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Glycosyltransferase

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563:). Suitable enzymes can be isolated from natural sources or produced recombinantly. As an alternative, whole cell-based systems using either endogenous glycosyl donors or cell-based systems containing cloned and expressed systems for synthesis of glycosyl donors have been developed. In cell-free approaches, the large-scale application of glycosyltransferases for glycoconjugate synthesis has required access to large quantities of the glycosyl donors. On the flip-side, nucleotide recycling systems that allow the resynthesis of glycosyl donors from the released nucleotide have been developed. The nucleotide recycling approach has a further benefit of reducing the amount of nucleotide formed as a by-product, thereby reducing the amount of inhibition caused to the glycosyltransferase of interest – a commonly observed feature of the nucleotide byproduct. 266: 31: 2256: 272:
Glycosyltransferases can be segregated into "retaining" or "inverting" enzymes according to whether the stereochemistry of the donor's anomeric bond is retained (α→α) or inverted (α→β) during the transfer. The inverting mechanism is straightforward, requiring a single nucleophilic attack from the
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Sequence-based classification methods have proven to be a powerful way of generating hypotheses for protein function based on sequence alignment to related proteins. The carbohydrate-active enzyme database presents a sequence-based classification of glycosyltransferases into over 90 families. The
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to D-galactose end of H antigen, producing the A antigen. The B allele encodes 1-3-galactosyltransferase that joins α-D-galactose bonded to D-galactose end of H antigen, creating the B antigen. In case of O allele the exon 6 contains a deletion that results in a loss of enzymatic activity. The O
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The retaining mechanism has been a matter of debate, but there exists strong evidence against a double displacement mechanism (which would cause two inversions about the anomeric carbon for a net retention of stereochemistry) or a dissociative mechanism (a prevalent variant of which was known as
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Kocev, A; Melamed, J; Wang, S; Kong, X; Vlahakis, JZ; Xu, Y; Szarek, WA; Brockhausen, I (June 2020). "Inhibition of bacterial growth and galactosyltransferase activity of WbwC by α, ω-bis(3-alkyl-1H-imidazolium)alkane salts: Effect of varying carbon content".
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SNi). An "orthogonal associative" mechanism has been proposed which, akin to the inverting enzymes, requires only a single nucleophilic attack from an acceptor from a non-linear angle (as observed in many crystal structures) to achieve anomer retention.
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database, only three different folds have been observed for glycosyltransferases Very recently, a new glycosyltransferase fold was identified for the glycosyltransferases involved in the biosynthesis of the NAG-NAM polymer backbone of
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The recent discovery of the reversibility of many reactions catalyzed by inverting glycosyltransferases served as a paradigm shift in the field and raises questions regarding the designation of sugar nucleotides as 'activated' donors.
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Glycosyltransferases have been widely used in both the targeted synthesis of specific glycoconjugates as well as the synthesis of differentially glycosylated libraries of drugs, biological probes or natural products in the context of
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Zhang, C; Albermann, C; Fu, X; Thorson, JS (27 December 2006). "The in vitro characterization of the iterative avermectin glycosyltransferase AveBI reveals reaction reversibility and sugar nucleotide flexibility".
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Zhang, C; Fu, Q; Albermann, C; Li, L; Thorson, JS (5 March 2007). "The in vitro characterization of the erythronolide mycarosyltransferase EryBV and its utility in macrolide diversification".
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Zhang, C; Griffith, BR; Fu, Q; Albermann, C; Fu, X; Lee, IK; Li, L; Thorson, JS (1 September 2006). "Exploiting the reversibility of natural product glycosyltransferase-catalyzed reactions".
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and results in translation of an almost entirely different protein that lacks enzymatic activity. This results in H antigen remaining unchanged in case of O groups.
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Lovering AL, de Castro LH, Lim D, Strynadka NC (March 2007). "Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis".
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expressing the glycosyltransferases has three main allelic forms: A, B, and O. The A allele encodes 1-3-N-acetylgalactosaminyltransferase that bonds α-
1577: 1572: 247:. The phosphate(s) of these donor molecules are usually coordinated by divalent cations such as manganese, however metal independent enzymes exist. 1220:
Gantt, RW; Peltier-Pain, P; Thorson, JS (October 2011). "Enzymatic methods for glyco(diversification/randomization) of drugs and small molecules".
