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Polygalacturonase

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of pectin is largely involved in the later stages of fruit ripening, especially as the fruit becomes overripe. While tomatoes are the prime example of high PG activity, this enzyme is also very active in avocado and peach ripening. PG enzymes in peach, two exo-PGs and one endo-PG, become active when
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Exo- and Endo-polygalacturonases utilize different hydrolytic modes of action. Endo-polygalacturonases hydrolyze in a random fashion along the polygalacturonan network. This method results in oligogalacturonides. Exo-polygalacturonases hydrolyze at the non-reducing end of the polymer, generating a
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It is largely unclear whether PGs play a role in facilitating abscission in certain plants, and if they do, whether they are exo- or endo-acting. Conflicting research has been published on, for example, whether PG is involved in citrus fruit abscission. One particular issue has been the usage of
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Daniel King, Carl Bergmann, Ron Orlando, Jacques A. E. Benen, Harry C. M. Kester, and Jaap Visser; "Use of Amide Exchange Mass Spectrometry To Study Conformational Changes within the Endopolygalacturonase II – Polygalacturonic Acid – Polygalacturonase Inhibiting Protein System", Biochem. 41,
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Federici L, Caprari C, Mattei B, Savino C, Di Matteo A, De Lorenzo G, Cervone F, Tsernoglou D. Structural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein). Proc Natl Acad Sci U S A. 2001 Nov
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plant PGs works to soften and sweeten fruit during the ripening process. Similarly, phytopathogens use PGs as a means to weaken the pectin network, so that digestive enzymes can be excreted into the plant host to acquire nutrients.
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that are not able to measure exo-PG activity. An additional complication is the difference in PG enzymatic activity between fruit and leaf cell-separation zones. In peach, PG activity was only detected in fruit abscission zones.
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the fruit is already soft. Fruits like persimmons may either lack PG enzymes or have very low levels of PG and as such they have not been detected yet. In these cases, other enzymes may catalyze the ripening process.
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Due to the applicability of this enzyme's activity on agricultural productivity and commercial success, much of the research on PGs has revolved around the role of PGs in the fruit ripening process,
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proteins that have been reported to demonstrate both non-competitive and competitive inhibition of PGs. The active site of PG interacts with a pocket containing multiple polar amino acids in
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PG gene was introduced, preventing polygalacturonase from ripening and softening the tomato. Although this method has been shown to reduce PG enzymatic activity by 70 to 90%, the PG antisense
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that slow the hydrolytic activity of PG. These inhibitors also prompt long chain oligogalacturonide accumulation in order to encourage a defense mechanism against the attack. The
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D'Ovidio R, Mattei B, Roberti S, Bellincampi D (February 2004). "Polygalacturonases, polygalacturonase-inhibiting proteins and pectic oligomers in plant-pathogen interactions".
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as D131, S133, T155, D157, T180, and D203. Using PGIP2 as a template, the theoretical structures of other PGIPs have been determined for some other common crops.
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Bonghi C, Rascio N, Ramina A, Casadoro G (December 1992). "Cellulase and polygalacturonase involvement in the abscission of leaf and fruit explants of peach".
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Jones, T. M., Anderson, A. J., and Albersheim, P. (1972) Host–pathogen interactions IV, Studies on the polysaccharide-degrading enzymes secreted by
1966: 200: 1152:"Altered middle lamella homogalacturonan and disrupted deposition of (1→5)-α-L-arabinan in the pericarp of Cnr, a ripening mutant of tomato" 442:-glycosyl bonds in pectin's polygalacturonan network, resulting in α-1,4-polygalacturonic residues. The rate of hydrolysis is dependent on 1632: 630:
Phytopathogenic fungi expose plant cell walls to cell wall degrading enzymes (CWDEs) like PGs. In response, most plants have natural
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damage cotton and other crops because they secrete PGs in their saliva that digest plant tissue. They employ both exo- and endo-PGs.
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Bonivento D, Pontiggia D, Matteo AD, Fernandez-Recio J, Salvi G, Tsernoglou D, Cervone F, Lorenzo GD, Federici L (January 2008).
