1499:
372:
It deglycosylates mannose glycoproteins, but the extent and rate of the deglycosylation depends to a high degree on the nature of the glycoproteins. The deglycosylation rate can be increased by denaturation of the glycoproteins (e.g., by carboxymethylation, sulfitolysis or by heating in the presence
373:
of sodium dodecyl sulfate). The addition of 0.1 M 2-mercaptoethanol highly increases enzyme activity against glycoproteins containing inter- or intra-molecular disulfide bridges, unlike detergents like Triton X-100, n- Octylglucoside, or zwitterionic detergents.
421:
subunits. Since all later oligosaccharide structures are resistant to cleavage by endoglycosidase H the enzyme is widely used to report the extent of oligosaccharide processing a protein of interest has undergone.
809:
614:
Tai T, Yamashita K, Ogata-Arakawa M, Koide N, Muramatsu T, Iwashita S, Inoue Y, Kobata A (November 1975). "Structural studies of two ovalbumin glycopeptides in relation to the endo-β-
241:
260:
836:
409:. It is this oligosaccharide molecule which is modified by a series of enzymes as the protein moves through the different compartments of the
774:
676:
Robbins PW, Trimble RB, Wirth DF, Hering C, Maley F, Maley GF, Das R, Gibson BW, Royal N, Biemann K (June 1984). "Primary structure of the
1218:
645:
Tarentino AL, Plummer TH, Maley F (February 1974). "The release of intact oligosaccharides from specific glycoproteins by endo-β-
253:
1100:
829:
382:
220:
196:
1374:
1112:
473:-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from
413:. Endoglycosidase H is able to cleave each structure of this oligosaccharide as it is processed until the enzyme Golgi
959:
1489:
406:
1359:
1475:
1462:
1449:
1436:
1423:
1410:
1397:
1170:
858:
822:
1369:
214:
1323:
1266:
849:
286:
33:
401:(ER) and translocated into the Golgi. Upon entering the ER a molecule containing 14 sugar subunits is linked
365:(GlcNAc) subunits directly proximal to the asparagine residue, generating a truncated sugar molecule with one
201:
1271:
1022:
1185:
930:
390:
265:
1292:
1211:
398:
341:
189:
1364:
50:
1144:
1095:
414:
358:
Endoglycosidase H cleaves the bond in the diacetylchitobiose core of the oligosaccharide between two
347:
121:
glycopeptide-D-mannosyl-4-N-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase
1328:
1039:
1027:
862:
359:
324:
217:
45:
141:
1261:
1083:
1078:
1056:
1044:
883:
323:. It is used for research purposes to deglycosylate glycoproteins and to monitor intracellular
1519:
1051:
925:
770:
747:
693:
658:
627:
596:
539:
486:
328:
208:
1307:
1302:
1276:
1204:
1061:
947:
739:
586:
578:
529:
521:
451:
316:
177:
1354:
1338:
1251:
1181:
803:
792:
410:
386:
308:
293:
153:
289:
38:
1503:
1392:
1333:
1122:
1034:
871:
814:
591:
558:
534:
505:
352:
236:
1513:
1297:
1256:
1068:
997:
980:
743:
710:
455:
320:
1246:
912:
1470:
1405:
1241:
1139:
1105:
1073:
1498:
1149:
1117:
312:
1444:
1418:
987:
920:
897:
887:
845:
394:
751:
697:
662:
600:
490:
355:
is 29 kDa. The primary structure was described by
Robbins et al. in 1984.
992:
543:
165:
975:
902:
892:
879:
418:
184:
631:
582:
525:
1457:
1227:
248:
160:
148:
136:
1431:
1154:
935:
381:
Endoglycosidase H is commonly used by cell biologists to monitor
1132:
1127:
1088:
1017:
1012:
1007:
1002:
952:
940:
722:
Trimble RB, Maley F (September 1984). "Optimizing hydrolysis of
172:
1200:
818:
305:-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase
510:-acetyl-β-D-glucosaminidase activity in rat liver and kidney"
89:
mannosyl-glycoprotein 1,4-N-acetamidodeoxy-β-D-glycohydrolase
812:(Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine_amidase)
1196:
319:, but not highly processed complex oligosaccharides from
369:-acetylglucosamine residue remaining on the asparagine.