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The combination of glycosyltransferases by both alleles present in each person determines whether there is an AB, A, B or O blood type.
1265: 1975: 1818: 643: 251: 340:. Some glycosyltransferase inhibitors are of use as drugs or antibiotics. Moenomycin is used in animal feed as a growth promoter. 1828: 2281: 1849: 1833: 2131: 497: 1258: 2246: 1368: 356:-based synthetic inhibitors of glycosyltransferases have been designed for use as antimicrobial and antiseptic agents. 1353: 1793: 2116: 2232: 2219: 2206: 2193: 2180: 2167: 2154: 1918: 1810: 1723: 1358: 1298: 1006: 607: 2126: 2080: 2023: 1363: 1336: 1289: 190: 54: 485: 337: 2028: 1853: 1416: 582: 159: 2276: 1331: 577: 572: 516: 175: 2311: 2286: 2049: 1968: 1897: 1383: 1373: 527: 2121: 626:
Williams, GJ; Thorson, JS (2009). "Natural Product Glycosyltransferases: Properties and Applications".
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for his work on carbohydrate metabolism. Glycosyltransferases that use non-nucleotide donors such as
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is an inhibitor of mycobacterial arabinotransferases and is used for the treatment of tuberculosis.
2085: 1727: 1642: 1540: 1313: 695: 433: 304: 232: 123: 1082:"Glycosyltransferase structural biology and its role in the design of catalysts for glycosylation" 630:. Advances in Enzymology - and Related Areas of Molecular Biology. Vol. 76. pp. 55–119. 265: 2018: 1880: 1564: 1302: 1173: 879: 800: 560: 69: 240: 228: 224: 324:
Many inhibitors of glycosyltransferases are known. Some of these are natural products, such as
2301: 2296: 1922: 1348: 1250: 1237: 1165: 1111: 1062: 977: 928: 871: 836: 792: 749: 672: 649: 639: 592: 587: 472: 84: 1200: 710:"Geometric Attributes of Retaining Glycosyltransferase Enzymes Favor an Orthogonal Mechanism" 2064: 2059: 2033: 1961: 1760: 1747: 1391: 1341: 1229: 1157: 1101: 1093: 1052: 1044: 967: 959: 918: 910: 863: 828: 784: 739: 729: 631: 556: 523: 73: 1632: 1627: 464: 30: 2291: 2111: 2095: 2008: 1779: 994: 255: 115: 58: 307:, glycosyltransferase have a much smaller range of structures. In fact, according to the 1153: 948:"Using simple donors to drive the equilibria of glycosyltransferase-catalyzed reactions" 780: 725: 2260: 2149: 2090: 1106: 1081: 1057: 1032: 972: 947: 923: 898: 744: 709: 597: 552: 414: 186: 119: 77: 2270: 2054: 2013: 1784: 1321: 602: 333: 313: 216: 201: 1177: 883: 804: 390: 352:
is an inhibitor of insect chitin syntheses and is used to control fleas in animals.
189:, the scientist who discovered the first sugar nucleotide and who received the 1970 2003: 460: 147: 107: 81: 426: 1097: 734: 402: 2227: 2162: 1998: 1281: 899:"The in vitro characterization of polyene glycosyltransferases AmphDI and NysDI" 344:
has been developed from the echinocandins and is in use as an antifungal agent.
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allele differs slightly from the A allele by deletion of a single nucleotide -
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is determined by what type of glycosyltransferases are expressed in the body.
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same three-dimensional fold is expected to occur within each of the families.
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Etzler ME, Varki A, Cummings RL, Esko JD, Freeze HH, Hart GW, eds. (2008).
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Gantt, RW; Peltier-Pain, P; Cournoyer, WJ; Thorson, JS (21 August 2011).
397: 194: 171: 135: 96: 62: 162:, which is relatively abundant in eukaryotes. Transferases may also use 1942: 1800: 1533: 1528: 1523: 1518: 1513: 1481: 1405: 1233: 1048: 532: 131: 1010: 832: 154:
to give N-linked glycoproteins. Mannosyl groups may be transferred to
2214: 1984: 1738: 1508: 1503: 1498: 1493: 1488: 1476: 1471: 1466: 1461: 1456: 1451: 1446: 1434: 1429: 1424: 671:(2nd ed.). Plainview, N.Y: Cold Spring Harbor Laboratory Press. 492: 211:
Mammals use only 9 sugar nucleotide donors for glycosyltransferases:
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Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B
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Glycoprotein-fucosylgalactoside a-N-acetylgalactosaminyltransferase
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Chang, A; Singh, S; Phillips GN, Jr; Thorson, JS (December 2011).