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chain length. Low rates of hydrolysis are associated with very short chains (e.g. digalacturonic acid) and very long chains.
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between strands, is a common characteristic of enzymes involved in the degradation of pectin. The interior of the β helix is
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binding, D212 (a general acid) is responsible for proton donation to the glycosydic oxygen, and D213 and D191 activate H
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Di Matteo A, Federici L, Mattei B, Salvi G, Johnson KA, Savino C, De Lorenzo G, Tsernoglou D, Cervone F (August 2003).
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G Downs C, J Brady C, Gooley A (June 1992). "Exopolygalacturonase protein accumulates late in peach fruit ripening".
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allows fungal polygalacturonases to more effectively degrade a wider range of plant tissues. PG variety in optimal
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has been used to determine the three-dimensional structure of several PGs in different organisms. Fungal PGs from
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Exo-PGs play a role in enabling pollen tube elongation since pectin rearrangement is necessary for the growth of
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Orfila C, Seymour GB, Willats WG, Huxham IM, Jarvis MC, Dover CJ, Thompson AJ, Knox JP (May 2001).
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polygalacturonase and a modeled structure of the polygalacturonase-octagalacturonate complex".
662:. The charged and polar residues that interact with the PG active site have been identified in 652: 471: 909:
van Santen Y, Benen JA, Schröter KH, Kalk KH, Armand S, Visser J, Dijkstra BW (October 1999).
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PGIP2. The inhibitor prevents substrate binding by occupying the active site, resulting in
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Pressey R, Reger BJ (1989). "Polygalacturonase in pollen from corn and other grasses".
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Ferrari S, Savatin DV, Sicilia F, Gramegna G, Cervone F, Lorenzo GD (13 Mar 2013).
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Proceedings of the National Academy of Sciences of the United States of America
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Proceedings of the National Academy of Sciences of the United States of America
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Polygalacturonan, whose major component is galacturonic acid, is a significant
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Celorio-Mancera Mde L, Carl Greve L, Teuber LR, Labavitch JM (February 2009).
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The crystal structures for PGIP and PGIP2 have been determined for the bean
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and identification of active site residues by site-directed mutagenesis"
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van Pouderoyen G, Snijder HJ, Benen JA, Dijkstra BW (November 2003).
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The mechanism of polygalacturonase: hydrolysis of polygalacturonan.
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Pickersgill R, Smith D, Worboys K, Jenkins J (September 1998).
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and its interaction with polygalacturonase-inhibiting proteins"
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Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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Cho SW, Lee S, Shin W (August 2001). "The X-ray structure of
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Computer generated image of Polygalacturonase as found in
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Harholt J, Suttangkakul A, Vibe Scheller H (June 2010).
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f. sp. lycopersici, Physiol. Plant Pathol. 2, 153-166.