563:-acetyl-β-D-glucosaminidase activity towards an asialo-
1487:
405:
to an asparagine in a selective manner by the enzyme
1383:
1347:
1316:
1285:
1234:
1169:
968:
911:
870:
857:
389:. Most proteins destined for the cell surface are
259:
247:
235:
230:
207:
195:
183:
171:
159:
147:
135:
130:
56:
44:
32:
27:
18:
73:mannosyl-glycoprotein endo-β-N-acetylglucosamidase
567:-acetyl-lactosaminic-type substrate in rat liver"
559:"Demonstration and cytosolic location of an endo-
726:-linked high-mannose oligosaccharides by endo-β-
438:Chien S, Weinburg R, Li S, Li Y (1977). "Endo-β-
77:di-N-acetylchitobiosyl β-N-acetylglucosaminidase
557:Pierce RJ, Spik G, Montreuil J (January 1980).
69:-diacetylchitobiosyl β-N-acetylglucosaminidase
1212:
830:
8:
504:Pierce RJ, Spik G, Montreuil J (June 1979).
469:Koide N, Muramatsu T (August 1974). "Endo-β-
1219:
1205:
1197:
867:
837:
823:
815:
283:-acetylglucosaminidase (endoglycosidase H)
227:
590:
533:
442:-acetylglucosaminidase from fig latex".
1494:
793:IUBMB Enzyme Nomenclature - EC 3.2.1.96
430:
15:
618:-acetylglucosaminidase specificity".
7:
85:endo-β-(1→4)-N-acetylglucosaminidase
769:(4th ed.). New York: Garland.
686:The Journal of Biological Chemistry
651:The Journal of Biological Chemistry
620:The Journal of Biological Chemistry
479:The Journal of Biological Chemistry
339:Endoglycosidase H is isolated from
14:
97:endo-N-acetyl-β-D-glucosaminidase
1497:
117:endo-β-N-acetylglucosaminidase L
113:endo-β-N-acetylglucosaminidase H
109:endo-β-N-acetylglucosaminidase F
105:endo-β-N-acetylglucosaminidase D
61:Endo-β-N-acetylglucosaminidase H
1101:Alpha-N-acetylgalactosaminidase
506:"Cytosolic location of an endo-
101:endo-N-acetyl-β-glucosaminidase
383:posttranslational modification
1:
1113:Alpha-N-acetylglucosaminidase
767:Molecular Biology of the Cell
711:Endoglycosidase H, North Star
444:Biochem. Biophys. Res. Commun
279:mannosyl-glycoprotein endo-β-
19:Mannosyl-glycoprotein endo-β-
744:10.1016/0003-2697(84)90080-0
456:10.1016/0006-291x(77)90727-6
81:endo-β-acetylglucosaminidase
730:-acetylglucosaminidase H".
684:-acetylglucosaminidase H".
649:-acetylglucosaminidase H".
1536:
407:oligosaccharyl transferase
307:. It is a highly specific
1375:Michaelis–Menten kinetics
226:
1267:Diffusion-limited enzyme
806:F and D, cleave Glc-Nac
377:Biochemical applications
1023:Bacterial neuraminidase
732:Analytical Biochemistry
571:The Biochemical Journal
514:The Biochemical Journal
1186:Oxoguanine glycosylase
475:Diplococcus pneumoniae
335:Structure and activity
301:-mannosyl-N-(N-acetyl-
23:-acetylglucosaminidase
1360:Eadie–Hofstee diagram
1293:Allosteric regulation
399:endoplasmic reticulum
342:Streptomyces plicatus
315:-linked mannose rich
1370:Lineweaver–Burk plot
1175:N-Glycosyl compounds
1145:Maltase-glucoamylase
1096:Galactosylceramidase
863:Glycoside hydrolases
848:: sugar hydrolases (
348:Streptomyces griseus
1028:Viral neuraminidase
325:protein trafficking
1329:Enzyme superfamily
1262:Enzyme promiscuity
1079:Glucosylceramidase
960:Debranching enzyme
884:Sucrase-isomaltase
765:Alberts B (2002).
