:
Proposed mechanism of catalysis of influenza virus sialidase 4 (Link to glycosidase mechanism)
2798:
2546:
2465:
826:
1718:
830:
2618:
2398:
2349:
1636:
973:
969:
683:
540:
102:
993:
850:
707:
564:
420:(viral) are major families that contain this enzyme. GH58 is the only endo-acting family.
8:
2582:
2293:
2281:
2116:
2048:
1880:
1750:
Dyason JC, Itzstein Mv (2001). "Anti-Influenza Virus Drug Design: Sialidase
Inhibitors".
1025:
687:
544:
427:
401:
357:
283:
259:
78:
44:
1640:
247:
37:
2515:
2337:
2332:
2310:
2298:
2137:
2068:
1983:
1719:
1659:
1624:
1444:
1390:
1369:
1306:
1253:
1054:-like domain and an irregular beta-stranded domain inserted into the catalytic domain.
282:
are a large family, found in a range of organisms. The best-known neuraminidase is the
263:
1600:
1583:
1523:
1498:
1333:
157:
2793:
2305:
2179:
2000:
1859:
1823:
1819:
1782:
1730:
1699:
1664:
1605:
1528:
1479:
1475:
1436:
1395:
1347:
1337:
1324:
Schauer R (1982). "Chemistry, metabolism, and biological functions of sialic acids".
1298:
1074:
133:
1514:
1448:
1310:
16:
Glycoside hydrolase enzymes that cleave the glycosidic linkages of neuraminic acids
2561:
2556:
2530:
2458:
2315:
2201:
2005:
1851:
1815:
1759:
1691:
1654:
1644:
1595:
1518:
1510:
1471:
1426:
1385:
1377:
1329:
1290:
964:
821:
678:
535:
1623:
Schmidt PM, Attwood RM, Mohr PG, Barrett SA, McKimm-Breschkin JL (February 2011).
353:
Endo hydrolysis of (2→8)-α-sialosyl linkages in oligo- or poly(sialic) acids (see
2608:
2592:
2505:
2435:
1952:
1649:
1083:
1066:
940:
797:
654:
511:
343:
267:
1277:
Rothe B, Rothe B, Roggentin P, Schauer R (April 1991). "The sialidase gene from
1003:
860:
717:
574:
161:
2757:
2646:
2587:
2376:
2288:
2125:
1988:
1855:
1043:
223:
218:
177:
1926:
1415:"The war against influenza: discovery and development of sialidase inhibitors"
2767:
2551:
2510:
2322:
2234:
152:
369:
Sialidases, also called neuraminidases, catalyze the hydrolysis of terminal
2500:
2166:
1935:
1863:
1668:
1440:
315:
1827:
1703:
1609:
1546:
Search in UniProt
Knowledgebase (Swiss-Prot and TrEMBL) for: neuraminidase
1532:
1483:
1399:
1351:
1302:
2724:
2659:
2495:
2393:
2359:
2327:
2022:
1994:
1188:
1176:
1058:
952:
809:
666:
523:
374:
370:
1695:
90:
2403:
2371:
2017:
1927:
1806:-acetylneuraminic acid: a potent influenza virus sialidase inhibitor".
1294:
947:
804:
661:
518:
386:
1381:
2698:
2672:
2241:
2174:
2151:
2141:
2099:
1180:
1172:
1062:
1030:
390:
342:
There are two major classes of neuraminidase that cleave exo or endo
334:). Sialidases may act as pathogenic factors in microbial infections.
311:
307:
299:
287:
1763:
1431:
1414:
2752:
2246:
1091:
1088:
423:
The following is a list of major classes of neuraminidase enzymes:
1254:"WEHI History: 1957 Discovery of Neuraminidase - Key Flu Molecule"
2229:
2156:
2146:
2133:
2038:
109:
928:
785:
642:
499:
2711:
2481:
1938:
1135:
1121:
1107:
1051:
935:
792:
649:
506:
279:
189:
85:
73:
61:
1187:, that is through intravenous or intramuscular injection; and
2685:
2408:
2189:
1326:
Advances in
Carbohydrate Chemistry and Biochemistry Volume 40
1141:
Chemical structures of 4- substituted Neu5Ac2en derivatives 8
1078:
1497:
Liu C, Eichelberger MC, Compans RW, Air GM (February 1995).