2283: 438:, an enzyme that degrades pectin by hydrolyzing the 1392:"Role of Polygalacturonase in Bean Leaf Abscission" 337:. This highly stable structure, thanks to numerous 1198: 560:. This PG activity has been found in grasses like 1223: 2307: 1003:"Information on EC 3.2.1.15 - polygalacturonase" 229:pectin depolymerase, pectolase, pectin hydrolase 1282: 1224:Sheehy RE, Kramer M, Hiatt WR (December 1988). 801: 799: 797: 414:residues: H188, R267, and K269 are involved in 1524: 1522: 1520: 1491:Archives of Insect Biochemistry and Physiology 241:-galacturonan glycanohydrolase (endo-cleaving) 2008: 1626: 956:"Crystal structure of polygalacturonase from 620:Polygalacturonase inhibitor protein found in 1217: 1022: 794: 1517: 1276: 902: 854: 2015: 2001: 1633: 1619: 1389: 1018: 1016: 947: 686: 24: 1564: 1554: 1415: 1308: 1259: 1249: 1175: 1126: 1077: 1067: 997: 995: 975: 930: 885: 837: 761: 759: 757: 755: 753: 564:as well as in trees, particularly in the 541:did not hinder normal color development. 485: 233:poly-α-1,4-galacturonide glycanohydrolase 727:"Medical Definition of Polygalacturonan" 615: 448: 351: 1358: 1199:Berg JM, Tymoczko JL, Stryer L (2012). 1013: 2308: 1390:Berger RK, Reid PD (15 January 1979). 992: 750: 333:form a helical shape that is called a 1996: 1614: 1283:Hadfield KA, Bennett AB (June 1998). 682: 680: 678: 362:(1HG8) showing active site in magenta 639:polygalacturonase inhibitor proteins 1361:"Polygalacturonase in tree pollens" 964:The Journal of Biological Chemistry 919:The Journal of Biological Chemistry 13: 1346:10.1111/j.1399-3054.1992.tb04715.x 675: 513:holds neighboring cells together. 14: 2327: 1601:PG & PGIP Structural Database 1594: 316:. Therefore, the activity of the 2293: 356:Image of polygalacturonase from 329:This enzyme's multiple parallel 1897:Alpha-N-acetylgalactosaminidase 1581: 1475: 1432: 1383: 1352: 1325: 1192: 1143: 1094: 1043: 458:Exo- vs Endo-polygalacturonases 809: 737: 719: 1: 1909:Alpha-N-acetylglucosaminidase 887:10.1016/s0014-5793(03)01221-3 669: 611: 397:have also been crystallized. 1377:10.1016/0031-9422(91)85006-L 1037:10.1016/0168-9452(89)90008-3 780:10.1016/j.bbapap.2003.08.012 693:Journal of Molecular Biology 429: 324: 7: 2022: 527:genetically modified tomato 501:Pectin is one of the three 10: 2332: 1056:Frontiers in Plant Science 525:available in stores was a 2179: 2171:Michaelis–Menten kinetics 2143: 2112: 2081: 2030: 1965: 1764: 1707: 1666: 1653: 1359:Pressey, Russell (1991). 