561:
545:
466:
553:
40:
1556:
251:
498:, the precursor to aromatic amino acids. 3-Dehydroquinate synthase is the enzyme that catalyzes reaction in the second step of this pathway. This second step of the reaction eliminates a phosphate from 3-deoxy-D-arabino-heptulosonate 7-phosphate, which results in 3-dehydroquinate. 3-Dehydroquinate synthase is a
540:
3-Dehydroquinate synthase catalyzes the second step in the shikimate pathway, which is essential for the production of aromatic amino acids in bacteria, plants, and fungi, but not mammals. This makes it an ideal target for new antimicrobial agents, anti-parasitic agents, and herbicides. Other enzymes
523:
to catalyze the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate into 3-dehydroquinate. Dehydroquinate synthase is of particular interest because of its complicated activity relative to its small size. In most bacteria, this enzyme has only one function. However, in fungi and protists, it is
589:. Other names in common use include 5-dehydroquinate synthase, 5-dehydroquinic acid synthetase, dehydroquinate synthase, 3-dehydroquinate synthetase, 3-deoxy-arabino-heptulosonate-7-phosphate phosphate-lyase, (cyclizing), and 3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing).
514:
3-Dehydroquinate synthase utilizes a complex multi-step mechanism that includes alcohol oxidation, phosphate β-elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. Dehydroquinate synthase requires
490:, which are essential to our diets because we cannot synthesize them in our bodies. Only plants, bacteria, and microbial eukaryotes are capable of producing aromatic amino acids. The pathway ultimately converts
418:
1060:
828:
Arora
VerasztĂł, H; Logotheti, M; Albrecht, R; Leitner, A; Zhu, H; Hartmann, MD (6 July 2020). "Architecture and functional dynamics of the pentafunctional AROM complex".
964:
Bender SL, Mehdi S, Knowles JR (September 1989). "Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis".
350:
205:
224:
993:
Carpenter EP, Hawkins AR, Frost JW, Brown KA (July 1998). "Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis".
1053:
619:
Liu JS, Cheng WC, Wang HJ, Chen YC, Wang WC (August 2008). "Structure-based inhibitor discovery of
Helicobacter pylori dehydroquinate synthase".
564:
This representation of 3-dehydroquinate synthase shows the surface of the enzyme, as well as the active site, which can be seen in the middle.
298:
556:
3-dehydroquinate synthase interacting with its substrates NAD, carbaphosphonate, and Zn, which are shown as spheres in this representation
1586:
1046:
1275:
503:
428:
217:
1237:
560:
544:
1140:
144:
1431:
370:
168:
1170:
1160:
502:
enzyme, and has a molecular weight of 39,000. 3-dehydroquinate synthase is activated by inorganic phosphate, and requires
1546:
548:
This cartoon representation of 3-dehydroquinate synthase shows the arrangement of the secondary structure of the protein
529:
465:
1150:
1135:
552:
1416:
1532:
1519:
1506:
1493:
1480:
1467:
1454:
1228:
1209:
1185:
1087:
1426:
1380:
1323:
1155:
1074:
162:
55:
358:
1581:
1328:
520:
455:
149:
1038:
403:
1349:
1268:
693:
Barten R, Meyer TF (April 1998). "Cloning and characterisation of the
Neisseria gonorrhoeae aroB gene".
229:
1421:
658:
Hawkins AR, Lamb HK (August 1995). "The molecular biology of multidomain proteins. Selected examples".
354:
137:
72:
1002:
889:
487:
311:
779:"Expression, Purification, and Characterisation of Dehydroquinate Synthase from Pyrococcus furiosus"
1385:
1242:
1145:
1131:
491:
67:
525:
165:
39:
1318:
1218:
1099:
1026:
853:
718:
89:
931:"The enzymic conversion of 3-deoxy-d-arabino-heptulosonic acid 7-phosphate to 5-dehydroquinate"
1576:
1194:
1175:
1018:
981:
952:
917:
845:
810:
756:
710:
675:
636:
609:
479:
442:, to be specific those carbon-oxygen lyases acting on phosphates. This enzyme participates in
432:
394:
345:
156:
1364:
1359:
1333:
1261:
1010:
973:
942:
907:
897:
837:
800:
790:
748:
702:
667:
628:
528:
that comprises steps two, three, four, five and six of the shikimate pathway. Together with
420:
337:
1411:
1395:
1308:
574:
125:
1006:
893:
101:
1560:
1449:
1390:
805:
778:
671:
200:
60:
947:
930:
912:
877:
180:
1570:
1354:
1313:
1119:
857:
752:
506:
for activity, although the reaction in total is neutral when catalyzed by an enzyme.