2386:
2381:
2342:
2271:
2266:
2261:
2256:
2206:
2194:
1957:
1202:-acetylneuraminic acid ) derivative 2-deoxy-2, 3-didehydro-
1070:
892:
877:
749:
734:
606:
591:
463:
448:
397:
331:
327:
323:
319:
295:
97:
2450:
1781:. Washington, DC: Taylor & Francis. pp. 822–823.
1276:
1622:
1496:
230:
2098:
1840:
1461:
1154:
release as the more thermodynamically stable β-Neu5Ac.
1127:
Proposed transition state for the sialidase mechanism 7
1042:
The structure of trans-sialidase includes a catalytic
2741:
286:, a drug target for the prevention of the spread of
1681:
1582:Luo Y, Li SC, Chou MY, Li YT, Luo M (April 1998).
302:. The viral neuraminidases are frequently used as
1801:
1770:
1710:
2765:
1716:
1749:
1171:are useful for combating influenza infection:
2466:
2084:
1912:
1725:. Oxford : Oxford University Press. pp.
1363:
1361:
1844:Bioorganic & Medicinal Chemistry Letters
1834:
1616:
1412:
2058:N-acetylglucosamine-1-phosphate transferase
1795:
1675:
1581:
1575:
1406:
2473:
2459:
2091:
2077:
1919:
1905:
1490:
1455:
1358:
1317:
1270:
1034:oriented in the opposite direction to the
1883:at the U.S. National Library of Medicine
1658:
1648:
1599:
1522:
1430:
1389:
229:
217:
1367:
1323:
1191:which is in phase III clinical trials.
2766:
1558:"CAZy search: activity: neuraminidase"
314:homologues have been described in the
2454:
2072:
1900:
1776:
13:
1328:. Vol. 40. pp. 131–234.
14:
2815:
1874:
592:sialidase 2 (cytosolic sialidase)
449:sialidase 1 (lysosomal sialidase)
2751:
1413:von Itzstein M (December 2007).
1283:Molecular & General Genetics
1134:
1120:
1106:
735:sialidase 3 (membrane sialidase)
2355:Alpha-N-acetylgalactosaminidase
1779:The organic chemistry of sugars
1752:Australian Journal of Chemistry
1743:
1717:Drickamer K, Taylor MP (2006).
1515:10.1128/JVI.69.2.1099-1106.1995
1087:, which allow for secretion of
373:residues from the newly formed
296:Walter and Eliza Hall Institute
1684:Journal of Medicinal Chemistry
1550:
1539:
1419:Nature Reviews. Drug Discovery
1246:
1175:, administered by inhalation;
1:
2367:Alpha-N-acetylglucosaminidase
1601:10.1016/S0969-2126(98)00053-7
1376:. 278 ( Pt 1) (Pt 1): 311–2.
1334:10.1016/S0065-2318(08)60109-2
1239:
1224:Glycoside hydrolase family 33
1198:The unsaturated sialic acid (
1157:
2784:Genes on human chromosome 11
1820:10.1016/0008-6215(94)84065-2
1721:Introduction to glycobiology
1650:10.1371/journal.pone.0016284
1476:10.1016/0042-6822(74)90276-1
1097:
1019:
404:families, of which families
7:
2779:Genes on human chromosome 2
2774:Genes on human chromosome 6
2480:
1217:
381:
364:
337:
10:
2820:
1856:10.1016/j.bmcl.2007.11.084
1368:Cabezas JA (August 1991).
1161:
1094:and further purification.