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Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase
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B-N-acetylglucosaminyl-glycopeptide b-1,4-galactosyltransferase
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Zhang, C; Moretti, R; Jiang, J; Thorson, JS (13 October 2008).
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In contrast to the diversity of 3D structures observed for
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Glycosyltransferases that use sugar nucleotide donors are
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Singh, S; Phillips GN, Jr; Thorson, JS (October 2012).
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Dolichyl-phosphate-mannose-protein mannosyltransferase
2244: 2140: 2104: 2073: 2042: 1991: 1917: 1873: 1842: 1809: 1746: 1737: 1722: 1641: 1563: 1415: 1382: 1312: 1297: 491: 471: 453: 448: 432: 420: 408: 396: 384: 376: 371: 366: 122:. Some glycosyltransferases catalyse transfer to 254:, and they are usually anchored to membranes of 1824:Hypoxanthine-guanine phosphoribosyltransferase 1969: 1266: 708:Schuman B, Evans SV, Fyles TM (August 2013). 8: 1933:Beta-galactoside alpha-2,6-sialyltransferase 1903:Indolylacetylinositol arabinosyltransferase 1129:SCOP: Structural Classification of Proteins 1976: 1962: 1954: 1743: 1734: 1309: 1273: 1259: 1251: 445: 273:accepting atom to invert stereochemistry. 87:molecule, the nucleophile of which can be 1105: 1056: 971: 922: 743: 733: 332:, inhibitors of chitin synthase, and the 106:The result of glycosyl transfer can be a 821:Journal of the American Chemical Society 2251: 618: 535:at position 261. The deletion causes a 1938:Monosialoganglioside sialyltransferase 1775:NAD(P):arginine ADP-ribosyltransferase 1756:NAD:diphthamide ADP-ribosyltransferase 363: 174:phosphates in eukaryotic organism, or 130:. Glycosyl transfer can also occur to 309:Structural Classification of Proteins 7: 1193:Bioorganic and Medicinal Chemistry 252:single-pass transmembrane proteins 25: 1819:Adenine phosphoribosyltransferase 2254: 1829:Uracil phosphoribosyltransferase 1086:Current Opinion in Biotechnology 1850:Purine nucleoside phosphorylase 206:non-Leloir glycosyltransferases 1834:Amidophosphoribosyltransferase 995:CAZypedia Glycosyltransferases 250:Many glycosyltransferases are 1: 1201:doi:10.1016/j.bmc.2020.115494 449:Available protein structures: 2307:Peripheral membrane proteins 1369:Ceramide glucosyltransferase 1098:10.1016/j.copbio.2011.04.013 735:10.1371/journal.pone.0071077 367:Glycosyltransferase family 6 1007:"CAZy Glycosyl Transferase" 2328: 1794:Poly ADP ribose polymerase 669:Essentials of Glycobiology 508: 290:Classification by sequence 2132:Michaelis–Menten kinetics 1811:Phosphoribosyltransferase 636:10.1002/9780470392881.ch2 608:Oligosaccharyltransferase 444: 360:Determinant of blood type 57:) that