410:PG comprises six charged 199: 187: 175: 170: 166: 147: 135: 123: 111: 99: 87: 75: 70: 58: 46: 41: 23: 18: 2063:Diffusion-limited enzyme 1103:"Biosynthesis of pectin" 977:10.1074/jbc.273.38.24660 932:10.1074/jbc.274.43.30474 602:Agricultural pests like 1819:Bacterial neuraminidase 1556:10.1073/pnas.1733690100 1441:Plant Molecular Biology 1251:10.1073/pnas.85.23.8805 1069:10.3389/fpls.2013.00049 434:Polygalacturonase is a 312:network that comprises 1982:Oxoguanine glycosylase 705:10.1006/jmbi.2001.4919 653:competitive inhibition 627: 486:Agricultural relevance 454: 363: 218:Endo-polygalacturonase 19:Endo-polygalacturonase 2156:Eadie–Hofstee diagram 2089:Allosteric regulation 1334:Physiologia Plantarum 1119:10.1104/pp.110.156588 820:Colletotrichum lupini 689:Aspergillus aculeatus 619: 452: 376:Aspergillus aculeatus 371:Colletotrichum lupini 367:X-ray crystallography 355: 33:Aspergillus aculeatus 2166:Lineweaver–Burk plot 1971:N-Glycosyl compounds 1941:Maltase-glucoamylase 1892:Galactosylceramidase 1659:Glycoside hydrolases 1644:: sugar hydrolases ( 1408:10.1104/pp.63.6.1133 1301:10.1104/pp.117.2.337 1168:10.1104/pp.126.1.210 407:Fusarium moniliforme 359:Fusarium moniliforme 1824:Viral neuraminidase 1547:2003PNAS..10010124D 1242:1988PNAS...85.8805S 643:leucine-rich repeat 424:nucleophilic attack 2125:Enzyme superfamily 2058:Enzyme promiscuity 1875:Glucosylceramidase 1756:Debranching enzyme 1680:Sucrase-isomaltase 1606:Pectinase Database 1503:10.1002/arch.20282 1453:10.1007/bf00027155 958:Erwinia carotovora 839:10.1002/prot.21610 806:6;98(23):13425-30. 745:Fusarium oxysporum 648:Phaseolus vulgaris 628: 623:Phaseolus vulgaris 566:Eastern cottonwood 455: 388:Erwinia carotovora 364: 235:; systematic name 2281: 2280: 1990: 1989: 1961: 1960: 1848:alpha-Mannosidase 1722:Alpha-glucosidase 1588:10225-10233, 2002 913:Aspergillus niger 865:Aspergillus niger 468:galacturonic acid 394:Bacillus subtilis 382:Aspergillus niger 308:component of the 294: 284: 266: 257:galacturonic acid 240: 215: 214: 211: 210: 130:metabolic pathway 2323: 2298: 2297: 2289: 2161:Hanes–Woolf plot 2104:Enzyme activator 2099:Enzyme inhibitor 2073:Enzyme catalysis 2017: 2010: 2003: 1994: 1993: 1978:DNA glycosylases 1744:Beta-glucosidase 1664: 1663: 1635: 1628: 1621: 1612: 1611: 1589: 1585: 1579: 1578: 1568: 1558: 1526: 1515: 1514: 1488: 1479: 1473: 1472: 1436: 1430: 1429: 1419: 1402:(6): 1133–1137. 1396:Plant Physiology 1387: 1381: 1380: 1371:(6): 1753–1755. 1356: 1350: 1349: 1329: 1323: 1322: 1312: 1289:Plant Physiology 1280: 1274: 1273: 1263: 1253: 1221: 1215: 1214: 1196: 1190: 1189: 1179: 1156:Plant Physiology 1147: 1141: 1140: 1130: 1107:Plant Physiology 1098: 1092: 1091: 1081: 1071: 1047: 1041: 1040: 1020: 1011: 1010: 999: 990: 989: 979: 960:ssp. carotovora" 951: 945: 944: 934: 925:(43): 30474–80. 