1023:
442:
256:acetylneuraminyl hydrolase
2637:
2629:Michaelis–Menten kinetics
2601:
2570:
2539:
2488:
2423:
2222:
2165:
2124:
2111:
2047:
2031:
1971:
1963:Oligosaccharyltransferase
1945:
1234:Hemagglutinin (influenza)
999:
989:
984:
980:
963:
958:
946:
934:
922:
910:
898:
888:
883:
876:
856:
846:
841:
837:
820:
815:
803:
791:
779:
767:
755:
745:
740:
733:
713:
703:
698:
694:
677:
672:
660:
648:
636:
624:
612:
602:
597:
590:
570:
560:
555:
551:
534:
529:
517:
505:
493:
481:
469:
459:
454:
447:
437:Mammalian neuraminidases:
200:
188:
176:
171:
167:
151:
132:
120:
108:
96:
84:
72:
60:
55:
43:
31:
26:
21:
2804:Neuraminidase inhibitors
2521:Diffusion-limited enzyme
1885:Medical Subject Headings
1229:Neuraminidase inhibitors
1169:Neuraminidase inhibitors
1164:Neuraminidase inhibitors
252:sialidase, neuraminidase
2277:Bacterial neuraminidase
2013:Aspartylglucosaminidase
1932:carbohydrate metabolism
1374:The Biochemical Journal
1179:, administered orally;
1084:Staphylothermus marinus
433:Bacterial neuraminidase
416:(viral and bacterial),
235:N-Acetylneuraminic acid
2789:Carbohydrate chemistry
2440:Oxoguanine glycosylase
412:(cellular organisms),
400:defines a total of 85
304:antigenic determinants
237:
227:
2614:Eadie–Hofstee diagram
2547:Allosteric regulation
1808:Carbohydrate Research
233:
222:Neuraminidase (GH34)
221:
2624:Lineweaver–Burk plot
2429:N-Glycosyl compounds
2399:Maltase-glucoamylase
2350:Galactosylceramidase
2117:Glycoside hydrolases
2102:: sugar hydrolases (
1279:Clostridium septicum
1057:Recent emergence of
2282:Viral neuraminidase
1696:10.1021/jm00031a011
1641:2011PLoSO...616284S
1503:Journal of Virology
1026:Viral neuraminidase
428:Viral neuraminidase
284:viral neuraminidase
264:glycosidic linkages
260:glycoside hydrolase
2583:Enzyme superfamily
2516:Enzyme promiscuity
2333:Glucosylceramidase
2214:Debranching enzyme
2138:Sucrase-isomaltase
1984:Beta-galactosidase
1295:10.1007/BF00273603
402:glycosyl hydrolase
360:endo-α-sialidase.)
254:; systematic name
238:
228:
2739:
2738:
2448:
2447:
2419:
2418:
2306:alpha-Mannosidase
2180:Alpha-glucosidase
2066:
2065:
2001:alpha-Mannosidase
1382:10.1042/bj2780311
1343:978-0-12-007240-8
1205:
1017:
1016:
1013:
1012:
1009:
1008:
870:
869:
866:
865:
727:
726:
723:
722:
584:
583:
580:
579:
344:poly-sialic acids
292:Alfred Gottschalk
262:that cleaves the
216:
215:
212:
211:
115:metabolic pathway
2811:
2756:
2755:
2747:
2619:Hanes–Woolf plot
2562:Enzyme activator
2557:Enzyme inhibitor
2531:Enzyme catalysis
2475:
2468:
2461:
2452:
2451:
2436:DNA glycosylases
2202:Beta-glucosidase
2122:
2121:
2093:
2086:
2079:
2070:
2069:
2006:beta-mannosidase
1921:
1914:
1907:
1898:
1897:
1891:Orthomyxoviruses
1868:
1867:
1838:
1832:
1831:
1799:
1793:
1792:
1777:Fgedi P (2006).
