799:
596:
288:
728:
438:
2793:
1748:
Miller YE, Drabkin H, Jones C, Fisher JH (September 1990). "Human aminoacylase-1: cloning, regional assignment to distal chromosome 3p21.1, and identification of a cross-hybridizing sequence on chromosome 18".
2201:
2194:
179:
2187:
198:
1446:
Mitta M, Ohnogi H, Yamamoto A, Kato I, Sakiyama F, Tsunasawa S (December 1992). "The primary structure of porcine aminoacylase 1 deduced from cDNA sequence".
426:
2430:
2016:
1581:
1736:
2818:
1920:
Tylki-Szymanska A, Gradowska W, Sommer A, et al. (December 2010). "Aminoacylase 1 deficiency associated with autistic behavior".
1601:
2512:
1885:
Van Coster RN, Gerlo EA, Giardina TG, et al. (December 2005). "Aminoacylase I deficiency: a novel inborn error of metabolism".
1530:
Otvös L, Moravcsik E, Mády G (September 1971). "Investigation on the mechanism of acylase-I-catalyzed acylamino acid hydrolysis".
191:
969:
875:
2405:
1959:
Xie Q, Guo T, Wang T, Lu J, Zhou HM (November 2003). "Aspartate-induced aminoacylase folding and forming of molten globule".
1687:"Lack of expression of aminoacylase-1 in small cell lung cancer. Evidence for inactivation of genes encoded by chromosome 3p"
972:
943:
894:
142:
118:
2668:
798:
780:
765:
758:
751:
747:
1642:
Ferri L, Funghini S, Fioravanti A, et al. (October 2013). "Aminoacylase I deficiency due to ACY1 mRNA exon skipping".
2783:
1273:
466:
1058:
739:
705:
693:
462:
458:
2367:
939:
686:
2653:
2769:
2756:
2743:
2730:
2717:
2704:
2691:
2465:
2442:
2377:
2344:
2311:
2223:
1080:
1070:
1062:
1034:
998:
994:
470:
2663:
595:
136:
2617:
2560:
2214:
713:
297:
224:
29:
123:
2565:
2284:
746:
is reversible while the subsequent steps are fast and irreversible. This reaction sequence is an example of
616:
1839:
Sass JO, Olbrich H, Mohr V, et al. (June 2007). "Neurological findings in aminoacylase 1 deficiency".
2109:
1042:
965:
883:
1402:
Lindner HA, Alary A, Wilke M, Sulea T (April 2008). "Probing the acyl-binding pocket of aminoacylase-1".
1315:"Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family"
203:
2586:
2505:
1193:
542:
336:
111:
2658:
1488:
Hernick M, Fierke CA (January 2005). "Zinc hydrolases: the mechanisms of zinc-dependent deacetylases".
2415:
1026:
776:
584:
46:
2073:
Huang MQ, Zhou HM (1994). "Alkaline unfolding and salt-induced folding of aminoacylase at high pH".
531:
2622:
2395:
2294:
2179:
1261:
1006:
979:. This response is evolutionarily advantageous, since a nutrient deficit means there isn't as much
743:
696:
after this point is unknown, with one possibility being that the carbonyl then reforms, breaks the
661:
553:
474:
313:
139:
41:
786:
experiments. The second and third forward steps cause the formation and release of the reaction's
63:
2555:
2420:
1941:
1864:
1667:
1356:"Hydrolysis of N-acyl derivatives of alanine and phenylalanine by acylase I and carboxypeptidase"
1233:
1118:
1054:
924:
446:
2033:
1355:
986:
that needs to be disposed of and since the body wants to salvage as many amino acids as it can.
2149:
Mitta M, Kato I, Tsunasawa S (August 1993). "The nucleotide sequence of human aminoacylase-1".