906: 900: 899: 889: 871: 858: 852: 851: 841: 813: 807: 803: 792: 791: 763: 748: 741: 735: 734: 723: 717: 716: 684: 584:Abscission zones 545:Depolymerization 314:plant cell walls 295:-galacturonosyl) 292: 285:-galacturonosyl) 282: 267:-galacturonosyl) 264: 253:glycosidic bonds 238: 168: 167: 36:(1IA5) at pH 8.5 28: 16: 15: 2331: 2330: 2326: 2325: 2324: 2322: 2321: 2320: 2306: 2305: 2304: 2292: 2284: 2282: 2277: 2189:Oxidoreductases 2175: 2151:Enzyme kinetics 2139: 2135:List of enzymes 2108: 2077: 2048:Catalytic triad 2026: 2021: 1991: 1986: 1970: 1957: 1760: 1703: 1649: 1639: 1597: 1592: 1586: 1582: 1541:(17): 10124–8. 1527: 1518: 1486: 1480: 1476: 1437: 1433: 1388: 1384: 1357: 1353: 1330: 1326: 1281: 1277: 1222: 1218: 1211: 1197: 1193: 1148: 1144: 1099: 1095: 1048: 1044: 1021: 1014: 1001: 1000: 993: 970:(38): 24660–4. 952: 948: 907: 903: 869: 859: 855: 814: 810: 804: 795: 764: 751: 742: 738: 725: 724: 720: 685: 676: 672: 614: 529:(also known as 507:plant cell wall 505:present in the 503:polysaccharides 488: 432: 421: 343:disulfide bonds 327: 300: 290: 280: 276: 37: 12: 11: 5: 2329: 2319: 2318: 2303: 2302: 2279: 2278: 2276: 2275: 2262: 2249: 2236: 2223: 2210: 2197: 2183: 2181: 2177: 2176: 2174: 2173: 2168: 2163: 2158: 2153: 2147: 2145: 2141: 2140: 2138: 2137: 2132: 2127: 2122: 2116: 2114: 2113:Classification 2110: 2109: 2107: 2106: 2101: 2096: 2091: 2085: 2083: 2079: 2078: 2076: 2075: 2070: 2065: 2060: 2055: 2050: 2045: 2040: 2034: 2032: 2028: 2027: 2020: 2019: 2012: 2005: 1997: 1988: 1987: 1985: 1984: 1974: 1972: 1963: 1962: 1959: 1958: 1956: 1955: 1954: 1953: 1943: 1938: 1933: 1932: 1931: 1926: 1919:Hexosaminidase 1916: 1911: 1906: 1905: 1904: 1894: 1889: 1888: 1887: 1882: 1872: 1867: 1862: 1861: 1860: 1850: 1845: 1844: 1843: 1838: 1831:Galactosidases 1828: 1827: 1826: 1821: 1816: 1811: 1806: 1801: 1791: 1786: 1781: 1780: 1779: 1768: 1766: 1762: 1761: 1759: 1758: 1753: 1752: 1751: 1741: 1740: 1739: 1734: 1729: 1719: 1713: 1711: 1705: 1704: 1702: 1701: 1696: 1691: 1686: 1672: 1670: 1668:Disaccharidase 1661: 1651: 1650: 1638: 1637: 1630: 1623: 1615: 1609: 1608: 1603: 1596: 1595:External links 1593: 1591: 1590: 1580: 1516: 1474: 1447:(5): 839–848. 1431: 1382: 1365:Phytochemistry 1351: 1340:(2): 133–140. 1324: 1275: 1236:(23): 8805–9. 1216: 1209: 1191: 1142: 1093: 1042: 1012: 991: 946: 901: 853: 808: 793: 749: 736: 718: 673: 671: 668: 613: 610: 605:Lygus hesperus 517:Fruit ripening 511:middle lamella 487: 484: 465:monosaccharide 444:polysaccharide 431: 428: 419: 339:hydrogen bonds 326: 323: 302: 301: 296: 286: 278: 268: 213: 212: 209: 208: 203: 197: 196: 191: 185: 184: 179: 173: 172: 164: 163: 152: 145: 144: 139: 133: 132: 127: 121: 120: 115: 109: 108: 103: 97: 96: 91: 85: 84: 79: 73: 72: 68: 67: 62: 56: 55: 50: 44: 43: 39: 38: 29: 21: 20: 9: 6: 4: 3: 2: 2328: 2317: 2314: 2313: 2311: 2301: 2296: 2291: 2290: 2287: 2273: 2269: 2268: 2263: 2260: 2256: 2255: 2250: 2247: 2243: 2242: 2237: 2234: 2230: 2229: 2224: 2221: 2217: 2216: 2211: 2208: 2204: 2203: 2198: 2195: 2191: 2190: 2185: 2184: 2182: 2178: 2172: 2169: 2167: 2164: 