1774:
1768:
1767:
1747:
1741:
1740:
1724:
1714:
1708:
1707:
1679:
1673:
1672:
1662:
1652:
1620:
1614:
1613:
1603:
1579:
1573:
1572:
1570:
1568:
1554:
1548:
1543:
1537:
1536:
1526:
1494:
1488:
1487:
1459:
1453:
1452:
1434:
1410:
1404:
1403:
1393:
1365:
1356:
1355:
1321:
1315:
1314:
1274:
1268:
1267:
1265:
1264:
1250:
1203:
1138:
1124:
1110:
982:
981:
874:
873:
839:
838:
731:
730:
696:
695:
588:
587:
553:
552:
445:
444:
441:
440:
268:neuraminic acids
169:
168:
19:
18:
2819:
2818:
2814:
2813:
2812:
2810:
2809:
2808:
2764:
2763:
2762:
2750:
2742:
2740:
2735:
2647:Oxidoreductases
2633:
2609:Enzyme kinetics
2597:
2593:List of enzymes
2566:
2535:
2506:Catalytic triad
2484:
2479:
2449:
2444:
2428:
2415:
2218:
2161:
2107:
2097:
2067:
2062:
2043:
2027:
1967:
1953:Dolichol kinase
1941:
1925:
1877:
1872:
1871:
1839:
1835:
1800:
1796:
1789:
1775:
1771:
1764:10.1071/CH01173
1758:(11): 663–670.
1748:
1744:
1737:
1715:
1711:
1680:
1676:
1621:
1617:
1580:
1576:
1566:
1564:
1556:
1555:
1551:
1544:
1540:
1509:(2): 1099–106.
1495:
1491:
1460:
1456:
1432:10.1038/nrd2400
1411:
1407:
1366:
1359:
1344:
1322:
1318:
1275:
1271:
1262:
1260:
1252:
1251:
1247:
1242:
1220:
1166:
1160:
1152:
1146:
1145:
1144:
1143:
1142:
1139:
1130:
1129:
1128:
1125:
1116:
1115:
1114:
1111:
1100:
1067:human influenza
1028:
1022:
384:
367:
340:
241:Exo-α-sialidase
22:exo-α-sialidase
17:
12:
11:
5:
2817:
2807:
2806:
2801:
2796:
2791:
2786:
2781:
2776:
2761:
2760:
2737:
2736:
2734:
2733:
2720:
2707:
2694:
2681:
2668:
2655:
2641:
2639:
2635:
2634:
2632:
2631:
2626:
2621:
2616:
2611:
2605:
2603:
2599:
2598:
2596:
2595:
2590:
2585:
2580:
2574:
2572:
2571:Classification
2568:
2567:
2565:
2564:
2559:
2554:
2549:
2543:
2541:
2537:
2536:
2534:
2533:
2528:
2523:
2518:
2513:
2508:
2503:
2498:
2492:
2490:
2486:
2485:
2478:
2477:
2470:
2463:
2455:
2446:
2445:
2443:
2442:
2432:
2430:
2421:
2420:
2417:
2416:
2414:
2413:
2412:
2411:
2401:
2396:
2391:
2390:
2389:
2384:
2377:Hexosaminidase
2374:
2369:
2364:
2363:
2362:
2352:
2347:
2346:
2345:
2340:
2330:
2325:
2320:
2319:
2318:
2308:
2303:
2302:
2301:
2296:
2289:Galactosidases
2286:
2285:
2284:
2279:
2274:
2269:
2264:
2259:
2249:
2244:
2239:
2238:
2237:
2226:
2224:
2220:
2219:
2217:
2216:
2211:
2210:
2209:
2199:
2198:
2197:
2192:
2187:
2177:
2171:
2169:
2163:
2162:
2160:
2159:
2154:
2149:
2144:
2130:
2128:
2126:Disaccharidase
2119:
2109:
2108:
2096:
2095:
2088:
2081:
2073:
2064:
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2035:
2033:
2029:
2028:
2026:
2025:
2020:
2015:
2010:
2009:
2008:
2003:
1991:
1989:Hexosaminidase
1986:
1981:
1975:
1973:
1969:
1968:
1966:
1965:
1960:
1955:
1949:
1947:
1943:
1942:
1924:
1923:
1916:
1909:
1901:
1895:
1894:
1888:
1876:
1875:External links
1873:
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1769:
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1709:
1674:
1615:
1574:
1549:
1538:
1489:
1470:(2): 397–410.