establish natural 2024:Diffusion-limited enzyme 1364:1,3-Beta-glucan synthase 191:Nobel Prize in Chemistry 166:as an acceptor, forming 1854:Thymidine phosphorylase 1222:Natural Product Reports 1162:10.1126/science.1136611 1037:Natural Product Reports 952:Nature Chemical Biology 789:10.1126/science.1130028 583:Glucuronosyltransferase 336:, inhibitors of fungal 2282:Carbohydrate chemistry 1748:ADP-ribosyltransferase 915:10.1002/cbic.200800349 868:10.1002/cbic.200600509 628:Advances in Enzymology 578:Chemical glycosylation 573:Carbohydrate chemistry 517:ABO blood group system 338:β-1,3-glucan synthases 281:Reaction reversibility 269: 176:undecaprenyl phosphate 35: 2117:Eadie–Hofstee diagram 2050:Allosteric regulation 1898:Arabinosyltransferase 1374:N-glycosyltransferase 528:N-acetylgalactosamine 268: 160:C-mannosyl tryptophan 134:residues, usually to 33: 2127:Lineweaver–Burk plot 1766:Pseudomonas exotoxin 1286:glycosyltransferases 964:10.1038/nchembio.638 559:(a process known as 305:glycoside hydrolases 76:(also known as the " 39:Glycosyltransferases 1541:Hyaluronan synthase 1154:2007Sci...315.1402L 781:2006Sci...313.1291Z 726:2013PLoSO...871077S 696:Membranome database 233:UDP-glucuronic acid 124:inorganic phosphate 59:glycosidic linkages 2086:Enzyme superfamily 2019:Enzyme promiscuity 1881:Xylosyltransferase 1354:Debranching enzyme 1234:10.1039/c1np00045d 1049:10.1039/c2np20039b 561:glycorandomization 270: 72:from an activated 36: 2242: 2241: 1951: 1950: 1913: 1912: 1869: 1868: 1718: 1717: 1349:Glycogen synthase 833:10.1021/ja065950k 678:978-0-87969-770-9 593:Glycosyl acceptor 588:Glycogen synthase 507: 506: 503: 502: 498:structure summary 146:to give O-linked 85:glycosyl acceptor 16:(Redirected from 2319: 2259: 2258: 2250: 2122:Hanes–Woolf plot 2065:Enzyme activator 2060:Enzyme inhibitor 2034:Enzyme catalysis 1978: 1971: 1964: 1955: 1761:Diphtheria toxin 1744: 1735: 1392:Lactose synthase 1359:Branching enzyme 1310: 1275: 1268: 1261: 1252: 1246: 1245: 1217: 1211: 1188: 1182: 1181: 1148:(5817): 1402–5. 1137: 1131: 1126: 1120: 1119: 1109: 1077: 1071: 1070: 1060: 1028: 1022: 1021: 1019: 1018: 1009:. Archived from 1003: 997: 992: 986: 985: 975: 943: 937: 936: 926: 894: 888: 887: 851: 845: 844: 815: 809: 808: 775:(5791): 1291–4. 764: 758: 757: 747: 737: 705: 699: 689: 683: 682: 664: 658: 657: 623: 557:drug development 446: 364: 74:nucleotide sugar 65:the transfer of 27:Class of enzymes 21: 18:Transglycosylase 2327: 2326: 2322: 2321: 2320: 2318: 2317: 2316: 2267: 2266: 2265: 2253: 2245: 2243: 2238: 2150:Oxidoreductases 2136: 2112:Enzyme kinetics 2100: 2096:List of enzymes 2069: 2038: 2009:Catalytic triad 1987: 1982: 1952: 1947: 1924: 1909: 1865: 1838: 1805: 1780:Pertussis toxin 1729: 1714: 1637: 1559: 1411: 1378: 1304: 1293: 1279: 1249: 1228:(11): 1811–53. 1219: 1218: 1214: 1189: 1185: 1139: 1138: 1134: 1127: 1123: 1079: 1078: 1074: 1043:(10): 1201–37. 