443:
303:
175:
722:
279:
1303:
1199:
1030:
587:-hept-2-ulosonate-7-phosphate phosphate-lyase (cyclizing; 3-dehydroquinate-forming)
541:
in the shikimate pathway have already been targeted and put to use as herbicides.
333:
291:
1527:
1462:
1298:
1091:
1078:
184:
1555:
882:
Proceedings of the
National Academy of Sciences of the United States of America
632:
841:
495:
451:
1501:
1475:
1165:
1124:
1109:
499:
390:
17:
956:
902:
849:
814:
760:
640:
44:
Ribbon representation of the
Helicobacter pylori 3-dehydroquinate synthase.
1022:
985:
921:
795:
714:
706:
679:
307:
1104:
486:. The shikimate pathway is responsible for producing the precursors for
447:
286:
977:
1114:
132:
113:
613:
1514:
1284:
483:
459:
383:
365:
212:
108:
96:
84:
516:
1488:
1070:
1014:
439:
327:
274:
120:
1257:
1042:
435:
which is involved in the biosynthesis of aromatic amino acids.
250:
878:"Mechanism and stereochemistry of 5-dehydroquinate synthetase"
741:
Annual Review of Plant
Physiology and Plant Molecular Biology
739:
Herrmann KM, Weaver LM (June 1999). "The
Shikimate Pathway".
532:, 3-dehydroquinate synthase forms the core of this complex.
1253:
929:
Srinivasan PR, Rothschild J, Sprinson DB (October 1963).
255:
3-Dehydroquinate synthase homodimer, Aspergillus nidulans
407:
646:
431:
to catalyze the reaction. This reaction is part of the
1544:
406:
1440:
1404:
1373:
1342:
1291:
1227:
1208:
1184:
1086:
621:
469:
The reaction catalyzed by 3-dehydroquinate synthase
438:3-Dehydroquinate synthase belongs to the family of
364:
344:
326:
321:
297:
285:
273:
265:
260:
243:
223:
211:
199:
194:
174:
155:
143:
131:
119:
107:
95:
83:
78:
66:
54:
49:
32:
412:
482:is composed of seven steps, each catalyzed by an
772:
770:
734:
732:
604:
602:
1269:
1054:
8:
876:Rotenberg SL, Sprinson DB (December 1970).
1276:
1262:
1254:
1061:
1047:
1039:
318:
191:
38:
946:
911:
901:
804:
794:
777:Negron L, Patchett ML, Parker EJ (2011).
405:
559:
551:
543:
464:
1551:
598:
240:
29:
7:
935:The Journal of Biological Chemistry
413:{\displaystyle \rightleftharpoons }
672:10.1111/j.1432-1033.1995.tb20775.x
25:
1554:
753:10.1146/annurev.arplant.50.1.473
695:Molecular & General Genetics
660:European Journal of Biochemistry
249:
1238:Carboxymethyloxysuccinate lyase
494:and 4-erythrose phosphate into
1141:Methylglutaconyl-CoA hydratase
454:biosynthesis. It employs one
1:
1171:Uroporphyrinogen III synthase
1161:3-Isopropylmalate dehydratase
948:10.1016/S0021-9258(18)48643-7
322:Available protein structures:
530:3-dehydroquinate dehydratase
524:part of the pentafunctional
1188:: Acting on polysaccharides
1151:Cystathionine beta synthase
1136:3-Hydroxyacyl ACP dehydrase
1603:
1587:Enzymes of known structure
633:10.1016/j.bbrc.2008.05.070
1432:Michaelis–Menten kinetics
842:10.1038/s41589-020-0587-9
387:3-dehydroquinate synthase
317:
248:
244:3-dehydroquinate synthase
190:
37:
33:3-dehydroquinate synthase
1324:Diffusion-limited enzyme
1156:Porphobilinogen synthase
577:of this enzyme class is
830:Nature Chemical Biology
1212:: Acting on phosphates
903:10.1073/pnas.67.4.1669
565:
557:
549:
470:
414:
1417:Eadie–Hofstee diagram
1350:Allosteric regulation
707:10.1007/s004380050704
563:
555:
547:
468:
415:
1427:Lineweaver–Burk plot
488:aromatic amino acids
404:
1243:Hydroperoxide lyase
1146:Tryptophan synthase
1132:Enoyl-CoA hydratase
1007:1998Natur.394..299C
978:10.1021/bi00445a009
894:1970PNAS...67.1669R
796:10.4061/2011/134893
492:phosphoenolpyruvate
1386:Enzyme superfamily
1319:Enzyme promiscuity
1219:Threonine synthase
1100:Carbonic anhydrase
566:
558:
550:
471:
410:
1542:
1541:
1251:
1250:
1195:Hyaluronate lyase
1176:Nitrile hydratase
1001:(6690): 299–302.