363:-acetylglucosamine
1485:
1484:
1194:
1193:
1165:
1164:
1052:alpha-Mannosidase
926:Alpha-glucosidase
776:978-0-8153-4072-0
583:10.1042/bj1850261
526:10.1042/bj1800673
329:secretory pathway
304:
300:
275:
274:
271:
270:
190:metabolic pathway
125:endoglycosidase H
93:endoglycosidase S
1527:
1502:
1501:
1493:
1365:Hanes–Woolf plot
1308:Enzyme activator
1303:Enzyme inhibitor
1277:Enzyme catalysis
1221:
1214:
1207:
1198:
1182:DNA glycosylases
948:Beta-glucosidase
868:
839:
832:
825:
816:
804:Endoglycosidases
781:
780:
762:
756:
755:
719:
713:
708:
702:
701:
673:
667:
666:
642:
636:
635:
611:
605:
604:
594:
554:
548:
547:
537:
501:
495:
494:
485:(15): 4897–904.
466:
460:
459:
435:
415:α-mannosidase II
317:oligosaccharides
302:
298:
228:
68:
16:
1535:
1534:
1530:
1529:
1528:
1526:
1525:
1524:
1510:
1509:
1508:
1496:
1488:
1486:
1481:
1393:Oxidoreductases
1379:
1355:Enzyme kinetics
1343:
1339:List of enzymes
1312:
1281:
1252:Catalytic triad
1230:
1225:
1195:
1190:
1174:
1161:
964:
907:
853:
843:
801:
789:
784:
777:
764:
763:
759:
721:
720:
716:
709:
705:
692:(12): 7577–83.
675:
674:
670:
644:
643:
639:
626:(21): 8569–75.
613:
612:
608:
556:
555:
551:
503:
502:
498:
468:
467:
463:
437:
436:
432:
428:
411:Golgi apparatus
397:into the rough
387:Golgi apparatus
379:
337:
309:endoglycosidase
294:systematic name
66:
12:
11:
5:
1533:
1531:
1523:
1522:
1512:
1511:
1507:
1506:
1483:
1482:
1480:
1479:
1466:
1453:
1440:
1427:
1414:
1401:
1387:
1385:
1381:
1380:
1378:
1377:
1372:
1367:
1362:
1357:
1351:
1349:
1345:
1344:
1342:
1341:
1336:
1331:
1326:
1320:
1318:
1317:Classification
1314:
1313:
1311:
1310:
1305:
1300:
1295:
1289:
1287:
1283:
1282:
1280:
1279:
1274:
1269:
1264:
1259:
1254:
1249:
1244:
1238:
1236:
1232:
1231:
1226:
1224:
1223:
1216:
1209:
1201:
1192:
1191:
1189:
1188:
1178:
1176:
1167:
1166:
1163:
1162:
1160:
1159:
1158:
1157:
1147:
1142:
1137:
1136:
1135:
1130:
1123:Hexosaminidase
1120:
1115:
1110:
1109:
1108:
1098:
1093:
1092:
1091:
1086:
1076:
1071:
1066:
1065:
1064:
1054:
1049:
1048:
1047:
1042:
1035:Galactosidases
1032:
1031:
1030:
1025:
1020:
1015:
1010:
1005:
995:
990:
985:
984:
983:
972:
970:
966:
965:
963:
962:
957:
956:
955:
945:
944:
943:
938:
933:
923:
917:
915:
909:
908:
906:
905:
900:
895:
890:
876:
874:
872:Disaccharidase
865:
855:
854:
844:
842:
841:
834:
827:
819:
800:
797:
796:
795:
788:
787:External links