1030: 1029: 1025: 1016: 1014: 1005: 1004: 1000: 993: 989: 945: 944: 940: 909:(15): 2506–14. 896: 895: 891: 853: 852: 848: 827:(51): 16420–1. 817: 816: 812: 766: 765: 761: 707: 706: 702: 690: 686: 679: 666: 665: 661: 646: 625: 624: 620: 616: 569: 548: 513: 410:OPM superfamily 362: 322: 301: 292: 283: 263: 256:Golgi apparatus 245:CMP-sialic acid 116:oligosaccharide 28: 23: 22: 15: 12: 11: 5: 2325: 2323: 2315: 2314: 2309: 2304: 2299: 2294: 2289: 2284: 2279: 2269: 2268: 2264: 2263: 2240: 2239: 2237: 2236: 2223: 2210: 2197: 2184: 2171: 2158: 2144: 2142: 2138: 2137: 2135: 2134: 2129: 2124: 2119: 2114: 2108: 2106: 2102: 2101: 2099: 2098: 2093: 2088: 2083: 2077: 2075: 2074:Classification 2071: 2070: 2068: 2067: 2062: 2057: 2052: 2046: 2044: 2040: 2039: 2037: 2036: 2031: 2026: 2021: 2016: 2011: 2006: 2001: 1995: 1993: 1989: 1988: 1983: 1981: 1980: 1973: 1966: 1958: 1949: 1948: 1946: 1945: 1940: 1935: 1929: 1927: 1915: 1914: 1911: 1910: 1908: 1907: 1906: 1905: 1895: 1894: 1893: 1888: 1877: 1875: 1871: 1870: 1867: 1866: 1864: 1863: 1862: 1861: 1846: 1844: 1840: 1839: 1837: 1836: 1831: 1826: 1821: 1815: 1813: 1807: 1806: 1804: 1803: 1797: 1796: 1790: 1789: 1788: 1787: 1782: 1771: 1770: 1769: 1768: 1763: 1752: 1750: 1741: 1732: 1720: 1719: 1716: 1715: 1713: 1712: 1707: 1702: 1697: 1692: 1687: 1682: 1676: 1675: 1670: 1665: 1664: 1663: 1658: 1647: 1645: 1639: 1638: 1636: 1635: 1630: 1625: 1620: 1615: 1610: 1605: 1600: 1595: 1590: 1585: 1580: 1575: 1569: 1567: 1561: 1560: 1558: 1557: 1552: 1547: 1537: 1536: 1531: 1526: 1521: 1516: 1511: 1506: 1501: 1496: 1491: 1485: 1484: 1479: 1474: 1469: 1464: 1459: 1454: 1449: 1444: 1438: 1437: 1432: 1427: 1421: 1419: 1413: 1412: 1410: 1409: 1399: 1394: 1388: 1386: 1380: 1379: 1377: 1376: 1371: 1366: 1361: 1356: 1351: 1346: 1345: 1344: 1339: 1334: 1329: 1318: 1316: 1307: 1295: 1294: 1280: 1278: 1277: 1270: 1263: 1255: 1248: 1247: 1212: 1199:(11): 115494. 1183: 1132: 1121: 1072: 1023: 998: 987: 958:(10): 685–91. 938: 889: 846: 810: 759: 700: 684: 677: 659: 644: 617: 615: 612: 611: 610: 605: 600: 598:Glycosyl donor 595: 590: 585: 580: 575: 568: 565: 553:drug discovery 547: 544: 509:Main article: 505: 504: 501: 500: 495: 489: 488: 475: 469: 468: 458: 451: 450: 442: 441: 436: 430: 429: 424: 418: 417: 412: 406: 405: 400: 394: 393: 388: 382: 381: 378: 374: 373: 369: 368: 361: 358: 321: 318: 300: 297: 291: 288: 282: 279: 262: 259: 187:Luis F. Leloir 183:Leloir enzymes 120:polysaccharide 78:glycosyl donor 26: 24: 14: 13: 10: 9: 6: 4: 3: 2: 2324: 2313: 2310: 2308: 2305: 2303: 2300: 2298: 2295: 2293: 2290: 2288: 2285: 2283: 2280: 2278: 2277:Carbohydrates 2275: 2274: 2272: 2262: 2257: 2252: 2248: 2234: 2230: 2229: 2224: 2221: 2217: 2216: 2211: 2208: 2204: 2203: 2198: 2195: 2191: 2190: 2185: 2182: 2178: 2177: 2172: 2169: 2165: 2164: 2159: 2156: 2152: 2151: 2146: 2145: 2143: 2139: 2133: 2130: 2128: 2125: 2123: 