1789:"Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn error of metabolism"
2813:
2390:
2166:
2131:
2090:
2055:
2012:
1976:
1933:
1902:
1856:
1818:
1766:
1716:
1659:
1624:
1577:
1547:
1505:
1463:
1419:
1377:
1336:
1285:
1249:
1209:
1169:
1161:
1141:
1121:
890:
787:
701:
649:
454:
287:
239:
130:
811:
2601:
2596:
2570:
2498:
2158:
2121:
2082:
2045:
2004:
1968:
1925:
1894:
1848:
1808:
1800:
1758:
1706:
1698:
1651:
1616:
1539:
1497:
1455:
1411:
1367:
1326:
1205:
1189:
1181:
1157:
1145:
868:
565:
538:
727:
99:
2648:
2632:
2545:
2272:
1459:
1084:
772:
572:
549:
500:
348:
2110:"Purification and characterization of a novel aminoacylase from Streptomyces mobaraensis"
75:
34:
2797:
2686:
2627:
2447:
2410:
2382:
2334:
2329:
2316:
2266:
2228:
1852:
1813:
1788:
1253:
1125:
1114:
1110:
1030:
1013:
604:
580:
576:
561:
520:
489:
485:
478:
437:
174:
2050:
1972:
1711:
1686:
1543:
1372:
154:
2807:
2591:
2550:
2474:
2400:
2349:
2162:
1762:
1257:
1185:
1103:
832:
668:
657:
504:
493:
340:
149:
1945:
1868:
1671:
2540:
2236:
1088:
864:
676:
321:
279:
2008:
1999:
Sato, Tadashi; Tosa, Tetsuya (2010). "L-Amino Acids
Production by Aminoacylase".
1620:
2764:
2699:
2535:
2324:
2251:
2241:
1217:
1201:
1165:
1137:
1096:
815:
672:
535:
512:
357:
317:
301:
269:
245:
158:
2792:
1898:
2479:
2362:
2279:
1929:
1501:
1276:
but replicates its function. It can be inferred from this data that these two
1245:
1221:
1213:
1177:
1173:
1153:
1149:
1038:
976:
961:
954:
928:
909:
887:
879:
860:
856:
848:
844:
840:
836:
829:
825:
821:
697:
689:
664:
216:
1313:
Lindner HA, Lunin VV, Alary A, Hecker R, Cygler M, MĂ©nard R (November 2003).
923:) in the body, a process that must be up-regulated during times of increased
735:
The nucleophilic attack by water is the rate-limiting step of aminoacylase's
2738:
2712:
2455:
2210:
1050:
905:
736:
635:
631:
627:
557:
508:
409:
332:
235:
2135:
2059:
1980:
1937:
1906:
1860:
1822:
1663:
1628:
1509:
1423:
1381:
1340:
1331:
1314:
2170:
2094:
1770:
1720:
1551:
1467:
2357:
1092:
1046:
1009:
942:
is up-regulated, producing more N-acetyl-L-glutamate, which up-regulates
852:
679:
2126:
227:
87:
2299:
1281:
1277:
1237:
1002:
980:
947:
932:
917:
913:
546:
450:
106:
2086:
1702:
1655:
1415:
2751:
2521:
2246:
1733:
1241:
1107:
1066:
898:
807:
802:
Aminoacylase's Role in Urea Cycle
Regulation (click for larger image)
783:
721:
682:
422:
352:
344:
328:
231:
186:
82:
70:
58:
2032:
Birnbaum SM, Levintow L, Kingsley RB, Greenstein JP (January 1952).
2151:
Biochimica et
Biophysica Acta (BBA) - Gene Structure and Expression
1804:
2725:
2425:
1269:
1074:
797:
726:
709:
639:
594:
436:
305:
255:
960:
Aminoacylase is up-regulated during times of nutrient deficit or
2289:
2261:
1609:
Biochimica et
Biophysica Acta (BBA) - Molecular Basis of Disease
1197:
1021:
1016:
717:
643:
620:
612:
608:
569:
527:
516:
497:
482:
94:
2494:
2183:
1600:
Sommer A, Christensen E, Schwenger S, et al. (June 2011).
1192:
was developed in the late 1970s that placed aminoacylases in a
2108:
Koreishi M, Asayama F, Imanaka H, et al. (October 2005).
1265:
653:
646:
623:
1961:
286:
1572:
Berg, Jeremy M.; Tymoczko, John L.; Stryer, Lubert (2012).
1240:
have used porcine aminoacylase as their model aminoacylase
2490:
847:, making it more resistant to degradation. Additionally,
599:
Aminoacylase
Reaction Mechanism (click for larger image)
441:
1787:
Sass JO, Mohr V, Olbrich H, et al. (March 2006).
1252:
of porcine aminoacylase have been determined. Porcine
2781:
1136:
Aminoacylases have been used for the production of L-
1576:. New York: W. H. Freeman and Company. p. 688.