785:
783:
782:
775:
757:
714:
703:
680:enzyme endo-β-
668:
637:
606:
549:
496:
461:
429:
427:
424:
378:
375:
353:molecular mass
336:
333:
311:which cleaves
273:
272:
269:
268:
263:
257:
256:
251:
245:
244:
239:
233:
232:
224:
223:
212:
205:
204:
199:
193:
192:
187:
181:
180:
175:
169:
168:
163:
157:
156:
151:
145:
144:
139:
133:
132:
128:
127:
58:
54:
53:
48:
42:
41:
36:
30:
29:
25:
24:
13:
10:
9:
6:
4:
3:
2:
1532:
1521:
1518:
1517:
1515:
1505:
1500:
1495:
1491:
1477:
1473:
1472:
1467:
1464:
1460:
1459:
1454:
1451:
1447:
1446:
1441:
1438:
1434:
1433:
1428:
1425:
1421:
1420:
1415:
1412:
1408:
1407:
1402:
1399:
1395:
1394:
1389:
1388:
1386:
1382:
1376:
1373:
1371:
1368:
1366:
1363:
1361:
1358:
1356:
1353:
1352:
1350:
1346:
1340:
1337:
1335:
1334:Enzyme family
1332:
1330:
1327:
1325:
1322:
1321:
1319:
1315:
1309:
1306:
1304:
1301:
1299:
1298:Cooperativity
1296:
1294:
1291:
1290:
1288:
1284:
1278:
1275:
1273:
1270:
1268:
1265:
1263:
1260:
1258:
1257:Oxyanion hole
1255:
1253:
1250:
1248:
1245:
1243:
1240:
1239:
1237:
1233:
1229:
1222:
1217:
1215:
1210:
1208:
1203:
1202:
1199:
1187:
1183:
1180:
1179:
1177:
1173:: Hydrolysing
1172:
1168:
1156:
1153:
1152:
1151:
1148:
1146:
1143:
1141:
1138:
1134:
1131:
1129:
1126:
1125:
1124:
1121:
1119:
1116:
1114:
1111:
1107:
1104:
1103:
1102:
1099:
1097:
1094:
1090:
1089:non-lysosomal
1087:
1085:
1082:
1081:
1080:
1077:
1075:
1072:
1070:
1069:Hyaluronidase
1067:
1063:
1060:
1059:
1058:
1057:Glucuronidase
1055:
1053:
1050:
1046:
1043:
1041:
1038:
1037:
1036:
1033:
1029:
1026:
1024:
1021:
1019:
1016:
1014:
1011:
1009:
1006:
1004:
1001:
1000:
999:
998:Neuraminidase
996:
994:
991:
989:
986:
982:
981:Alpha-amylase
979:
978:
977:
974:
973:
971:
967:
961:
958:
954:
951:
950:
949:
946:
942:
939:
937:
934:
932:
929:
928:
927:
924:
922:
919:
918:
916:
914:
910:
904:
901:
899:
896:
894:
891:
889:
885:
881:
878:
877:
875:
873:
869:
866:
864:
860:
856:
851:
847:
840:
835:
833:
828:
826:
821:
820:
817:
813:
811:
807:
805:
799:Close enzymes
798:
794:
791:
790:
786:
778:
772:
768:
761:
758:
753:
749:
745:
741:
738:(2): 515–22.
737:
733:
729:
725:
718:
715:
712:
707:
704:
699:
695:
691:
687:
683:
679:
672:
669:
664:
660:
657:(3): 818–24.
656:
652:
648:
641:
638:
633:
629:
625:
621:
617:
610:
607:
602:
598:
593:
588:
584:
580:
576:
572:
568:
566:
562:
553:
550:
545:
541:
536:
531:
527:
523:
520:(3): 673–76.