2120: 2118: 2115: 2113: 2110: 2109: 2107: 2103: 2097: 2094: 2092: 2091:Enzyme family 2089: 2087: 2084: 2082: 2079: 2078: 2076: 2072: 2066: 2063: 2061: 2058: 2056: 2055:Cooperativity 2053: 2051: 2048: 2047: 2045: 2041: 2035: 2032: 2030: 2027: 2025: 2022: 2020: 2017: 2015: 2014:Oxyanion hole 2012: 2010: 2007: 2005: 2002: 2000: 1997: 1996: 1994: 1990: 1986: 1979: 1974: 1972: 1967: 1965: 1960: 1959: 1956: 1944: 1941: 1939: 1936: 1934: 1931: 1930: 1928: 1926: 1920: 1916: 1904: 1901: 1900: 1899: 1896: 1892: 1889: 1887: 1884: 1883: 1882: 1879: 1878: 1876: 1872: 1860: 1857: 1856: 1855: 1851: 1848: 1847: 1845: 1841: 1835: 1832: 1830: 1827: 1825: 1822: 1820: 1817: 1816: 1814: 1812: 1808: 1802: 1799: 1798: 1795: 1792: 1791: 1786: 1785:Cholera toxin 1783: 1781: 1778: 1777: 1776: 1773: 1772: 1767: 1764: 1762: 1759: 1758: 1757: 1754: 1753: 1751: 1749: 1745: 1742: 1740: 1736: 1733: 1731: 1725: 1721: 1711: 1708: 1706: 1703: 1701: 1698: 1696: 1693: 1691: 1688: 1686: 1683: 1681: 1678: 1677: 1674: 1671: 1669: 1666: 1662: 1659: 1657: 1654: 1653: 1652: 1649: 1648: 1646: 1644: 1640: 1634: 1631: 1629: 1626: 1624: 1621: 1619: 1616: 1614: 1611: 1609: 1606: 1604: 1601: 1599: 1596: 1594: 1591: 1589: 1586: 1584: 1581: 1579: 1576: 1574: 1571: 1570: 1568: 1566: 1562: 1556: 1553: 1551: 1548: 1546: 1542: 1539: 1538: 1535: 1532: 1530: 1527: 1525: 1522: 1520: 1517: 1515: 1512: 1510: 1507: 1505: 1502: 1500: 1497: 1495: 1492: 1490: 1487: 1486: 1483: 1480: 1478: 1475: 1473: 1470: 1468: 1465: 1463: 1460: 1458: 1455: 1453: 1450: 1448: 1445: 1443: 1440: 1439: 1436: 1433: 1431: 1428: 1426: 1423: 1422: 1420: 1418: 1417:Glucuronosyl- 1414: 1407: 1403: 1400: 1398: 1395: 1393: 1390: 1389: 1387: 1385: 1381: 1375: 1372: 1370: 1367: 1365: 1362: 1360: 1357: 1355: 1352: 1350: 1347: 1343: 1340: 1338: 1335: 1333: 1330: 1328: 1325: 1324: 1323: 1322:Phosphorylase 1320: 1319: 1317: 1315: 1311: 1308: 1306: 1300: 1296: 1291: 1287: 1283: 1276: 1271: 1269: 1264: 1262: 1257: 1256: 1253: 1243: 1239: 1235: 1231: 1227: 1223: 1216: 1213: 1209: 1206: 1202: 1198: 1194: 1187: 1184: 1179: 1175: 1171: 1167: 1163: 1159: 1155: 1151: 1147: 1143: 1136: 1133: 1130: 1125: 1122: 1117: 1113: 1108: 1103: 1099: 1095: 1091: 1087: 1083: 1076: 1073: 1068: 1064: 1059: 1054: 1050: 1046: 1042: 1038: 1034: 1027: 1024: 1013:on 2009-03-23 1012: 1008: 1002: 999: 996: 991: 988: 983: 979: 974: 969: 965: 961: 957: 953: 949: 942: 939: 934: 930: 925: 920: 916: 912: 908: 904: 900: 893: 890: 885: 881: 877: 873: 869: 865: 862:(4): 385–90. 861: 857: 850: 847: 842: 838: 834: 830: 826: 822: 814: 811: 806: 802: 798: 794: 790: 786: 782: 778: 774: 770: 763: 760: 755: 751: 746: 741: 736: 731: 727: 723: 720:(8): e71077. 