327:
304:
201:
226:
1396:
333:
232:
1505:
normal levels. Though the exact mechanism of how loss of aspartoacylase activity leads to
Canavan disease is not fully understood, there are two primary competing explanations. The first is that it leads to defective myelin synthesis due to a deficiency of acetyl-CoA derived from the acetate product. Another explanation is that the elevated levels of N-acetyl-l-aspartate interfere with its normal brain
1546:
1069:
1530:
1388:
1504:
disorder that causes spongy degeneration of the white matter in the brain and severe psychomotor retardation, usually leading to death at a young age. The loss of aspartoacylase activity leads to the buildup of N-acetyl-L-aspartate in the brain and an increase in urine concentration by up to 60 times
52:
1399:
Active site of aspartoacylase with a bound N-phosphonamidate-L-aspartate. This is a tetrahedral intermediate analogue with phosphorus replacing the attacked carbon. In the structure, zinc, Arg-63, and Glu-178 are stabilizing the tetrahedral intermediate. Generated from
1512:
There are over 70 reported mutations of this enzyme, but the most common ones are the amino acid substitutions E285A and A305E. E285A reduces activity of aspartoacylase down to as low as 0.3% of its normal function and is found in 98% of cases with
1437:
1425:. Aspartoacylase follows the deprotonated water mechanism. Zinc lowers the pKa of a ligated water molecule and the reaction proceeds via an attack on N-acetyl-l-aspartate when the water molecule is deprotonated by Glu-178. This leads to a
1457:. It is not known why so much N-acetyl-L-aspartate is produced in the brain nor what its primary function is. However, one hypothesis is that it is potentially used as a chemical reservoir that can be tapped into for acetate for
1453:-acetyl-L-aspartate by catalyzing its deacylation. Aspartoacylase prevents the buildup of N-acetyl-L-aspartate in the brain. It is believed that controlling N-acetyl-L-aspartate levels is essential for developing and maintaining
1371:
The zinc cofactor is found at the active site and is held by Glu-24, His-21, and His 116. The substrate is held in place by Arg-63, Asn-70, Arg-71, Tyr-164, Arg-168, and Tyr-288. The zinc cofactor is used to lower the
1517:
ancestry. The mutation A305E is found in about 40% of non-Jewish patients and reduces activity to about 10%. Of these two mutations, a crystal structure of the E285A mutant has been taken, showing that the loss of the
2590:
2316:
Baslow MH (April 2002). "Evidence supporting a role for N-acetyl-L-aspartate as a molecular water pump in myelinated neurons in the central nervous system. An analytical review".
2410:
Namboodiri AM, Peethambaran A, Mathew R, Sambhu PA, Hershfield J, Moffett JR, Madhavarao CN (June 2006). "Canavan disease and the role of N-acetylaspartate in myelin synthesis".
2583:
2453:
Baslow MH, Guilfoyle DN (April 2013). "Canavan disease, a rare early-onset human spongiform leukodystrophy: insights into its genesis and possible clinical interventions".
1348:
domain from residues 1-212 and the C-terminal domain from residues 213–313. The N-terminal domain of aspartoacylase is similar to that of zinc-dependent hydrolases such as
340:
239:
1206:
2576:
1225:
1368:
access to the active site in aspartoacylase. Instead, the N-domain and C-domain of aspartoacylase form a deep narrow channel that leads to the active site.
1772:
2491:
Zano S, Wijayasinghe YS, Malik R, Smith J, Viola RE (January 2013). "Relationship between enzyme properties and disease progression in
Canavan disease".
792:
773:
162:
1426:
3180:
2819:
1680:
1433:
is then reformed, the bond with nitrogen is broken, and the nitrogen is protonated by the proton taken by Glu-178 all in one concerted step.
1662:
326:
49:
2137:
Zhang C, Liu X, Xue Y (January 2012). "A general acid–general base reaction mechanism for human brain aspartoacylase: A QM/MM study".
1967:"Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease"
1007:
303:
2901:
1810:
1000:
2269:"Intraneuronal N-acetylaspartate supplies acetyl groups for myelin lipid synthesis: evidence for myelin-associated aspartoacylase"
1218:
2169:"N-Acetylaspartate reductions in brain injury: impact on post-injury neuroenergetics, lipid synthesis, and protein acetylation"
1649:
1628:
1533:
Distortion of the active site caused by the E285A mutation. Wild type ASPA is on the left (2O4H) and E285A on the right (4NFR).
2362:
Moore RA, Le Coq J, Faehnle CR, Viola RE (May 2003). "Purification and preliminary characterization of brain aspartoacylase".
2794:
1185:
1161:
225:
200:
3057:
1645:
1391:
A monomer of aspartoacylase with the N-domain in green, C-domain in yellow, and zinc cofactor in red. Generated from 2I3C.
1624:
142:
1526:
change that distorts the active site and alters the substrate binding, leading to the much lower catalytic activity.