582:
480:shikimate pathway
433:shikimate pathway
427:The protein uses
395:chemical reaction
380:
379:
376:
375:
371:structure summary
239:
238:
235:
234:
138:metabolic pathway
16:(Redirected from
1594:
1559:
1558:
1550:
1422:Hanes–Woolf plot
1365:Enzyme activator
1360:Enzyme inhibitor
1334:Enzyme catalysis
1278:
1271:
1264:
1255:
1077:4.2) (primarily
1063:
1056:
1049:
1040:
1034:
989:
960:
950:
925:
915:
905:
862:
861:
825:
819:
818:
808:
798:
774:
765:
764:
736:
727:
726:
690:
684:
683:
655:
649:
645:; rendered with
644:
616:
606:
580:
421:3-dehydroquinate
419:
417:
416:
411:
319:
253:
241:
192:
42:
30:
21:
1602:
1601:
1597:
1596:
1595:
1593:
1592:
1591:
1567:
1566:
1565:
1553:
1545:
1543:
1538:
1450:Oxidoreductases
1436:
1412:Enzyme kinetics
1400:
1396:List of enzymes
1369:
1338:
1309:Catalytic triad
1287:
1282:
1252:
1247:
1223:
1204:
1180:
1082:
1067:
1037:
992:
972:(19): 7555–60.
963:
941:(10): 3176–82.
928:
875:
871:
869:Further reading
866:
865:
827:
826:
822:
783:Enzyme Research
776:
775:
768:
738:
737:
730:
692:
691:
687:
657:
656:
652:
618:
608:
607:
600:
595:
575:systematic name
571:
538:
512:
476:
402:
401:
256:
45:
28:
23:
22:
15:
12:
11:
5:
1600:
1598:
1590:
1589:
1584:
1582:Cobalt enzymes
1579:
1569:
1568:
1564:
1563:
1540:
1539:
1537:
1536:
1523:
1510:
1497:
1484:
1471:
1458:
1444:
1442:
1438:
1437:
1435:
1434:
1429:
1424:
1419:
1414:
1408:
1406:
1402:
1401:
1399:
1398:
1393:
1388:
1383:
1377:
1375:
1374:Classification
1371:
1370:
1368:
1367:
1362:
1357:
1352:
1346:
1344:
1340:
1339:
1337:
1336:
1331:
1326:
1321:
1316:
1311:
1306:
1301:
1295:
1293:
1289:
1288:
1283:
1281:
1280:
1273:
1266:
1258:
1249:
1248:
1246:
1245:
1240:
1234:
1232:
1225:
1224:
1222:
1221:
1215:
1213:
1206:
1205:
1203:
1202:
1197:
1191:
1189:
1182:
1181:
1179:
1178:
1173:
1168:
1163:
1158:
1153:
1148:
1143:
1138:
1129:
1128:
1127:
1122:
1112:
1107:
1102:
1096:
1094:
1084:
1083:
1069:Carbon–oxygen
1068:
1066:
1065:
1058:
1051:
1043:
1036:
1035:
990:
961:
926:
888:(4): 1669–72.
872:
870:
867:
864:
863:
836:(9): 973–978.
820:
766:
728:
701:(1–2): 34–44.