2162: 2159: 2157: 2154: 2152: 2149: 2148: 2146: 2142: 2136: 2133: 2131: 2130:Enzyme family 2128: 2126: 2123: 2121: 2118: 2117: 2115: 2111: 2105: 2102: 2100: 2097: 2095: 2094:Cooperativity 2092: 2090: 2087: 2086: 2084: 2080: 2074: 2071: 2069: 2066: 2064: 2061: 2059: 2056: 2054: 2053:Oxyanion hole 2051: 2049: 2046: 2044: 2041: 2039: 2036: 2035: 2033: 2029: 2025: 2018: 2013: 2011: 2006: 2004: 1999: 1998: 1995: 1983: 1979: 1976: 1975: 1973: 1969:: Hydrolysing 1968: 1964: 1952: 1949: 1948: 1947: 1944: 1942: 1939: 1937: 1934: 1930: 1927: 1925: 1922: 1921: 1920: 1917: 1915: 1912: 1910: 1907: 1903: 1900: 1899: 1898: 1895: 1893: 1890: 1886: 1885:non-lysosomal 1883: 1881: 1878: 1877: 1876: 1873: 1871: 1868: 1866: 1865:Hyaluronidase 1863: 1859: 1856: 1855: 1854: 1853:Glucuronidase 1851: 1849: 1846: 1842: 1839: 1837: 1834: 1833: 1832: 1829: 1825: 1822: 1820: 1817: 1815: 1812: 1810: 1807: 1805: 1802: 1800: 1797: 1796: 1795: 1794:Neuraminidase 1792: 1790: 1787: 1785: 1782: 1778: 1777:Alpha-amylase 1775: 1774: 1773: 1770: 1769: 1767: 1763: 1757: 1754: 1750: 1747: 1746: 1745: 1742: 1738: 1735: 1733: 1730: 1728: 1725: 1724: 1723: 1720: 1718: 1715: 1714: 1712: 1710: 1706: 1700: 1697: 1695: 1692: 1690: 1687: 1685: 1681: 1677: 1674: 1673: 1671: 1669: 1665: 1662: 1660: 1656: 1652: 1647: 1643: 1636: 1631: 1629: 1624: 1622: 1617: 1616: 1613: 1607: 1604: 1602: 1599: 1598: 1584: 1576: 1572: 1567: 1562: 1557: 1552: 1548: 1544: 1540: 1536: 1532: 1525: 1523: 1521: 1512: 1508: 1504: 1500: 1497:(2): 122–35. 1496: 1492: 1485: 1478: 1470: 1466: 1462: 1458: 1454: 1450: 1446: 1442: 1435: 1427: 1423: 1418: 1413: 1409: 1405: 1401: 1397: 1393: 1386: 1378: 1374: 1370: 1366: 1362: 1355: 1347: 1343: 1339: 1335: 1328: 1320: 1316: 1311: 1306: 1302: 1298: 1295:(2): 337–43. 1294: 1290: 1286: 1279: 1271: 1267: 1262: 1257: 1252: 1247: 1243: 1239: 1235: 1231: 1227: 1220: 1212: 1210:9781429229364 1206: 1202: 1195: 1187: 1183: 1178: 1173: 1169: 1165: 1162:(1): 210–21. 1161: 1157: 1153: 1146: 1138: 1134: 1129: 1124: 1120: 1116: 1113:(2): 384–95. 1112: 1108: 1104: 1097: 1089: 1085: 1080: 1075: 1070: 1065: 1061: 1057: 1053: 1046: 1038: 1034: 1030: 1026: 1025:Plant Science 1019: 1017: 1008: 1004: 998: 996: 987: 983: 978: 973: 969: 965: 961: 959: 950: 942: 938: 933: 928: 924: 920: 916: 914: 905: 897: 893: 888: 883: 879: 875: 868: 866: 857: 849: 845: 840: 835: 831: 827: 823: 821: 812: 802: 800: 798: 789: 785: 781: 777: 774:(2): 237–44. 773: 769: 762: 760: 758: 756: 754: 746: 740: 732: 728: 722: 714: 710: 706: 702: 699:(4): 863–78. 