2677:
2641:
2610:
2579:
2528:
2464:
2441:
2376:
2343:
2310:
2222:
1887:
1532:
197:
185:
173:
168:
148:
129:
117:
105:
93:
81:
69:
57:
52:
40:
28:
23:
18:
1602:"The molecular basis of aminoacylase 1 deficiency"
1260:subunits each consisting of 406 amino acids, with
731:Michaelis-Menten Kinetics of Aminoacylase Reaction
1077:but seem to recover fully in the next few years.
1880:
1878:
1834:
1832:
1782:
1780:
1595:
1593:
1483:
1481:
1479:
1477:
1397:
1395:
1393:
1391:
1308:
1306:
1304:
1302:
1300:
1156:, aminoacylases can be used to reliably take a
851:cannot be used directly as building blocks for
626:inside of aminoacylase are each coordinated to
1525:
1523:
1521:
1519:
1441:
1439:
1437:
1435:
1433:
1144:since the late 1950s. Since aminoacylases are
1073:often start expressing symptoms shortly after
477:. The associated papers identify two types of
2506:
2195:
8:
1685:Miller YE, Minna JD, Gazdar AF (June 1989).
1204:were then continuously washed through. This
2114:Bioscience, Biotechnology, and Biochemistry
1567:
1565:
1563:
1561:
1188:for many years, a faster and less wasteful
2513:
2499:
2491:
2202:
2188:
2180:
165:
2125:
2049:
1812:
1710:
1371:
1330:
427:urea cycle and metabolism of amino groups
2001:Encyclopedia of Industrial Biotechnology
938:. When amino acid catabolism increases,
2788:
1994:
1992:
1990:
1490:Archives of Biochemistry and Biophysics
1296:
946:and allows it to dispose of the excess
1922:Journal of Inherited Metabolic Disease
1284:, retaining function but diverging in
15:
2431:Activation-induced cytidine deaminase
1691:The Journal of Clinical Investigation
1460:10.1093/oxfordjournals.jbchem.a123968
7:
2034:"Specificity of amino acid acylases"
1106:) that leads to a deficiency in the
931:breakdown produces large amounts of
912:. The urea cycle gets rid of excess
362:. Other names in common use include
2038:The Journal of Biological Chemistry
1360:The Journal of Biological Chemistry
1319:The Journal of Biological Chemistry
806:Aminoacylases are expressed in the
449:have been solved for this class of
1853:10.1212/01.wnl.0000264933.56204.e8
1793:American Journal of Human Genetics
1117:is known for the fact that it can
818:and aid in urea cycle regulation.
14:
2791:
1280:evolved from a common ancestral
1172:- which can then be isolated by
1059:impaired psychomotor development
874:Aminoacylase is involved in the
2213:: carbon-nitrogen non-peptide (
855:and must first be converted to
511:to occur, since aminoacylase's
2406:Inosine monophosphate synthase
1354:Fones WS, Lee M (April 1953).
1065:has also been associated with
973:carbamoyl phosphate synthetase
944:carbamoyl phosphate synthetase
895:carbamoyl phosphate synthetase
1:
2051:10.1016/S0021-9258(18)55898-1
1973:10.1016/S1357-2725(03)00131-6
1544:10.1016/S0006-291X(71)80192-4
1373:10.1016/S0021-9258(18)66242-8
1256:is composed of two identical
469:also correspond to two known
2163:10.1016/0167-4781(93)90116-U
2009:10.1002/9780470054581.eib497
1763:10.1016/0888-7543(90)90237-O
1621:10.1016/j.bbadis.2011.03.005
859:by aminoacylase. Again, the
750:, allowing one to determine
471:primary amino acid sequences
1264:at the N-terminus of each.
1037:results in a dysfunctional
843:provides stability for the
488:- which bind Zn ions - and
2835:
2819:Enzymes of known structure
2368:Protein-arginine deiminase
2290:Fatty acid amide hydrolase
1899:10.1016/j.bbrc.2005.10.126
1268:aminoacylase differs from
940:N-Acetylglutamate synthase
481:comprising aminoacylases:
2669:Michaelis–Menten kinetics
1930:10.1007/s10545-010-9089-3
1502:10.1016/j.abb.2004.08.006
1236:throughout the past half
1081:Aminoacylase 2 deficiency
1029:. The lack of functional
995:Aminoacylase 1 deficiency
863:products can be used for
748:Michaelis–Menten kinetics
667:. The negatively charged
343:, specifically in linear
331:belongs to the family of
164:
2561:Diffusion-limited enzyme
2285:Aspartylglucosaminidase
1448:Journal of Biochemistry
1164:and only convert the L
724:to its original state.