339:
238:
2756:
3042:
3158:
3145:
3132:
3119:
3106:
3093:
3080:
2854:
2831:
2766:
2733:
2700:
2612:
332:
231:
3052:
1179:
3006:
2949:
2603:
2541:
1523:
1381:
1357:
1253:
1084:
837:
150:
1166:
2954:
2673:
2087:"Examination of the mechanism of human brain aspartoacylase through the binding of an intermediate analogue"
1395:
818:
2371:
1764:
1422:
1230:
2975:
2894:
1466:
1154:
214:
3047:
1352:. However, carboxypeptidases do not have something similar to the C-domain. In carboxypeptidase A, the
2804:
1978:
1501:
1318:
2376:
1469:
molecules and aspartoacylase is used to release them. For example, N-acetyl-L-aspartate produced in
3011:
2784:
2683:
2568:
1301:
in a mechanism analogous to many other zinc-dependent hydrolases. It is most commonly found in the
1182:
962:
911:
129:
1409:
There are two types of possible mechanisms for zinc-dependent hydrolases depending on what is the
1380:
water molecule so that an attack on N-acetyl-L-aspartate may occur and to stabilize the resulting
1106:
2944:
2809:
2516:
2435:
2341:
2298:
2249:
2218:
Hershfield JR, Madhavarao CN, Moffett JR, Benjamins JA, Garbern JY, Namboodiri A (October 2006).
2004:
1462:
1349:
174:
983:
958:
932:
907:
2035:"Aspartoacylase catalytic deficiency as the cause of Canavan disease: a structural perspective"
3185:
2779:
2548:
2508:
2470:
2427:
2389:
2333:
2290:
2241:
2200:
2116:
2056:
1996:
1947:
1898:
1849:
1806:
1746:
1569:
1564:
1333:
1321:
1279:
1173:
122:
42:
1485:
that acts as a molecular water pump that helps maintain a proper fluid balance in the brain.
2990:
2985:
2959:
2887:
2500:
2462:
2419:
2381:
2325:
2280:
2231:
2190:
2180:
2146:
2106:
2098:
2046:
1986:
1937:
1929:
1888:
1880:
1869:"Characterization of human aspartoacylase: the brain enzyme responsible for Canavan disease"
1839:
1798:
1736:
1726:
1365:
419:
350:
294:
249:
1142:
3037:
3021:
2934:
2661:
2537:
1497:
1474:
1314:
394:
170:
1297:. It is a zinc-dependent hydrolase that promotes the deprotonation of water to use as a
1118:
1982:
1089:
3075:
3016:
2836:
2799:
2771:
2723:
2718:
2705:
2617:
2195:
2168:
2111:
2086:
1942:
1917:
1893:
1868:
1741:
1714:
1551:
1514:
1506:
1344:
and uses a zinc cofactor in each. There are two distinct domains in each monomer: the
1201:
621:
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
2385:
2329:
1844:
1827:
1802:
707:
702:
697:
692:
687:
671:
666:
661:
645:
640:
635:
630:
625:
620:
615:
610:
3174:
2980:
2939:
2863:
2789:
2738:
2557:
2285:
2268:
1559:
1519:
1418:
1414:
1290:
597:
2520:
2439:
2345:
2302:
2253:
2008:
2929:
2645:
2625:
1933:
1454:
412:
191:
1991:
1966:
1496:
that lead to loss of aspartoacylase activity have been identified as the cause of
1440:
Aspartoacylase mechanism. All the coordinating residues are not shown for clarity.
154:
2466:
2150:
178:
3153:
3088:
2924:
2713:
2640:
2630:
1685:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1667:
National Center for
Biotechnology Information, U.S. National Library of Medicine
1410:
1361:
1353:
1298:
1719:
Proceedings of the
National Academy of Sciences of the United States of America
1545:
495:
2868:
2751:
2668:
2504:
2423:
1541:
1458:
1345:
1341:
311:
208:
158:
2185:
3127:
3101:
2844:
2599:
1731:
1529:
1436:
1275:
1246:
737:
555:
433:
378:
365:
277:
264:
166:
2512:
2474:
2431:
2393:
2337:
2294:
2245:
2204:
2120:
2085:
Le Coq J, Pavlovsky A, Malik R, Sanishvili R, Xu C, Viola RE (March 2008).
2060:
2000:
1951:
1902:
1853:
1750:
1715:"Structure of aspartoacylase, the brain enzyme impaired in Canavan disease"
2236:
2219:
1387:
1047:
1042:
2746:
1918:"Mutational analysis of aspartoacylase: implications for Canavan disease"
1713:
Bitto E, Bingman CA, Wesenberg GE, McCoy JG, Phillips GN (January 2007).
1493:
1482:
1430:
1310:
1031:
882:
863:
1965:
Herga S, Berrin JG, Perrier J, Puigserver A, Giardina T (October 2006).
1916:
Hershfield JR, Pattabiraman N, Madhavarao CN, Namboodiri MA (May 2007).
1481:
synthesis. Another hypothesis is that N-acetyl-L-aspartate is essential
1256:
1130:
2688:
2562:
2552:
1337:
1294:
1149:
1068:
849:
804:
2102:
2051:
2034:
1884:
99:
95:
91:
87:
83:
79:
75:
71:
3140:
2910:
2635:
1478:
1470:
1377:
1249:
1213:
1125:
1113:
1101:
1015:
759:
1826:
Birnbaum SM, Levintow L, Kingsley RB, Greenstein JP (January 1952).
1413:. The first uses deprotonated water and the second attacks with an
1313:
that result in loss of aspartoacylase activity are associated with
3114:
2814:
1528:
1435:
1429:
that is stabilized by the zinc, Arg-63, and Glu-178. Finally, the
1394:
1386:
1302:
2267:
Chakraborty G, Mekala P, Yahya D, Wu G, Ledeen RW (August 2001).
2167:
Moffett JR, Arun P, Ariyannur PS, Namboodiri AM (December 2013).