698: 694: 690: 683: 681: 679: 674: 667: 665: 661: 656: 654: 650: 649: 644: 640: 636: 633: 625: 624: 618: 609: 607: 606: 600: 599: 595: 592: 586: 585: 581: 579: 575: 571: 567: 563: 559: 554: 553: 549: 546: 542: 540: 536: 532: 528: 524: 519: 518: 514: 512: 508: 504: 499: 497: 493: 483: 481: 477: 473: 469: 466: 460: 459: 451: 447: 445: 441: 437: 427: 425: 417: 413: 409: 408: 403: 398: 396: 395: 390: 389: 384: 383: 378: 377: 372: 368: 361: 360: 354: 350: 348: 344: 340: 336: 332: 322: 319: 315: 311: 307: 299: 289: 275: 271: 262: 261: 260: 258: 254: 250: 246: 242: 234: 230: 226: 223: 219: 207: 204: 202: 198: 195: 192: 190: 186: 183: 180: 178: 174: 169: 165: 162: 159: 156: 153: 150: 146: 143: 140: 138: 134: 131: 128: 126: 122: 119: 116: 114: 110: 107: 106:NiceZyme view 104: 102: 98: 95: 92: 90: 86: 83: 80: 78: 74: 69: 66: 63: 61: 57: 54: 51: 49: 45: 40: 35: 34: 27: 22: 17: 2267:Translocases 2264: 2251: 2238: 2225: 2212: 2202:Transferases 2199: 2186: 2043:Binding site 1709:Glucosidases 1583: 1538: 1534: 1494: 1490: 1477: 1444: 1440: 1434: 1399: 1395: 1385: 1368: 1364: 1354: 1337: 1333: 1327: 1292: 1288: 1278: 1233: 1229: 1219: 1201:Biochemistry 1200: 1194: 1159: 1155: 1145: 1110: 1106: 1096: 1059: 1055: 1045: 1031:(1): 57–62. 1028: 1024: 1006: 967: 963: 957: 949: 922: 918: 912: 904: 880:(3): 462–6. 877: 874:FEBS Letters 873: 864: 856: 832:(1): 294–9. 829: 825: 819: 811: 771: 767: 744: 739: 730: 721: 696: 692: 688: 663: 659: 657: 646: 641:(PGIPs) are 629: 621: 603: 601: 597: 596: 587: 583: 582: 558:pollen tubes 555: 551: 550: 543: 520: 516: 515: 500: 489: 472:polymorphism 461: 457: 456: 439: 433: 405: 399: 392: 386: 380: 374: 370: 365: 357: 328: 306:carbohydrate 303: 297: 287: 273: 269: 236: 232: 228: 217: 216: 94:BRENDA entry 31: 2038:Active site 1936:Iduronidase 1870:Pullulanase 664:P. vulgaris 660:P. vulgaris 402:active site 347:hydrophobic 281:O = (1,4-α- 82:IntEnz view 42:Identifiers 2241:Isomerases 2215:Hydrolases 2082:Regulation 1946:Heparanase 1914:Fucosidase 1732:Neutral AB 1062:(49): 49. 670:References 612:Inhibition 531:Flavr Savr 521:The first 496:abscission 412:amino acid 318:endogenous 259:residues: 251:the α-1,4 249:hydrolyzes 151:structures 118:KEGG entry 65:9032-75-1 2120:EC number 1880:lysosomal 1784:Chitinase 1749:cytosolic 1737:Neutral C 1717:Cellulase 1694:Trehalase 1684:Invertase 1642:Hydrolase 632:inhibitor 535:antisense 436:pectinase 430:Mechanism 416:substrate 325:Structure 291:+ (1,4-α- 71:Databases 2316:EC 3.2.1 2310:Category 2144:Kinetics 2068:Cofactor 2031:Activity 1789:Lysozyme 1575:12904578 1511:19085947 1469:12409373 1426:16660870 1270:16593997 1186:11351084 1137:20427466 1088:23493833 941:10521427 896:14623112 848:17876815 826:Proteins 788:14871664 731:Lexic.us 713:11518536 635:proteins 422:O for a 331:β sheets 255:between 243:) is an 237:(1→4)-α- 225:3.2.1.15 206:proteins 194:articles 182:articles 155:RCSB PDB 53:3.2.1.15 2300:Biology 2254:Ligases 2024:Enzymes 1772:Amylase 1699:Lactase 1689:Maltase 1676:Sucrase 1543:Bibcode 1461:1281437 1319:9625687 1310:1539180 1238:Bibcode 