1454:
1425:(12): 967–74.
1405:
1357:
1342:
1316:
1289:(1–2): 190–7.
1269:
1244:
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1238:
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1162:Main article:
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1024:Main article:
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622:
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383:
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366:
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351:
339:
336:
278:Neuraminidase
276:
275:
224:ribbon diagram
214:
213:
210:
209:
204:
198:
197:
192:
186:
185:
180:
174:
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165:
164:
155:
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137:
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106:
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24:
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15:
9:
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2:
2816:
2805:
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2800:
2797:
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2790:
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2777:
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2759:
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2731:
2727:
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2721:
2718:
2714:
2713:
2708:
2705:
2701:
2700:
2695:
2692:
2688:
2687:
2682:
2679:
2675:
2674:
2669:
2666:
2662:
2661:
2656:
2653:
2649:
2648:
2643:
2642:
2640:
2636:
2630:
2627:
2625:
2622:
2620:
2617:
2615:
2612:
2610:
2607:
2606:
2604:
2600:
2594:
2591:
2589:
2588:Enzyme family
2586:
2584:
2581:
2579:
2576:
2575:
2573:
2569:
2563:
2560:
2558:
2555:
2553:
2552:Cooperativity
2550:
2548:
2545:
2544:
2542:
2538:
2532:
2529:
2527:
2524:
2522:
2519:
2517:
2514:
2512:
2511:Oxyanion hole
2509:
2507:
2504:
2502:
2499:
2497:
2494:
2493:
2491:
2487:
2483:
2476:
2471:
2469:
2464:
2462:
2457:
2456:
2453:
2441:
2437:
2434:
2433:
2431:
2427:: Hydrolysing
2426:
2422:
2410:
2407:
2406:
2405:
2402:
2400:
2397:
2395:
2392:
2388:
2385:
2383:
2380:
2379:
2378:
2375:
2373:
2370:
2368:
2365:
2361:
2358:
2357:
2356:
2353:
2351:
2348:
2344:
2343:non-lysosomal
2341:
2339:
2336:
2335:
2334:
2331:
2329:
2326:
2324:
2323:Hyaluronidase
2321:
2317:
2314:
2313:
2312:
2311:Glucuronidase
2309:
2307:
2304:
2300:
2297:
2295:
2292:
2291:
2290:
2287:
2283:
2280:
2278:
2275:
2273:
2270:
2268:
2265:
2263:
2260:
2258:
2255:
2254:
2253:
2252:Neuraminidase
2250:
2248:
2245:
2243:
2240:
2236:
2235:Alpha-amylase
2233:
2232:
2231:
2228:
2227:
2225:
2221:
2215:
2212:
2208:
2205:
2204:
2203:
2200:
2196:
2193:
2191:
2188:
2186:
2183:
2182:
2181:
2178:
2176:
2173:
2172:
2170:
2168:
2164:
2158:
2155:
2153:
2150:
2148:
2145:
2143:
2139:
2135:
2132:
2131:
2129:
2127:
2123:
2120:
2118:
2114:
2110:
2105:
2101:
2094:
2089:
2087:
2082:
2080:
2075:
2074:
2071:
2059:
2056:
2055:
2053:
2050:
2046:
2040:
2037:
2036:
2034:
2030:
2024:
2021:
2019:
2016:
2014:
2011:
2007:
2004:
2002:
1999:
1998:
1997:
1996:
1992:
1990:
1987:
1985:
1982:
1980:
1979:Neuraminidase
1977:
1976:
1974:
1970:
1964:
1961:
1959:
1956:
1954:
1951:
1950:
1948:
1944:
1940:
1937:
1933:
1929:
1922:
1917:
1915:
1910:
1908:
1903:
1902:
1899:
1892:
1889:
1886:
1882:
1881:Neuraminidase
1879:
1878:
1865:
1861:
1857:
1853:
1849:
1845:
1837:
1829:
1825:
1821:
1817:
1813:
1809:
1805:
1798:
1790:
1788:0-8247-5355-0
1784:
1780:
1773:
1765:
1761:
1757:
1753:
1746:
1738:
1736:0-19-928278-1
1732:
1728:
1723:
1722:
1713:
1705:
1701:
1697:
1693:
1690:(5): 616–24.