519:
515:
511:
509:
500:
497:
492:
488:
484:
480:
476:
472:
465:
462:
457:
453:
449:
445:
441:
434:
431:
425:
423:
420:
416:
412:
408:
404:
400:
396:
392:
388:
384:
376:
374:
370:
368:
364:
362:
356:
354:
350:
349:
344:
343:
334:
332:
330:
326:
322:
321:glycoproteins
318:
314:
310:
306:
297:glycopeptide-
295:
291:
288:
284:
282:
267:
264:
262:
258:
255:
252:
250:
246:
243:
240:
238:
234:
229:
225:
222:
219:
216:
213:
210:
206:
203:
200:
198:
194:
191:
188:
186:
182:
179:
176:
174:
170:
167:
166:NiceZyme view
164:
162:
158:
155:
152:
150:
146:
143:
140:
138:
134:
129:
126:
122:
118:
114:
110:
106:
102:
98:
94:
90:
86:
82:
78:
74:
70:
62:
59:
55:
52:
49:
47:
43:
40:
37:
35:
31:
26:
22:
17:
1471:Translocases
1468:
1455:
1442:
1429:
1416:
1406:Transferases
1403:
1390:
1247:Binding site
913:Glucosidases
808:
802:
766:
760:
735:
731:
727:
723:
717:
706:
689:
685:
681:
678:Streptomyces
677:
671:
654:
650:
646:
640:
623:
619:
615:
609:
577:(1): 261–4.
574:
570:
564:
560:
552:
517:
513:
507:
499:
482:
478:
474:
470:
464:
447:
443:
439:
433:
417:removes two
402:
380:
371:
366:
360:
357:
346:
340:
338:
327:through the
296:
280:
278:
276:
154:BRENDA entry
124:
120:
116:
112:
108:
104:
100:
96:
92:
88:
84:
80:
76:
72:
64:
60:
20:
1242:Active site
1140:Iduronidase
1074:Pullulanase
450:: 317–323.
277:The enzyme
142:IntEnz view
51:37278-88-9
28:Identifiers
1445:Isomerases
1419:Hydrolases
1286:Regulation
1150:Heparanase
1118:Fucosidase
936:Neutral AB
426:References
391:translated
313:asparagine
211:structures
178:KEGG entry
57:Alt. names
1324:EC number
1084:lysosomal
988:Chitinase
953:cytosolic
941:Neutral C
921:Cellulase
898:Trehalase
888:Invertase
846:Hydrolase
395:ribosomes
131:Databases
1520:EC 3.2.1
1514:Category
1348:Kinetics
1272:Cofactor
1235:Activity
993:Lysozyme
810:PNGase F
290:3.2.1.96
266:proteins
254:articles
242:articles
215:RCSB PDB
39:3.2.1.96
1504:Biology
1458:Ligases
1228:Enzymes
976:Amylase
903:Lactase
893:Maltase
880:Sucrase
752:6437277
698:6429133
663:4204553
601:7378051
592:1161293
535:1161109
491:4152561
419:mannose
403:en bloc
385:in the
202:profile
185:MetaCyc
46:CAS no.
1490:Portal
1432:Lyases
1062:Klotho
773:
750:
696:
661:
630:
599:
589:
544:486141
542:
532:
489:
351:. Its
292:) has
249:PubMed
231:Search
221:PDBsum
161:ExPASy
149:BRENDA
137:IntEnz
34:EC no.
1384:Types
1171:3.2.2
1155:HPSE2
1040:Alpha
969:Other
859:3.2.1
197:PRIAM
1476:list
1469:EC7
1463:list
1456:EC6
1450:list
1443:EC5
1437:list
1430:EC4
1424:list
1417:EC3
1411:list
1404:EC2
1398:list
1391:EC1
1133:HEXB
1128:HEXA
1106:NAGA
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