704:. At some point in the
419:short acyl amidoacylase
1924:. 33 Suppl 3: S211–4.
1332:10.1074/jbc.M304233200
1043:neurological disorders
1041:, causing an array of
803:
732:
600:
579:come together to make
442:
415:long acyl amidoacylase
408:alpha-N-acylaminoacid
291:
2654:Eadie–Hofstee diagram
2587:Allosteric regulation
810:, where they recycle
801:
777:substrate specificity
730:
598:
568:structure, meaning 2
515:lies between its two
445:As of late 2007, two
440:
337:carbon-nitrogen bonds
290:
2664:Lineweaver–Burk plot
2416:GTP cyclohydrolase I
2075:Enzyme & Protein
1178:N-acyl-D-amino acids
1154:N-acyl-D-amino acids
1150:N-acyl-L-amino acids
1132:Industrial relevance
975:and the rest of the
966:N-acetyl-L-glutamate
884:N-acetyl-L-glutamate
849:N-acyl-L-amino acids
822:N-acyl-L-amino acids
812:N-acyl-L-amino acids
712:molecule enters and
700:, and forms the two
585:quaternary structure
552:together around the
543:conformational shift
404:L-amino-acid acylase
388:amido acid deacylase
2396:Adenosine deaminase
2295:Histone deacetylase
2127:10.1271/bbb.69.1914
1210:industrial settings
1176:from the unreacted
1142:industrial settings
1007:autosomal recessive
794:Biological function
744:nucleophilic attack
656:, facilitating its
575:and 2 dimerization
536:N-acyl-L-amino acid
364:dehydropeptidase II
358:N-acyl-L-amino acid
302:N-acyl-L-amino acid
300:of this enzyme are
246:N-acyl-L-amino acid
2623:Enzyme superfamily
2556:Enzyme promiscuity
2421:Cytidine deaminase
2380:: Cyclic amidines/
2347:: Linear amidines/
1234:scientific studies
1214:N-acyl-amino acids
1055:mental retardation
925:protein catabolism
804:
733:
603:Aminoacylase is a
601:
443:
335:, those acting on
312:, whereas its two
292:
2779:
2778:
2488:
2487:
2391:Guanine deaminase
2226:: Linear amides /
2087:10.1159/000474993
2018:978-0-470-05458-1
2003:. pp. 1–20.
1703:10.1172/JCI114125
1656:10.1111/cge.12297
1644:Clinical Genetics
1583:978-1-4292-2936-4
1416:10.1021/bi702156h
1325:(45): 44496–504.
1250:primary structure
1212:today to convert
1208:is still used in
1122:N-acetylaspartate
1085:Canavan's disease
990:Disease relevance
968:breakdown, which
833:covalently bonded
619:to function. The
240:chemical reaction
213:
212:
209:
208:
112:metabolic pathway
2826:
2796:
2795:
2787:
2659:Hanes–Woolf plot
2602:Enzyme activator
2597:Enzyme inhibitor
2571:Enzyme catalysis
2515:
2508:
2501:
2492:
2314:: Cyclic amides/
2204:
2197:
2190:
2181:
2175:
2174:
2146:
2140:
2139:
2129:
2105:
2099:
2098:
2070:
2064:
2063:
2053:
2029:
2023:
2022:
1996:
1985:
1984:
1956:
1950:
1949:
1917:
1911:
1910:
1882:
1873:
1872:
1836:
1827:
1826:
1816:
1784:
1775:
1774:
1745:
1739:
1731:
1725:
1724:
1714:
1682:
1676:
1675:
1639:
1633:
1632:
1606:
1597:
1588:
1587:
1569:
1556:
1555:
1527:
1514:
1513:
1485:
1472:
1471:
1443:
1428:
1427:
1399:
1386:
1385:
1375:
1351:
1345:
1344:
1334:
1310:
1272:aminoacylase in
1222:enantiomerically
1083:- also known as
1069:. Patients with
824:are formed when
781:Michaelis-Menten
779:through classic
720:, returning the
675:and attacks the
591:Enzyme mechanism
566:heterotetrameric
545:that brings the
530:facilitates the
492:that facilitate
457:accession codes
433:Enzyme structure
425:participates in
278:
274:
268:
264:
254:
250:
166:
16:
2834:
2833:
2829:
2828:
2827:
2825:
2824:
2823:
2804:
2803:
2802:
2790:
2782:
2780:
2775:
2687:Oxidoreductases
2673:
2649:Enzyme kinetics
2637:
2633:List of enzymes
2606:
2575:
2546:Catalytic triad
2524:
2519:
2489:
2484:
2460:
2448:Aminohydrolases
2446:
2437:
2383:Aminohydrolases
2381:
2372:
2348:
2339:
2317:Amidohydrolases
2315:
2306:
2229:Amidohydrolases
2227:
2218:
2208:
2178:
2148:
2147:
2143:
2120:(10): 1914–22.