719: 715: 711: 704: 701: 697: 693: 688: 685: 680: 674: 670: 663: 660: 655: 651: 647: 645:9780470392881 641: 637: 633: 629: 622: 619: 613: 609: 606: 604: 603:Glycosylation 601: 599: 596: 594: 591: 589: 586: 584: 581: 579: 576: 574: 571: 570: 566: 564: 562: 558: 554: 545: 543: 540: 538: 534: 529: 525: 520: 518: 512: 499: 496: 494: 490: 487: 483: 479: 476: 474: 470: 466: 462: 459: 456: 452: 447: 443: 440: 437: 435: 431: 428: 425: 423: 419: 416: 413: 411: 407: 404: 401: 399: 395: 392: 389: 387: 383: 379: 375: 370: 365: 359: 357: 355: 351: 347: 343: 339: 335: 334:echinocandins 331: 327: 319: 317: 315: 314:peptidoglycan 310: 306: 298: 296: 289: 287: 280: 278: 274: 267: 260: 258: 257: 253: 248: 246: 242: 238: 234: 230: 226: 222: 218: 217:UDP-galactose 214: 209: 207: 203: 202:pyrophosphate 200: 196: 192: 188: 184: 179: 178:in bacteria. 177: 173: 169: 165: 161: 157: 153: 149: 148:glycoproteins 145: 141: 137: 133: 129: 125: 121: 117: 113: 109: 104: 102: 98: 94: 90: 86: 83: 79: 75: 71: 68: 64: 60: 56: 52: 48: 44: 40: 32: 19: 2312:Glycobiology 2287:Transferases 2228:Translocases 2225: 2212: 2199: 2186: 2173: 2163:Transferases 2160: 2147: 2004:Binding site 1925:transferases 1730:transferases 1305:transferases 1285: 1282:Transferases 1225: 1221: 1215: 1196: 1192: 1186: 1145: 1141: 1135: 1124: 1092:(6): 800–8. 1089: 1085: 1075: 1040: 1036: 1026: 1015:. Retrieved 1011:the original 1001: 990: 955: 951: 941: 906: 902: 892: 859: 855: 849: 824: 820: 813: 772: 768: 762: 717: 713: 703: 692:Transferases 687: 668: 662: 627: 621: 549: 541: 521: 514: 323: 302: 293: 284: 275: 271: 249: 210: 205: 182: 180: 158:to generate 108:carbohydrate 105: 82:nucleophilic 46: 42: 38: 37: 1999:Active site 1384:Galactosyl- 903:ChemBioChem 856:ChemBioChem 422:OPM protein 372:Identifiers 354:Imidazolium 342:Caspofungin 330:nikkomycins 237:GDP-mannose 213:UDP-glucose 168:glycolipids 2271:Categories 2202:Isomerases 2176:Hydrolases 2043:Regulation 1337:Cellobiose 1017:2009-08-25 614:References 537:frameshift 524:gene locus 461:structures 434:Membranome 346:Ethambutol 326:moenomycin 320:Inhibitors 241:GDP-fucose 229:UDP-xylose 225:UDP-GalNAc 221:UDP-GlcNAc 199:polyprenol 156:tryptophan 152:asparagine 67:saccharide 2081:EC number 1728:Pentosyl- 1643:Mannosyl- 1314:Glucosyl- 403:IPR005076 350:Lufenuron 299:Structure 261:Mechanism 144:threonine 112:glycoside 2302:EC 2.4.2 2297:EC 2.4.1 2105:Kinetics 2029:Cofactor 1992:Activity 1565:Fucosyl- 1332:Glycogen 1303:Hexosyl- 1242:21901218 1208:32312486 1178:41658295 1170:17347437 1116:21592771 1067:22688446 982:21857660 933:18798210 884:45058028 876:17262863 841:17177349 805:38072017 797:16946071 754:23936487 714:PLOS ONE 654:18990828 567:See also 522:The ABO 478:RCSB PDB 398:InterPro 195:dolichol 185:, after 172:dolichol 150:, or to 136:tyrosine 103:-based. 