722:
718:
2678:
2650:
1465:. This way, N-acetyl-L-aspartate can be used to transport these
1271:
1137:
146:
2883:
2572:
1373:
2547:
Overview of all the structural information available in the
2879:
2220:"Aspartoacylase is a regulated nuclear-cytoplasmic enzyme"
1797:. Methods in Enzymology. Vol. 2. pp. 115–119.
402:
2033:
Wijayasinghe YS, Pavlovsky AG, Viola RE (August 2014).
1073:
Structure of aspartoacylase dimer. Generated from 2I3C.
708:
positive regulation of oligodendrocyte differentiation
567:
2028:
2026:
2024:
2022:
2020:
2018:
3066:
3030:
2999:
2968:
2917:
2853:
2830:
2765:
2732:
2699:
2611:
1224:
1212:
1200:
1195:
1172:
1160:
1148:
1136:
1124:
1112:
1100:
1095:
1083:
1078:
1061:
976:
951:
925:
900:
2405:
2403:
1867:Le Coq J, An HJ, Lebrilla C, Viola RE (May 2006).
1641:
1639:
1637:
1620:
1618:
1616:
1267:and other names) that in humans is encoded by the
349:
248:
16:Hydrolytic enzyme encoded on human chromosome 17
2162:
2160:
1646:GRCm38: Ensembl release 89: ENSMUSG00000020774
2895:
2584:
2357:
2355:
2132:
2130:
1509:mechanism leading to osmotic disequilibrium.
8:
2486:
2484:
1708:
1706:
1704:
1702:
1700:
1698:
1696:
1694:
2080:
2078:
2076:
2074:
2072:
2070:
1625:GRCh38: Ensembl release 89: ENSG00000108381
2902:
2888:
2880:
2591:
2577:
2569:
1192:
1067:
733:
593:
390:
289:
186:
60:
2540:at the U.S. National Library of Medicine
2375:
2284:
2235:
2194:
2184:
2110:
2050:
1990:
1941:
1892:
1843:
1740:
1730:
1477:and the acetate released can be used for
631:hydrolase activity, acting on ester bonds
693:cellular amino acid biosynthetic process
2364:Archives of Biochemistry and Biophysics
2139:Computational and Theoretical Chemistry
1612:
1581:
2493:Journal of Inherited Metabolic Disease
1058:
20:
2820:Activation-induced cytidine deaminase
1461:synthesis or aspartate for glutamate
1449:Aspartoacylase is used to metabolize
1360:like the bulky C-terminal residue of
354:
315:
310:
253:
212:
207:
7:
2412:Molecular and Cellular Endocrinology
1828:"Specificity of amino acid acylases"
1832:The Journal of Biological Chemistry
1305:, where it controls the levels of
973:
948:
922:
897:
873:
854:
828:
809:
783:
764:
703:central nervous system myelination
572:
490:
428:
407:
14:
1775:from the original on 22 July 2022
2286:10.1046/j.1471-4159.2001.00456.x
1590:N-acetylaspartate amidohydrolase
1544:
1384:along with Arg-63, and Glu-178.
464:inferior ganglion of vagus nerve
338:
331:
325:
302:
237:
230:
224:
199:
2602:: carbon-nitrogen non-peptide (
2795:Inosine monophosphate synthase
1934:10.1016/j.brainres.2007.02.069
1765:"Aspartoacylase (EC 3.5.1.15)"
556:More reference expression data
1:
2386:10.1016/s0003-9861(03)00055-9
2330:10.1016/s0197-0186(01)00095-x
1992:10.1016/j.febslet.2006.09.056
1845:10.1016/S0021-9258(18)55898-1
1803:10.1016/S0076-6879(55)02176-9
323:
222:
3181:Genes on human chromosome 17
2467:10.1016/j.biochi.2012.10.023
2318:Neurochemistry International
2173:Frontiers in Neuroenergetics
2151:10.1016/j.comptc.2011.11.023
1588:The enzyme is also known as
1500:. Canavan disease is a rare
542:anterior horn of spinal cord
698:aspartate catabolic process
133:, ACY2, ASP, aspartoacylase
3202:
2757:Protein-arginine deiminase
2679:Fatty acid amide hydrolase
1522:from glutamate leads to a
3058:Michaelis–Menten kinetics
2505:10.1007/s10545-012-9520-z
2424:10.1016/j.mce.2006.03.016
2273:Journal of Neurochemistry
1795:[12] Aminoacylase
1681:"Mouse PubMed Reference:"
1663:"Human PubMed Reference:"
1594:acetyl-aspartic deaminase
1191:
1066:
1046:
1041:
1037:
1030:
1014:
995:
980:
955:
944:
929:
904:
893:
880:
876:
861:
857:
848:
835:
831:
816:
812:
803:
790:
786:
771:
767:
758:
743:
736:
732:
716:
646:identical protein binding
596:
592:
580:
575:
566:
553:
502:
493:
440:
431:
401:
393:
389:
372:
359:
322:
301:
292:
288:
271:
258:
221:
198:
189:
185:
140:
137:
127:
120:
115:
68:
63:
46:
41:
36:
32:
28:
23:
2950:Diffusion-limited enzyme
2561:(Aspartoacylase) at the
2542:Medical Subject Headings
2186:10.3389/fnene.2013.00011
1473:can be transported into
1427:tetrahedral intermediate
1382:tetrahedral intermediate
476:inferior olivary nucleus
452:internal globus pallidus
2674:Aspartylglucosaminidase
1732:10.1073/pnas.0607817104
1364:, whereas the C-domain
1356:is accessible to large
1008:Chr 11: 73.2 – 73.22 Mb
636:aspartoacylase activity
1534:
1441:
1401:
1392:
534:deep cerebellar nuclei
3043:Eadie–Hofstee diagram
2976:Allosteric regulation
2237:10.1096/fj.05-5358fje
1532:
1439:
1398:
1390:
1309:-acetyl-l-aspartate.