685:
650:
597:
596:
594:
591:
570:
567:
537:
534:
511:
508:
475:
472:
425:
424:
409:
378:
377:
374:
373:
368:
362:
361:
348:
342:
341:
331:
324:
323:
315:
314:
301:
295:
294:
289:
283:
282:
277:
271:
270:
267:
263:
262:
258:
257:
254:
246:
245:
237:
236:
233:
232:
227:
221:
220:
215:
209:
208:
203:
197:
196:
188:
187:
178:
172:
171:
160:
153:
152:
147:
141:
140:
135:
129:
128:
123:
117:
116:
111:
105:
104:
99:
93:
92:
87:
81:
80:
76:
75:
70:
64:
63:
58:
52:
51:
47:
46:
43:
35:
34:
26:
24:
14:
13:
10:
9:
6:
4:
3:
2:
1599:
1588:
1585:
1583:
1580:
1578:
1575:
1574:
1572:
1562:
1557:
1552:
1548:
1534:
1530:
1529:
1524:
1521:
1517:
1516:
1511:
1508:
1504:
1503:
1498:
1495:
1491:
1490:
1485:
1482:
1478:
1477:
1472:
1469:
1465:
1464:
1459:
1456:
1452:
1451:
1446:
1445:
1443:
1439:
1433:
1430:
1428:
1425:
1423:
1420:
1418:
1415:
1413:
1410:
1409:
1407:
1403:
1397:
1394:
1392:
1391:Enzyme family
1389:
1387:
1384:
1382:
1379:
1378:
1376:
1372:
1366:
1363:
1361:
1358:
1356:
1355:Cooperativity
1353:
1351:
1348:
1347:
1345:
1341:
1335:
1332:
1330:
1327:
1325:
1322:
1320:
1317:
1315:
1314:Oxyanion hole
1312:
1310:
1307:
1305:
1302:
1300:
1297:
1296:
1294:
1290:
1286:
1279:
1274:
1272:
1267:
1265:
1260:
1259:
1256:
1244:
1241:
1239:
1236:
1235:
1233:
1230:
1226:
1220:
1217:
1216:
1214:
1211:
1207:
1201:
1198:
1196:
1193:
1192:
1190:
1187:
1183:
1177:
1174:
1172:
1169:
1167:
1164:
1162:
1159:
1157:
1154:
1152:
1149:
1147:
1144:
1142:
1139:
1137:
1133:
1130:
1126:
1123:
1121:
1118:
1117:
1116:
1113:
1111:
1108:
1106:
1103:
1101:
1098:
1097:
1095:
1093:
1089:
1085:
1080:
1076:
1072:
1064:
1059:
1057:
1052:
1050:
1045:
1044:
1041:
1032:
1028:
1024:
1020:
1016:
1015:10.1038/28431
1012:
1008:
1004:
1000:
996:
991:
987:
983:
979:
975:
971:
967:
962:
958:
954:
949:
944:
940:
936:
932:
927:
923:
919:
914:
909:
904:
899:
895:
891:
887:
883:
879:
874:
873:
868:
859:
855:
851:
847:
843:
839:
835:
831:
824:
821:
816:
812:
807:
802:
797:
792:
788:
784:
780:
773:
771:
767:
762:
758:
754:
750:
746:
742:
735:
733:
729:
724:
720:
716:
712:
708:
704:
700:
696:
689:
686:
681:
677:
673:
669:
665:
661:
654:
651:
648:
642:
638:
634:
630:
626:
622:
615:
611:
605:
603:
599:
592:
590:
588:
586:
576:
568:
562:
554:
546:
542:
535:
533:
531:
527:
522:
519:and a cobalt
518:
509:
507:
505:
501:
497:
493:
489:
485:
481:
473:
467:
463:
461:
457:
453:
449:
445:
444:phenylalanine
441:
436:
434:
430:
422:
399:
398:
397:
396:
392:
389:(EC 4.2.3.4)
388:
385:
372:
369:
367:
363:
360:
356:
352:
349:
347:
343:
339:
335:
332:
329:
325:
320:
316:
313:
309:
305:
302:
300:
296:
293:
290:
288:
284:
281:
278:
276:
272:
268:
264:
259:
252:
247:
242:
231:
228:
226:
222:
219:
216:
214:
210:
207:
204:
202:
198:
193:
189:
186:
182:
179:
177:
176:Gene Ontology
173:
170:
167:
164:
161:
158:
154:
151:
148:
146:
142:
139:
136:
134:
130:
127:
124:
122:
118:
115:
114:NiceZyme view
112:
110:
106:
103:
100:
98:
94:
91:
88:
86:
82:
77:
74:
71:
69:
65:
62:
59:
57:
53:
48:
41:
36:
31:
19:
1528:Translocases
1525:
1512:
1499:
1486:
1473:
1463:Transferases
1460:
1447:
1304:Binding site
1200:Pectin lyase
1092:Hydro-Lyases
1079:dehydratases
998:
994:
969:
966:Biochemistry
965:
938:
934:
885:
881:
833:
829:
823:
786:
782:
744:
740:
698:
694:
688:
663:
659:
653:
624:
620:
584:
578:
572:
569:Nomenclature
539:
536:Applications
526:AROM complex
513:
477:
437:
426:
386:
381:
269:DHQ_synthase
102:BRENDA entry
18:DHQ synthase
1299:Active site
747:: 473–503.