1128:2879803 1079:3595604 986:9733763 574:citrate 523:GM food 335:β helix 263:(1,4-α- 142:profile 125:MetaCyc 60:CAS no. 2286:Portal 2228:Lyases 1858:Klotho 1573:  1566:187787 1563:  1509:  1467:  1459:  1424:  1417:542983 1414:  1317:  1307:  1268:  1261:282595 1258:  1207:  1184:  1177:102295 1174:  1135:  1125:  1086:  1076:  1007:BRENDA 984:  939:  894:  846:  786:  711:  591:assays 576:, and 552:Pollen 494:, and 492:pollen 379:, and 310:pectin 245:enzyme 231:, and 189:PubMed 171:Search 161:PDBsum 101:ExPASy 89:BRENDA 77:IntEnz 48:EC no. 2180:Types 1967:3.2.2 1951:HPSE2 1836:Alpha 1765:Other 1655:3.2.1 1487:(PDF) 1465:S2CID 870:(PDF) 598:Other 562:maize 480:fungi 247:that 137:PRIAM 2272:list 2265:EC7 2259:list 2252:EC6 2246:list 2239:EC5 2233:list 2226:EC4 2220:list 2213:EC3 2207:list 2200:EC2 2194:list 2187:EC1 1929:HEXB 1924:HEXA 1902:NAGA 1841:Beta 1814:NEU4 1809:NEU3 1804:NEU2 1799:NEU1 1727:Acid 1648:3.2) 1571:PMID 1507:PMID 1457:PMID 1422:PMID 1315:PMID 1266:PMID 1205:ISBN 1182:PMID 1133:PMID 1084:PMID 982:PMID 937:PMID 892:PMID 844:PMID 784:PMID 772:1696 709:PMID 578:EDTA 570:NaCl 400:The 391:and 341:and 201:NCBI 158:PDBe 113:KEGG 1561:PMC 1551:doi 1539:100 1499:doi 1449:doi 1412:PMC 1404:doi 1373:doi 1342:doi 1305:PMC 1297:doi 1293:117 1256:PMC 1246:doi 1172:PMC 1164:doi 1160:126 1123:PMC 1115:doi 1111:153 1074:PMC 1064:doi 1033:doi 972:doi 968:273 927:doi 923:274 882:doi 878:554 834:doi 776:doi 701:doi 697:311 539:RNA 404:of 277:+ H 227:, 177:PMC 149:PDB 2312:: 1980:: 1657:: 1646:EC 1569:. 1559:. 1549:. 1537:. 1533:. 1519:^ 1505:. 1495:70 1493:. 1489:. 1463:. 1455:. 1445:20 1443:. 1420:. 1410:. 1400:63 1398:. 1394:. 1369:30 1367:. 1363:. 1338:85 1336:. 1313:. 1303:. 1291:. 1287:. 1264:. 1254:. 1244:. 1234:85 1232:. 1228:. 1180:. 1170:. 1158:. 1154:. 1131:. 1121:. 1109:. 1105:. 1082:. 1072:. 1058:. 1054:. 1029:59 1027:. 1015:^ 1005:. 994:^ 980:. 966:. 962:. 935:. 921:. 917:. 890:. 876:. 872:. 842:. 830:70 828:. 824:. 796:^ 782:. 770:. 752:^ 729:. 707:. 695:. 677:^ 655:. 580:. 572:, 498:. 482:. 476:pH 426:. 373:, 349:. 222:EC 2288:: 2274:) 2270:( 2261:) 2257:( 2248:) 2244:( 2235:) 2231:( 2222:) 2218:( 2209:) 2205:( 2196:) 2192:( 2016:e 2009:t 2002:v 1682:/ 1678:/ 1634:e 1627:t 1620:v 1577:. 1553:: 1545:: 1513:. 1501:: 1471:. 1451:: 1428:. 1406:: 1379:. 1375:: 1348:. 1344:: 1321:. 1299:: 1272:. 1248:: 1240:: 1213:. 1188:. 1166:: 1139:. 1117:: 1090:. 1066:: 1060:4 1039:. 1035:: 1009:. 988:. 974:: 943:. 929:: 898:. 884:: 867:" 850:. 836:: 790:. 778:: 733:. 715:. 703:: 440:O 420:2 298:m 293:D 288:n 283:D 279:2 274:m 272:+ 270:n 265:D 239:D 220:(

Index


Aspergillus aculeatus
EC no.
3.2.1.15
CAS no.
9032-75-1
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
EC
3.2.1.15

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