1001:Chr 17: 3.47 – 3.5 Mb
641:aminoacylase activity
317:Chromosome 11 (mouse)
215:Chromosome 17 (human)
3053:Lineweaver–Burk plot
2805:GTP cyclohydrolase I
1793:Birnbaum SM (1955).
1332:Aspartoacylase is a
530:brown adipose tissue
64:List of PDB id codes
37:Available structures
2785:Adenosine deaminase
2684:Histone deacetylase
1983:2006FEBSL.580.5899H
1502:autosomal recessive
1445:Biological function
1319:autosomal recessive
1283:-acetyl-l-aspartate
1278:the deacylation of
460:trigeminal ganglion
3012:Enzyme superfamily
2945:Enzyme promiscuity
2810:Cytidine deaminase
2769:: Cyclic amidines/
2736:: Linear amidines/
1535:
1442:
1402:
1393:
1366:sterically hinders
1287:N-acetylaspartate)
838:ENSMUSG00000020774
681:Biological process
655:Cellular component
616:hydrolase activity
604:Molecular function
3168:
3167:
2877:
2876:
2780:Guanine deaminase
2615:: Linear amides /
2103:10.1021/bi702400x
2052:10.1021/bi500719k
1885:10.1021/bi052608w
1570:Enzyme deficiency
1565:Neurodegeneration
1489:Disease relevance
1421:first forming an
1350:carboxypeptidaseA
1336:of two identical
1322:neurodegenerative
1240:
1239:
1236:
1235:
1155:metabolic pathway
1057:
1056:
1053:
1052:
1026:
1025:
991:
990:
970:
969:
940:
939:
919:
918:
889:
888:
870:
869:
844:
843:
825:
824:
799:
798:
780:
779:
728:
727:
626:metal ion binding
588:
587:
584:
583:
562:
561:
549:
548:
522:intestinal villus
487:
486:
385:
384:
284:
283:
111:
110:
107:
106:
47:Ortholog search:
3193:
3048:Hanes–Woolf plot
2991:Enzyme activator
2986:Enzyme inhibitor
2960:Enzyme catalysis
2904:
2897:
2890:
2881:
2703:: Cyclic amides/
2593:
2586:
2579:
2570:
2525:
2524:
2488:
2479:
2478:
2450:
2444:
2443:
2407:
2398:
2397:
2379:
2359:
2350:
2349:
2313:
2307:
2306:
2288:
2264:
2258:
2257:
2239:
2215:
2209:
2208:
2198:
2188:
2164:
2155:
2154:
2134:
2125:
2124:
2114:
2082:
2065:
2064:
2054:
2030:
2013:
2012:
1994:
1977:(25): 5899–904.
1962:
1956:
1955:
1945:
1913:
1907:
1906:
1896:
1864:
1858:
1857:
1847:
1823:
1817:
1816:
1790:
1784:
1783:
1781:
1780:
1761:
1755:
1754:
1744:
1734:
1710:
1689:
1688:
1677:
1671:
1670:
1659:
1653:
1643:
1632:
1622:
1600:
1586:
1554:
1549:
1548:
1520:hydrogen bonding
1515:Ashkenazi Jewish
1475:oligodendrocytes
1193:
1071:
1059:
1039:
1038:
1010:
1003:
986:
974:
965:
949:
945:RefSeq (protein)
935:
923:
914:
898:
874:
855:
829:
810:
784:
765:
734:
594:
573:
558:
498:
496:Top expressed in
491:
472:endothelial cell
436:
434:Top expressed in
429:
408:
391:
381:
368:
357:
342:
335:
329:
318:
306:
290:
280:
267:
256:
241:
234:
228:
217:
203:
187:
181:
179:ASPA - orthologs
132:
125:
102:
61:
55:
34:
33:
21:
3201:
3200:
3196:
3195:
3194:
3192:
3191:
3190:
3171:
3170:
3169:
3164:
3076:Oxidoreductases
3062:
3038:Enzyme kinetics
3026:
3022:List of enzymes
2995:
2964:
2935:Catalytic triad
2913:
2908:
2878:
2873:
2849:
2837:Aminohydrolases
2835:
2826:
2772:Aminohydrolases
2770:
2761:
2737:
2728:
2706:Amidohydrolases
2704:
2695:
2618:Amidohydrolases
2616:
2607:
2597:
2534:
2529:
2528:
2490:
2489:
2482:
2452:
2451:
2447:
2418:(1–2): 216–23.
2409:
2408:
2401:
2377:10.1.1.600.6321
2361:
2360:
2353:
2315:
2314:
2310:
2266:
2265:
2261:
2230:(12): 2139–41.
2217:
2216:
2212:
2166:
2165:
2158:
2136:
2135:
2128:
2097:(11): 3484–92.
2084:
2083:
2068:
2032:
2031:
2016:
1964:
1963:
1959:
1915:
1914:
1910:
1879:(18): 5878–84.