666:(1): 7–18.
423:+ phosphate
261:Identifiers
90:IntEnz view
73:37211-77-1
50:Identifiers
1571:Categories
1502:Isomerases
1476:Hydrolases
1343:Regulation
789:: 134893.
627:(1): 1–7.
593:References
496:chorismate
474:Background
452:tryptophan
334:structures
159:structures
126:KEGG entry
1381:EC number
1166:Urocanase
1125:Enolase 2
1110:Aconitase
858:220375879
617:;
500:monomeric
408:⇌
391:catalyzes
292:IPR002658
79:Databases
1577:EC 4.2.3
1405:Kinetics
1329:Cofactor
1292:Activity
1105:Fumarase
957:14085358
850:32632294
815:21603259
761:15012217
723:26380973
647:MacPyMOL
641:18503755
579:3-deoxy-
521:cofactor
510:Function
456:cofactor
448:tyrosine
351:RCSB PDB
287:InterPro
230:proteins
218:articles
206:articles
163:RCSB PDB
1561:Biology
1515:Ligases
1285:Enzymes
1231:: Other
1115:Enolase
1031:4423190
1023:9685163
1003:Bibcode
986:2514789
922:5275368
890:Bibcode
806:3092513
715:9613570
680:7556173
585:arabino
280:PF01761
185:QuickGO
150:profile
133:MetaCyc
68:CAS no.
61:4.2.3.4
1547:Portal
1489:Lyases
1229:4.2.99
1071:lyases
1029:
1021:
995:Nature
984:
955:
920:
913:283410
910:
856:
848:
813:
803:
759:
721:
713:
678:
639:
484:enzyme
462:(Co).
460:cobalt
450:, and
440:lyases
384:enzyme
366:PDBsum
340:
330:
312:SUPFAM
266:Symbol
213:PubMed
195:Search
181:AmiGO
169:PDBsum
109:ExPASy
97:BRENDA
85:IntEnz
56:EC no.
27:Enzyme
1441:Types
1210:4.2.3
1186:4.2.2
1120:Alpha
1088:4.2.1
1027:S2CID
854:S2CID
719:S2CID
308:SCOPe
299:SCOP2
145:PRIAM
1533:list
1526:EC7
1520:list
1513:EC6
1507:list
1500:EC5
1494:list
1487:EC4
1481:list
1474:EC3
1468:list
1461:EC2
1455:list
1448:EC1
1019:PMID
982:PMID
953:PMID
918:PMID
846:PMID
811:PMID
787:2011
757:PMID
711:PMID
676:PMID
637:PMID
614:3CLH
573:The
478:The
393:the
382:The
359:PDBj
355:PDBe
338:ECOD
328:Pfam
304:1dqs
275:Pfam
225:NCBI
166:PDBe
121:KEGG
1011:doi
999:394
974:doi
943:doi
939:238
908:PMC
898:doi
838:doi
801:PMC
791:doi
749:doi
703:doi
699:258
668:doi
664:232
629:doi
625:373
610:PDB
517:NAD
504:NAD
429:NAD
346:PDB
201:PMC
157:PDB
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