2107:
2106:
2102:
2072:
2071:
2067:
2031:
2030:
2026:
2019:
1998:
1997:
1988:
1967:(11): 1558–72.
1958:
1957:
1953:
1919:
1918:
1914:
1884:
1883:
1876:
1838:
1837:
1830:
1786:
1785:
1778:
1747:
1746:
1742:
1732:
1728:
1684:
1683:
1679:
1641:
1640:
1636:
1604:
1599:
1598:
1591:
1584:
1571:
1570:
1559:
1529:
1528:
1517:
1487:
1486:
1475:
1445:
1444:
1431:
1410:(14): 4266–75.
1401:
1400:
1389:
1353:
1352:
1348:
1312:
1311:
1298:
1294:
1230:
1134:
1027:chromosome 3p21
992:
984:
951:
936:
921:
904:
901:that commits NH
867:or catabolized
796:
773:turnover number
769:
762:
755:
593:
573:binding domains
501:binding domains
486:binding domains
435:
349:systematic name
309:
276:
272:
266:
262:
259:
252:
248:
12:
11:
5:
2832:
2830:
2822:
2821:
2816:
2806:
2805:
2801:
2800:
2777:
2776:
2774:
2773:
2760:
2747:
2734:
2721:
2708:
2695:
2681:
2679:
2675:
2674:
2672:
2671:
2666:
2661:
2656:
2651:
2645:
2643:
2639:
2638:
2636:
2635:
2630:
2625:
2620:
2614:
2612:
2611:Classification
2608:
2607:
2605:
2604:
2599:
2594:
2589:
2583:
2581:
2577:
2576:
2574:
2573:
2568:
2563:
2558:
2553:
2548:
2543:
2538:
2532:
2530:
2526:
2525:
2520:
2518:
2517:
2510:
2503:
2495:
2486:
2485:
2483:
2482:
2477:
2471:
2469:
2462:
2461:
2459:
2458:
2452:
2450:
2439:
2438:
2436:
2435:
2434:
2433:
2428:
2418:
2413:
2411:DCMP deaminase
2408:
2403:
2398:
2393:
2387:
2385:
2374:
2373:
2371:
2370:
2365:
2360:
2354:
2352:
2350:Ureohydrolases
2341:
2340:
2338:
2337:
2335:Dihydroorotase
2332:
2330:Beta-lactamase
2327:
2321:
2319:
2308:
2307:
2305:
2304:
2303:
2302:
2292:
2287:
2282:
2277:
2276:
2275:
2270:
2267:Aspartoacylase
2264:
2254:
2249:
2244:
2239:
2233:
2231:
2220:
2219:
2209:
2207:
2206:
2199:
2192:
2184:
2177:
2176:
2141:
2100:
2065:
2024:
2017:
1986:
1951:
1912:
1874:
1847:(24): 2151–3.
1828:
1805:10.1086/500563
1776:
1740:
1726:
1677:
1650:(4): 367–372.
1634:
1589:
1582:
1557:
1538:(5): 1056–64.
1515:
1473:
1429:
1387:
1346:
1295:
1293:
1290:
1254:aminoacylase 1
1229:
1226:
1224:specific way.