1866:
1865:
1861:
1825:
1824:
1820:
1813:
1792:
1791:
1787:
1778:
1776:
1763:
1762:
1758:
1712:
1711:
1692:
1679:
1678:
1674:
1661:
1660:
1656:
1644:
1635:
1623:
1614:
1609:
1604:
1603:
1587:
1583:
1578:
1550:
1543:
1540:
1498:Canavan disease
1491:
1447:
1407:
1330:
1315:Canavan disease
1261:aminoacylase II
1074:
1048:View/Edit Mouse
1043:View/Edit Human
1006:
999:
996:Location (UCSC)
982:
961:
957:
931:
910:
906:
819:ENSG00000108381
712:
676:
650:
611:protein binding
554:
545:
540:
538:globus pallidus
536:
532:
528:
524:
520:
516:
512:
510:proximal tubule
508:
494:
483:
478:
474:
470:
466:
462:
458:
454:
450:
446:
444:corpus callosum
432:
376:
363:
355:
345:
344:
343:
336:
316:
293:Gene location (
275:
262:
254:
244:
243:
242:
235:
213:
190:Gene location (
141:
128:
121:
70:
48:
17:
12:
11:
5:
3199:
3197:
3189:
3188:
3183:
3173:
3172:
3166:
3165:
3163:
3162:
3149:
3136:
3123:
3110:
3097:
3084:
3070:
3068:
3064:
3063:
3061:
3060:
3055:
3050:
3045:
3040:
3034:
3032:
3028:
3027:
3025:
3024:
3019:
3014:
3009:
3003:
3001:
3000:Classification
2997:
2996:
2994:
2993:
2988:
2983:
2978:
2972:
2970:
2966:
2965:
2963:
2962:
2957:
2952:
2947:
2942:
2937:
2932:
2927:
2921:
2919:
2915:
2914:
2909:
2907:
2906:
2899:
2892:
2884:
2875:
2874:
2872:
2871:
2866:
2860:
2858:
2851:
2850:
2848:
2847:
2841:
2839:
2828:
2827:
2825:
2824:
2823:
2822:
2817:
2807:
2802:
2800:DCMP deaminase
2797:
2792:
2787:
2782:
2776:
2774:
2763:
2762:
2760:
2759:
2754:
2749:
2743:
2741:
2739:Ureohydrolases
2730:
2729:
2727:
2726:
2724:Dihydroorotase
2721:
2719:Beta-lactamase
2716:
2710:
2708:
2697:
2696:
2694:
2693:
2692:
2691:
2681:
2676:
2671:
2666:
2665:
2664:
2659:
2656:Aspartoacylase
2653:
2643:
2638:
2633:
2628:
2622:
2620:
2609:
2608:
2598:
2596:
2595:
2588:
2581:
2573:
2567:
2566:
2545:
2538:Aspartoacylase
2533:
2532:External links
2530:
2527:
2526:
2480:
2445:
2399:
2351:
2324:(4): 295–300.
2308:
2259:
2210:
2156:
2126:
2066:
2045:(30): 4970–8.
2014:
1957:
1922:Brain Research
1908:
1859:
1818:
1811:
1785:
1756:
1690:
1672:
1654:
1633:
1611:
1610:
1608:
1605:
1602:
1601:
1580:
1579:
1577:
1574:
1573:
1572:
1567:
1562:
1556:
1555:
1552:Biology portal
1539:
1536:
1524:conformational
1507:osmoregulatory
1490:
1487:
1446:
1443:
1406:
1403:
1329:
1326:
1259:, also called
1243:Aspartoacylase
1238:
1237:
1234:
1233:
1228:
1222:
1221:
1216:
1210:
1209:
1204:
1198:
1197:
1189:
1188:
1177:
1170:
1169:
1164:
1158:
1157:
1152:
1146:
1145:
1140:
1134:
1133:
1128:
1122:
1121:
1116:
1110:
1109:
1104:
1098:
1097:
1093:
1092:
1087:
1081:
1080:
1076:
1075:
1072:
1064:
1063:
1062:Aspartoacylase
1055:
1054:
1051:
1050:
1045:
1035:
1034:
1028:
1027:
1024:
1023:
1021:
1019:
1012:
1011:
1004:
997:
993:
992:
989:
988:
978:
977:
971:
968:
967:
953:
952:
946:
942:
941:
938:
937:
927:
926:
920:
917:
916:
902:
901:
895:
891:
890:
887:
886:
878:
877:
871:
868:
867:
859:
858:
852:
846:
845:
842:
841:
833:
832:
826:
823:
822:
814:
813:
807:
801:
800:
797:
796:
788:
787:
781:
778:
777:
769:
768:
762:
756:
755:
750:
745:
741:
740:
730:
729:
726:
725:
714:
713:
711:
710:
705:
700:
695:
690:
684:
682:
678:
677:
675:
674:
669:
664:
658:
656:
652:
651:
649:
648:
643:
638:
633:
628:
623:
618:
613:
607:
605:
601:
600:
590:
589:
586:
585:
582:
581:
578:
577:
570:
564:
563:
560:
559:
551:
550:
547:
546:
544:
543:
539:
535:
531:
527:
523:
519:
515:
511:
507:
503:
500:
499:
488:
485:
484:
482:
481:
477:
473:
469:
465:
461:
457:
456:jejunal mucosa
453:
449:
445:
441:
438:
437:
425:
424:
416:
405:
399:
398:
395:RNA expression
387:
386:
383:
382:
374:
370:
369:
361:
358:
353:
347:
346:
337:
330:
324:
320:
319:
314:
308:
307:
299:
298:
286:
285:
282:
281:
273:
269:
268:
260:
257:
252:
246:
245:
236:
229:
223:
219:
218:
211:
205:
204:
196:
195:
183:
182:
139:
135:
134:
126:
118:
117:
113:
112:
109:
108:
105:
104:
66:
65:
57:
56:
45:
39:
38:
30:
29:
26:
25:
15:
13:
10:
9:
6:
4:
3:
2:
3198:
3187:
3184:
3182:
3179:
3178:
3176:
3160:
3156:
3155:
3150:
3147:
3143:
3142:
3137:
3134:
3130:
3129:
3124:
3121:
3117:
3116:
3111:
3108:
3104:
3103:
3098:
3095:
3091:
3090:
3085:
3082:
3078:
3077:
3072:
3071:
3069:
3065:
3059:
3056:
3054:
3051:
3049:
3046:
3044:
3041:
3039:
3036:
3035:
3033:
3029:
3023:
3020:
3018:
3017:Enzyme family
3015:
3013:
3010:
3008:
3005:
3004:
3002:
2998:
2992:
2989:
2987:
2984:
2982:
2981:Cooperativity
2979:
2977:
2974:
2973:
2971:
2967:
2961:
2958:
2956:
2953:
2951:
2948:
2946:
2943:
2941:
2940:Oxyanion hole
2938:
2936:
2933:
2931:
2928:
2926:
2923:
2922:
2920:
2916:
2912:
2905:
2900:
2898:
2893:
2891:
2886:
2885:
2882:
2870:
2869:Thiaminase II
2867:
2865:
2864:Riboflavinase
2862:
2861:
2859:
2856:
2852:
2846:
2843:
2842:
2840:
2838:
2833:
2829:
2821:
2818:
2816:
2813:
2812:
2811:
2808:
2806:
2803:
2801:
2798:
2796:
2793:
2791:
2790:AMP deaminase
2788:
2786:
2783:
2781:
2778:
2777:
2775:
2773:
2768:
2764:
2758:
2755:
2753:
2750:
2748:
2745:
2744:
2742:
2740:
2735:
2731:
2725:
2722:
2720:
2717:
2715:
2712:
2711:
2709:
2707:
2702:
2698:
2690:
2687:
2686:
2685:
2682:
2680:
2677:
2675:
2672:
2670:
2667:
2663:
2660:
2657:
2654:
2652:
2649:
2648:
2647:
2644:
2642:
2639:
2637:
2634:
2632:
2629:
2627:
2624:
2623:
2621:
2619:
2614:
2610:
2605:
2601:
2594:
2589:
2587:
2582:
2580:
2575:
2574:
2571:
2564:
2560:
2559:
2554:
2550:
2546:
2543:
2539:
2536:
2535:
2531:
2522:
2518:
2514:
2510:
2506:
2502:
2498:
2494:
2487:
2485:
2481:
2476:
2472:
2468:
2464:
2461:(4): 946–56.
2460:
2456:
2449:
2446:
2441:
2437:
2433:
2429:
2425:
2421:
2417:
2413:
2406:
2404:
2400:
2395:
2391:
2387:
2383:
2378:
2373:
2369:
2365:
2358:
2356:
2352:
2347:
2343:
2339:
2335:
2331:
2327:
2323:
2319:
2312:
2309:
2304:
2300:
2296:
2292:
2287:
2282:
2279:(4): 736–45.
2278:
2274:
2270:
2263:
2260:
2255:
2251:
2247:
2243:
2238:
2233:
2229:
2225:
2224:FASEB Journal
2221:
2214:
2211:
2206:
2202:
2197:
2192:
2187:
2182:
2178:
2174:
2170:
2163:
2161:
2157:
2152:
2148:
2144:
2140:
2133:
2131:
2127:
2122:
2118:
2113:
2108:
2104:
2100:
2096:
2092:
2088:
2081:
2079:
2077:
2075:
2073:
2071:
2067:
2062:
2058:
2053:
2048:
2044:
2040:
2036:
2029:
2027:
2025:
2023:
2021:
2019:
2015:
2010:
2006:
2002:
1998:
1993:
1988:
1984:
1980:
1976:
1972:
1968:
1961:
1958:
1953:
1949:
1944:
1939:
1935:
1931:
1927:
1923:
1919:
1912:
1909:
1904:
1900:
1895:
1890:
1886:
1882:
1878:
1874:
1870:
1863:
1860:
1855:
1851:
1846:
1841:
1838:(1): 455–70.
1837:
1833:
1829:
1822:
1819:
1814:
1812:9780121818029
1808:
1804:
1800:
1796:
1789:
1786:
1774:
1770:
1766:
1760:
1757:
1752:
1748:
1743:
1738:
1733:
1728:
1725:(2): 456–61.