1689:
1685:
1678:
1670:
1666:
1661:
1656:
1651:
1646:
1642:
1638:
1635:(2): e16284.
1634:
1630:
1626:
1619:
1611:
1607:
1602:
1597:
1594:(4): 521–30.
1593:
1589:
1585:
1578:
1563:
1559:
1553:
1547:
1542:
1534:
1530:
1525:
1520:
1516:
1512:
1508:
1504:
1500:
1493:
1485:
1481:
1477:
1473:
1469:
1465:
1458:
1450:
1446:
1442:
1438:
1433:
1428:
1424:
1420:
1416:
1409:
1401:
1397:
1392:
1387:
1383:
1379:
1375:
1371:
1364:
1362:
1353:
1349:
1345:
1339:
1335:
1331:
1327:
1320:
1312:
1308:
1304:
1300:
1296:
1292:
1288:
1284:
1280:
1273:
1259:
1255:
1249:
1245:
1235:
1232:
1230:
1227:
1225:
1222:
1221:
1215:
1211:
1209:
1201:
1196:
1192:
1190:
1186:
1183:administered
1182:
1178:
1174:
1170:
1165:
1155:
1137:
1123:
1109:
1095:
1093:
1090:
1086:
1085:
1080:
1076:
1072:
1068:
1064:
1060:
1055:
1053:
1049:
1045:
1040:
1037:
1036:hemagglutinin
1032:
1027:
1005:
1002:
998:
995:
992:
988:
983:
979:
976:
975:
971:
968:
966:
962:
957:
954:
951:
949:
945:
942:
939:
937:
933:
930:
927:
925:
921:
918:
915:
913:
909:
906:
903:
901:
897:
894:
891:
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882:
879:
875:
872:
862:
859:
855:
852:
849:
845:
840:
836:
833:
832:
828:
825:
823:
819:
814:
811:
808:
806:
802:
799:
796:
794:
790:
787:
784:
782:
778:
775:
772:
770:
766:
763:
760:
758:
754:
751:
748:
744:
739:
736:
732:
729:
719:
716:
712:
709:
706:
702:
697:
693:
690:
689:
685:
682:
680:
676:
671:
668:
665:
663:
659:
656:
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651:
647:
644:
641:
639:
635:
632:
629:
627:
623:
620:
617:
615:
611:
608:
605:
601:
596:
593:
589:
586:
576:
573:
569:
566:
563:
559:
554:
550:
547:
546:
542:
539:
537:
533:
528:
525:
522:
520:
516:
513:
510:
508:
504:
501:
498:
496:
492:
489:
486:
484:
480:
477:
474:
472:
468:
465:
462:
458:
453:
450:
446:
443:
436:
434:
431:
429:
426:
425:
424:
421:
419:
415:
411:
407:
403:
399:
395:
392:
388:
379:
376:
372:
359:
356:
352:
349:
348:
347:
345:
335:
333:
329:
325:
321:
317:
313:
309:
305:
301:
297:
293:
289:
285:
281:
273:
272:
271:
269:
265:
261:
257:
253:
249:
246:
242:
236:
232:
225:
220:
208:
205:
203:
199:
196:
193:
191:
187:
184:
181:
179:
175:
170:
166:
163:
159:
156:
154:
153:Gene Ontology
150:
147:
144:
141:
138:
135:
131:
128:
125:
123:
119:
116:
113:
111:
107:
104:
101:
99:
95:
92:
91:NiceZyme view
89:
87:
83:
80:
77:
75:
71:
68:
65:
63:
59:
54:
51:
48:
46:
42:
39:
36:
34:
30:
25:
20:
2799:Glycobiology
2725:Translocases
2722:
2709:
2696:
2683:
2670:
2660:Transferases
2657:
2644:
2501:Binding site
2251:
2167:Glucosidases
1993:
1978:
1936:glycoprotein
1850:(2): 532–7.