97:nitrogen 80:") to a 70:moieties 63:catalyze 2261:Biology 2215:Ligases 1985:Enzymes 1943:ST8SIA4 1801:Sirtuin 1534:UGT2B28 1529:UGT2B17 1524:UGT2B15 1519:UGT2B11 1514:UGT2B10 1482:UGT1A10 1406:C1GALT1 1150:Bibcode 1142:Science 1107:3163058 1058:3627186 973:3177962 924:2947747 777:Bibcode 769:Science 745:3731257 722:Bibcode 533:Guanine 391:PF03414 132:protein 118:, or a 61:. They 51:enzymes 2292:EC 2.4 2247:Portal 2189:Lyases 1923:Sialyl 1919:2.4.99 1739:Ribose 1578:POFUT2 1573:POFUT1 1509:UGT2B7 1504:UGT2B4 1499:UGT2A3 1494:UGT2A2 1489:UGT2A1 1477:UGT1A9 1472:UGT1A8 1467:UGT1A7 1462:UGT1A6 1457:UGT1A5 1452:UGT1A4 1447:UGT1A3 1442:UGT1A1 1435:B3GAT3 1430:B3GAT2 1425:B3GAT1 1327:Starch 1240:  1176:  1168:  1114:  1104:  1065:  1055:  980:  970:  931:  921:  882:  874:  839:  803:  795:  752:  742:  675:  652:  642:  493:PDBsum 467:  457:  377:Symbol 243:, and 164:lipids 140:serine 101:sulfur 99:-, or 93:carbon 89:oxygen 55:EC 2.4 49:) are 2141:Types 1891:XYLT2 1886:XYLT1 1874:Other 1859:ECGF1 1843:Other 1724:2.4.2 1710:ALG12 1661:POMT2 1656:POMT1 1633:FUT11 1628:FUT10 1299:2.4.1 1174:S2CID 880:S2CID 801:S2CID 142:, or 128:water 2233:list 2226:EC7 2220:list 2213:EC6 2207:list 2200:EC5 2194:list 2187:EC4 2181:list 2174:EC3 2168:list 2161:EC2 2155:list 2148:EC1 1705:ALG9 1700:ALG8 1695:ALG6 1690:ALG3 1685:ALG2 1680:ALG1 1673:DPM3 1668:DPM1 1623:FUT9 1618:FUT8 1613:FUT7 1608:FUT6 1603:FUT5 1598:FUT4 1593:FUT3 1588:FUT2 1583:FUT1 1555:HAS3 1550:HAS2 1545:HAS1 1342:Myo- 1292:2.4) 1238:PMID 1205:PMID 1166:PMID 1112:PMID 1063:PMID 978:PMID 929:PMID 872:PMID 837:PMID 793:PMID 750:PMID 673:ISBN 650:PMID 640:ISBN 555:and 546:Uses 515:The 486:PDBj 482:PDBe 465:ECOD 455:Pfam 427:2rj6 386:Pfam 204:are 47:Gtfs 43:GTFs 1230:doi 1158:doi 1146:315 1102:PMC 1094:doi 1053:PMC 1045:doi 968:PMC 960:doi 919:PMC 911:doi 864:doi 829:doi 825:128 785:doi 773:313 740:PMC 730:doi 694:in 632:doi 473:PDB 439:468 415:199 380:GT6 197:or 126:or 95:-, 2273:: 1921:: 1852:: 1726:: 1543:: 1301:: 1290:EC 1284:: 1236:. 1226:28 1224:. 1203:. 1197:28 1195:. 1172:. 1164:. 1156:. 1144:. 1110:. 1100:. 1090:22 1088:. 1084:. 1061:. 1051:. 1041:29 1039:. 1035:. 976:. 966:. 954:. 950:. 927:. 917:. 905:. 901:. 878:. 870:. 858:. 835:. 823:. 799:. 791:. 783:. 771:. 748:. 738:. 728:. 716:. 712:. 648:. 638:. 484:; 480:; 463:/ 316:. 239:, 235:, 231:, 227:, 223:, 219:, 215:, 208:. 138:, 114:, 110:, 91:- 45:, 2249:: 2235:) 2231:( 2222:) 2218:( 2209:) 2205:( 2196:) 2192:( 2183:) 2179:( 2170:) 2166:( 2157:) 2153:( 1977:e 1970:t 1963:v 1408:) 1404:( 1288:( 1274:e 1267:t 1260:v 1244:. 1232:: 1210:. 1180:. 1160:: 1152:: 1118:. 1096:: 1069:. 1047:: 1020:. 984:. 962:: 956:7 935:. 913:: 907:9 886:. 866:: 860:8 843:. 831:: 807:. 787:: 779:: 756:. 732:: 724:: 718:8 698:. 681:. 656:. 634:: 53:( 41:( 20:)

Index

Transglycosylase

enzymes
EC 2.4
glycosidic linkages
catalyze
saccharide
moieties
nucleotide sugar
glycosyl donor
nucleophilic
glycosyl acceptor
oxygen
carbon
nitrogen
sulfur
carbohydrate
glycoside
oligosaccharide
polysaccharide
inorganic phosphate
water
protein
tyrosine
serine
threonine
glycoproteins
asparagine
tryptophan
C-mannosyl tryptophan

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