1724:
1720:
1716:
1709:
1707:
1705:
1703:
1701:
1699:
1697:
1695:
1691:
1686:
1682:
1676:
1673:
1668:
1664:
1658:
1655:
1651:
1647:
1642:
1640:
1638:
1634:
1630:
1626:
1621:
1619:
1617:
1613:
1606:
1599:
1595:
1591:
1585:
1582:
1575:
1571:
1568:
1566:
1563:
1561:
1560:Aspartic acid
1558:
1557:
1553:
1547:
1542:
1537:
1531:
1527:
1525:
1521:
1516:
1510:
1508:
1503:
1499:
1495:
1488:
1486:
1484:
1480:
1476:
1472:
1468:
1464:
1460:
1456:
1452:
1444:
1438:
1434:
1432:
1428:
1424:
1420:
1416:
1412:
1404:
1397:
1389:
1385:
1383:
1379:
1375:
1369:
1367:
1363:
1359:
1355:
1351:
1347:
1343:
1339:
1335:
1327:
1325:
1323:
1320:
1316:
1312:
1308:
1304:
1300:
1296:
1292:
1288:
1284:
1282:
1277:
1273:
1270:
1266:
1262:
1258:
1255:
1251:
1248:
1244:
1232:
1229:
1227:
1223:
1220:
1217:
1215:
1211:
1208:
1205:
1203:
1199:
1194:
1190:
1187:
1184:
1181:
1178:
1175:
1171:
1168:
1165:
1163:
1159:
1156:
1153:
1151:
1147:
1144:
1141:
1139:
1135:
1132:
1131:NiceZyme view
1129:
1127:
1123:
1120:
1117:
1115:
1111:
1108:
1105:
1103:
1099:
1094:
1091:
1088:
1086:
1082:
1077:
1070:
1065:
1060:
1049:
1044:
1040:
1036:
1033:
1029:
1022:
1020:
1017:
1013:
1009:
1005:
1002:
998:
994:
987:
985:
979:
975:
972:
966:
964:
960:
954:
950:
947:
943:
936:
934:
928:
924:
921:
915:
913:
909:
903:
899:
896:
894:RefSeq (mRNA)
892:
885:
884:
879:
875:
872:
866:
865:
860:
856:
853:
851:
847:
840:
839:
834:
830:
827:
821:
820:
815:
811:
808:
806:
802:
795:
794:
789:
785:
782:
776:
775:
770:
766:
763:
761:
757:
754:
751:
749:
746:
742:
739:
735:
731:
724:
720:
715:
709:
706:
704:
701:
699:
696:
694:
691:
689:
686:
685:
683:
680:
679:
673:
670:
668:
665:
663:
660:
659:
657:
654:
653:
647:
644:
642:
639:
637:
634:
632:
629:
627:
624:
622:
619:
617:
614:
612:
609:
608:
606:
603:
602:
599:
598:Gene ontology
595:
591:
579:
574:
571:
569:
565:
557:
552:
541:
537:
533:
529:
525:
521:
517:
514:sciatic nerve
513:
509:
505:
504:
501:
497:
492:
489:
479:
475:
471:
467:
463:
459:
455:
451:
448:kidney tubule
447:
443:
442:
439:
435:
430:
427:
426:
423:
421:
417:
415:
414:
410:
409:
406:
404:
400:
396:
392:
388:
380:
375:
371:
367:
362:
356:11|11 B4
352:
348:
341:
334:
328:
321:
313:
309:
305:
300:
296:
291:
287:
279:
274:
270:
266:
261:
251:
247:
240:
233:
227:
220:
216:
210:
206:
202:
197:
193:
188:
184:
180:
176:
172:
168:
164:
160:
156:
152:
148:
144:
136:
131:
124:
119:
114:
103:
101:
97:
93:
89:
85:
81:
77:
73:
67:
62:
59:
58:
54:
51:
44:
40:
35:
31:
27:
22:
19:
3154:Translocases
3151:
3138:
3125:
3112:
3099:
3089:Transferases
3086:
3073:
2930:Binding site
2655:
2646:Aminoacylase
2626:Asparaginase
2556:
2496:
2492:
2458:
2454:
2448:
2415:
2411:
2367:
2363:
2321:
2317:
2311:
2276:
2272:
2262:
2227:
2223:
2213:
2176:
2172:
2142:
2138:
2094:
2091:Biochemistry
2090:
2042:
2039:Biochemistry
2038:
1974:
1971:FEBS Letters
1970:
1960:
1925:
1921:
1911:
1876:
1873:Biochemistry
1872:
1862:
1835:
1831:
1821:
1794:
1788:
1777:. Retrieved
1768:
1759:
1722:
1718:
1684:
1675:
1666:
1657:
1597:
1593:
1589:
1584:
1511:
1492:
1455:white matter
1450:
1448:
1408:
1370:
1362:polypeptides
1331:
1306:
1286:
1280:
1268:
1264:
1260:
1242:
1241:
1119:BRENDA entry
981:
963:NP_001121557
956:
930:
912:NM_001128085
905:
881:
862:
836:
817:
791:
772:
752:
747:
526:human kidney
506:right kidney
418:
411:
138:External IDs
69:
18:
2925:Active site
2834:: Nitriles/
2714:Barbiturase
2641:Biotinidase
2631:Glutaminase
1411:nucleophile
1354:active site
1342:amino acids
1299:nucleophile
1107:IntEnz view
1079:Identifiers
377:73,220,422
364:73,195,818
116:Identifiers
3175:Categories
3128:Isomerases
3102:Hydrolases
2969:Regulation
2752:Agmatinase
2669:Ceramidase
2600:Hydrolases
2499:(1): 1–6.
2370:(1): 1–8.
1779:2022-07-22
1769:biocyc.org
1652:, May 2017
1631:, May 2017
1607:References
1598:acylase II
1459:acetyl-CoA
1358:substrates
1346:N-terminal
1247:hydrolytic
1176:structures
1143:KEGG entry
688:metabolism
480:glomerulus
468:C1 segment
422:(ortholog)
276:3,503,405
263:3,472,374
159:HomoloGene
3007:EC number
2845:Nitrilase
2455:Biochimie
2372:CiteSeerX
2145:: 85–91.