1847:
1843:
1836:
1814:(2): 301–5.
1811:
1807:
1803:
1797:
1778:
1772:
1755:
1751:
1745:
1720:
1712:
1687:
1683:
1677:
1632:
1628:
1618:
1591:
1587:
1577:
1565:. Retrieved
1562:www.cazy.org
1561:
1552:
1541:
1506:
1502:
1492:
1467:
1463:
1457:
1422:
1418:
1408:
1373:
1325:
1319:
1286:
1282:
1278:
1272:
1261:. Retrieved
1257:
1248:
1212:
1207:
1199:
1197:
1193:
1185:parenterally
1167:
1147:
1082:
1056:
1047:
1041:
1029:
972:
829:
686:
543:
422:
396:
385:
368:
341:
316:human genome
277:
255:
251:
240:
239:
79:BRENDA entry
2496:Active site
2394:Iduronidase
2328:Pullulanase
1995:mannosidase
1189:laninamivir
1177:oseltamivir
1089:FLAG-tagged
1075:recombinant
1059:oseltamivir
1044:β-propeller
994:Swiss-model
884:Identifiers
878:sialidase 4
851:Swiss-model
741:Identifiers
708:Swiss-model
598:Identifiers
565:Swiss-model
455:Identifiers
371:sialic acid
67:IntEnz view
27:Identifiers
2768:Categories
2699:Isomerases
2673:Hydrolases
2540:Regulation
2404:Heparanase
2372:Fucosidase
2190:Neutral AB
2018:Fucosidase
1972:Catabolism
1928:Metabolism
1263:2023-11-08
1240:References
1158:Inhibitors
1065:resistant
1050:-terminal
1046:domain, a
990:Structures
985:Search for
959:Other data
847:Structures
842:Search for
816:Other data
704:Structures
699:Search for
673:Other data
561:Structures
556:Search for
530:Other data
387:Swiss-Prot
136:structures
103:KEGG entry
50:9001-67-6
2578:EC number
2338:lysosomal
2242:Chitinase
2207:cytosolic
2195:Neutral C
2175:Cellulase
2152:Trehalase
2142:Invertase
2100:Hydrolase
2032:Transport
1946:Anabolism
1588:Structure
1181:peramivir
1173:zanamivir
1098:Mechanism
1063:zanamivir
1031:Influenza
1020:Structure
941:NM_080741
900:NCBI gene
798:NM_006656
757:NCBI gene
655:NM_005383
614:NCBI gene
512:NM_000434
471:NCBI gene
408:(viral),
391:influenza
358:3.2.1.129
312:sialidase
308:virulence
300:Melbourne
288:influenza
56:Databases
2794:EC 3.2.1
2602:Kinetics
2526:Cofactor
2489:Activity
2247:Lysozyme
1864:18068975
1669:21326879
1629:PLOS ONE
1567:28 April
1464:Virology
1449:36867756
1441:18049471
1311:21308462
1218:See also
1092:proteins
1004:InterPro
861:InterPro
718:InterPro
575:InterPro
382:Subtypes
365:Function
338:Reaction
248:3.2.1.18
207:proteins
195:articles
183:articles
140:RCSB PDB
38:3.2.1.18
2758:Biology
2712:Ligases
2482:Enzymes
2230:Amylase
2157:Lactase
2147:Maltase
2134:Sucrase
2051:tagging
2039:SLC17A5
1939:enzymes
1934:·
1828:8050102
1704:8126701
1660:3034727
1637:Bibcode
1610:9562562
1533:7815489
1484:4472498
1400:1883340
1391:1151486
1352:6762816
1303:2034213
1000:Domains
948:UniProt
857:Domains
827:Chr. 11
805:UniProt
714:Domains
662:UniProt
571:Domains
519:UniProt
375:virions
294:at the
280:enzymes
258:) is a
162:QuickGO
127:profile
110:MetaCyc
45:CAS no.