1494:Mutations
1467:precursor
1463:synthesis
1423:anhydride
1419:glutamate
1415:aspartate
1405:Mechanism
1328:Structure
1324:disease.
1317:, a rare
1311:Mutations
1291:aspartate
1276:catalyzes
1096:Databases
984:NP_075602
959:NP_000040
933:NM_023113
908:NM_000049
738:Orthologs
667:cytoplasm
167:GeneCards
3186:EC 3.5.1
3031:Kinetics
2955:Cofactor
2918:Activity
2747:Arginase
2521:34211521
2513:22850825
2475:23151389
2440:12255670
2432:16647192
2394:12706335
2346:34902757
2338:11792458
2303:23338456
2295:11520894
2254:36296718
2246:16935940
2205:24421768
2121:18293939
2061:25003821
2009:41351955
2001:17027983
1952:17391648
1928:: 1–14.
1903:16669630
1854:14927637
1773:Archived
1751:17194761
1648:–
1627:–
1538:See also
1483:osmolyte
1431:carbonyl
1338:monomers
1257:3.5.1.15
1231:proteins
1219:articles
1207:articles
1180:RCSB PDB
1090:3.5.1.15
1032:Wikidata
717:Sources:
3141:Ligases
2911:Enzymes
2857:: Other
2689:Sirtuin
2563:PDBe-KB
2553:UniProt
2196:3872778
2112:2666850
1979:Bibcode
1943:1933483
1894:2566822
1742:1766406
1650:Ensembl
1629:Ensembl
1471:neurons
1378:ligated
1340:of 313
1295:acetate
1274:. ASPA
1167:profile
1150:MetaCyc
850:UniProt
805:Ensembl
744:Species
723:QuickGO
672:cytosol
662:nucleus
518:jejunum
397:pattern
255:17p13.2
123:Aliases
3115:Lyases
2855:3.5.99
2658:(ACY2)
2636:Urease
2558:P45381
2544:(MeSH)
2519:
2511:
2473:
2438:
2430:
2392:
2374:
2344:
2336:
2301:
2293:
2252:
2244:
2203:
2193:
2179:: 11.
2119:
2109:
2059:
2007:
1999:
1950:
1940:
1901:
1891:
1852:
1809:
1749:
1739:
1479:myelin
1250:enzyme
1214:PubMed
1196:Search
1186:PDBsum
1126:ExPASy
1114:BRENDA
1102:IntEnz
1085:EC no.
1018:search
1016:PubMed
883:Q8R3P0
864:P45381
760:Entrez
568:BioGPS
147:608034
3067:Types
2832:3.5.5
2815:AICDA
2767:3.5.4
2734:3.5.3
2701:3.5.2
2613:3.5.1
2517:S2CID
2436:S2CID
2342:S2CID
2299:S2CID
2250:S2CID
2005:S2CID
1576:Notes
1400:2O4H.
1376:of a
1334:dimer
1303:brain
1289:into
1245:is a
1162:PRIAM
793:11484
753:Mouse
748:Human
719:Amigo
420:Mouse
413:Human
360:Start
295:Mouse
259:Start
192:Human
155:87914
3159:list
3152:EC7
3146:list
3139:EC6
3133:list
3126:EC5
3120:list
3113:EC4
3107:list
3100:EC3
3094:list
3087:EC2
3081:list
3074:EC1
2662:ACY3
2651:ACY1
2606:3.5)
2551:for
2509:PMID
2471:PMID
2428:PMID
2390:PMID
2334:PMID
2291:PMID
2242:PMID
2201:PMID
2117:PMID
2057:PMID
1997:PMID
1948:PMID
1926:1148
1899:PMID
1850:PMID
1807:ISBN
1747:PMID
1293:and
1272:gene
1269:ASPA
1265:ASPA
1226:NCBI
1183:PDBe
1138:KEGG
403:Bgee
351:Band
312:Chr.
250:Band
209:Chr.
171:ASPA
143:OMIM
130:ASPA
100:4TNU
96:4MXU
92:4NFR
88:2O53
84:2Q51
80:2O4H
76:2I3C
72:4MRI
53:RCSB
50:PDBe
24:ASPA
2549:PDB
2501:doi
2463:doi
2420:doi
2416:252
2382:doi
2368:413
2326:doi
2281:doi
2232:doi
2191:PMC
2181:doi
2147:doi
2143:980
2107:PMC
2099:doi
2047:doi
1987:doi
1975:580
1938:PMC
1930:doi
1889:PMC
1881:doi
1840:doi
1836:194
1799:doi
1737:PMC
1727:doi
1723:104
1596:or
1417:or
1374:pKa
1202:PMC
1174:PDB
774:443
576:n/a
373:End
272:End
175:OMA
151:MGI
43:PDB
3177::
2604:EC
2555::
2515:.
2507:.
2497:36
2495:.
2483:^
2469:.
2459:95
2457:.
2434:.
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1985:.
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1924:.
1920:.
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1683:.
1665:.
1636:^
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1592:,
1263:,
1254:EC
721:/
379:bp
366:bp
278:bp
265:bp
173:;
169::
165:;
163:33
161::
157:;
153::
149:;
145::
98:,
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90:,
86:,
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1981::
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1451:N
1307:N
1285:(
1281:N
1252:(
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177::
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