2744:Portal
2686:Lyases
2316:Klotho
1887:(MeSH)
1862:
1826:
1785:
1733:
1729:–178.
1702:
1667:
1657:
1608:
1531:
1524:188682
1521:
1482:
1447:
1439:
1398:
1388:
1350:
1340:
1309:
1301:
1052:lectin
970:Chr. 2
953:Q8WWR8
936:RefSeq
929:608527
905:129807
889:Symbol
810:Q9UQ49
793:RefSeq
786:604617
746:Symbol
684:Chr. 2
667:Q9Y3R4
650:RefSeq
643:605528
603:Symbol
541:Chr. 6
524:Q99519
507:RefSeq
500:608272
460:Symbol
190:PubMed
172:Search
158:AmiGO
146:PDBsum
86:ExPASy
74:BRENDA
62:IntEnz
33:EC no.
2638:Types
2425:3.2.2
2409:HPSE2
2294:Alpha
2223:Other
2113:3.2.1
1445:S2CID
1307:S2CID
1079:yeast
974:q37.3
965:Locus
917:21328
831:q13.5
822:Locus
762:10825
679:Locus
536:Locus
318:(see
122:PRIAM
2730:list
2723:EC7
2717:list
2710:EC6
2704:list
2697:EC5
2691:list
2684:EC4
2678:list
2671:EC3
2665:list
2658:EC2
2652:list
2645:EC1
2387:HEXB
2382:HEXA
2360:NAGA
2299:Beta
2272:NEU4
2267:NEU3
2262:NEU2
2257:NEU1
2185:Acid
2106:3.2)
2023:NAGA
1958:GCS1
1860:PMID
1824:PMID
1783:ISBN
1731:ISBN
1700:PMID
1665:PMID
1606:PMID
1569:2019
1529:PMID
1480:PMID
1437:PMID
1396:PMID
1348:PMID
1338:ISBN
1299:PMID
1258:WEHI
1081:and
1071:H1N1
1061:and
924:OMIM
912:HGNC
893:NEU4
781:OMIM
774:7760
769:HGNC
750:NEU3
638:OMIM
631:7759
626:HGNC
619:4759
607:NEU2
495:OMIM
488:7758
483:HGNC
476:4758
464:NEU1
418:GH83
414:GH58
410:GH33
406:GH34
398:CAZy
332:NEU4
328:NEU3
324:NEU2
320:NEU1
202:NCBI
143:PDBe
98:KEGG
2049:M6P
1852:doi
1816:doi
1812:259
1760:doi
1727:177
1692:doi
1655:PMC
1645:doi
1596:doi
1519:PMC
1511:doi
1472:doi
1427:doi
1386:PMC
1378:doi
1330:doi
1291:doi
1287:226
688:q37
545:p21
298:in
266:of
178:PMC
134:PDB
2770::
2438::
2115::
2104:EC
1930::
1858:.
1848:18
1846:.
1822:.
1810:.
1756:54
1754:.
1698:.
1688:37
1686:.
1663:.
1653:.
1643:.
1631:.
1627:.
1604:.
1590:.
1586:.
1560:.
1527:.
1517:.
1507:69
1505:.
1501:.
1478:.
1468:61
1466:.
1443:.
1435:.
1421:.
1417:.
1394:.
1384:.
1372:.
1360:^
1346:.
1336:.
1305:.
1297:.
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