1184:was done in a
1133:
1130:
1126:aminoacylase 1
1115:Aminoacylase 2
1111:aminoacylase 2
1031:aminoacylase 1
1014:aminoacylase 1
991:
988:
982:
970:down-regulates
949:
934:
919:
902:
795:
792:
767:
760:
753:
605:metallo-enzyme
592:
589:
581:aminoacylase 1
562:Aminoacylase 1
434:
431:
400:aminoacylase I
392:L-aminoacylase
360:amidohydrolase
307:
296:Thus, the two
294:
293:
283:
282:
257:
211:
210:
207:
206:
201:
195:
194:
189:
183:
182:
177:
171:
170:
162:
161:
152:
146:
145:
134:
127:
126:
121:
115:
114:
109:
103:
102:
97:
91:
90:
85:
79:
78:
73:
67:
66:
61:
55:
54:
50:
49:
44:
38:
37:
32:
26:
25:
21:
20:
13:
10:
9:
6:
4:
3:
2:
2831:
2820:
2817:
2815:
2812:
2811:
2809:
2799:
2794:
2789:
2785:
2771:
2767:
2766:
2761:
2758:
2754:
2753:
2748:
2745:
2741:
2740:
2735:
2732:
2728:
2727:
2722:
2719:
2715:
2714:
2709:
2706:
2702:
2701:
2696:
2693:
2689:
2688:
2683:
2682:
2680:
2676:
2670:
2667:
2665:
2662:
2660:
2657:
2655:
2652:
2650:
2647:
2646:
2644:
2640:
2634:
2631:
2629:
2628:Enzyme family
2626:
2624:
2621:
2619:
2616:
2615:
2613:
2609:
2603:
2600:
2598:
2595:
2593:
2592:Cooperativity
2590:
2588:
2585:
2584:
2582:
2578:
2572:
2569:
2567:
2564:
2562:
2559:
2557:
2554:
2552:
2551:Oxyanion hole
2549:
2547:
2544:
2542:
2539:
2537:
2534:
2533:
2531:
2527:
2523:
2516:
2511:
2509:
2504:
2502:
2497:
2496:
2493:
2481:
2480:Thiaminase II
2478:
2476:
2475:Riboflavinase
2473:
2472:
2470:
2467:
2463:
2457:
2454:
2453:
2451:
2449:
2444:
2440:
2432:
2429:
2427:
2424:
2423:
2422:
2419:
2417:
2414:
2412:
2409:
2407:
2404:
2402:
2401:AMP deaminase
2399:
2397:
2394:
2392:
2389:
2388:
2386:
2384:
2379:
2375:
2369:
2366:
2364:
2361:
2359:
2356:
2355:
2353:
2351:
2346:
2342:
2336:
2333:
2331:
2328:
2326:
2323:
2322:
2320:
2318:
2313:
2309:
2301:
2298:
2297:
2296:
2293:
2291:
2288:
2286:
2283:
2281:
2278:
2274:
2271:
2268:
2265:
2263:
2260:
2259:
2258:
2255:
2253:
2250:
2248:
2245:
2243:
2240:
2238:
2235:
2234:
2232:
2230:
2225:
2221:
2216:
2212:
2205:
2200:
2198:
2193:
2191:
2186:
2185:
2182:
2172:
2168:
2164:
2160:
2156:
2152:
2145:
2142:
2137:
2133:
2128:
2123:
2119:
2115:
2111:
2104:
2101:
2096:
2092:
2088:
2084:
2081:(4): 229–37.
2080:
2076:
2069:
2066:
2061:
2057:
2052:
2047:
2044:(1): 455–70.
2043:
2039:
2035:
2028:
2025:
2020:
2014:
2010:
2006:
2002:
1995:
1993:
1991:
1987:
1982:
1978:
1974:
1970:
1966:
1962:
1955:
1952:
1947:
1943:
1939:
1935:
1931:
1927:
1923:
1916:
1913:
1908:
1904:
1900:
1896:
1893:(3): 1322–6.
1892:
1888:
1881:
1879:
1875:
1870:
1866:
1862:
1858:
1854:
1850:
1846:
1842:
1835:
1833:
1829:
1824:
1820:
1815:
1810:
1806:
1802:
1798:
1794:
1790:
1783:
1781:
1777:
1772:
1768:
1764:
1760:
1757:(1): 149–54.
1756:
1752:
1744:
1741:
1738:
1735:
1730:
1727:
1722:
1718:
1713:
1708:
1704:
1700:
1697:(6): 2120–4.
1696:
1692:
1688:
1681:
1678:
1673:
1669:
1665:
1661:
1657:
1653:
1649:
1645:
1638:
1635:
1630:
1626:
1622:
1618:
1615:(6): 685–90.
1614:
1610:
1603:
1596:
1594:
1590:
1585:
1579:
1575:
1568:
1566:
1564:
1562:
1558:
1553:
1549:
1545:
1541:
1537:
1533:
1526:
1524:
1522:
1520:
1516:
1511:
1507:
1503:
1499:
1495:
1491:
1484:
1482:
1480:
1478:
1474:
1469:
1465:
1461:
1457:
1454:(6): 737–42.
1453:
1449:
1442:
1440:
1438:
1436:
1434:
1430:
1425:
1421:
1417:
1413:
1409:
1405:
1398:
1396:
1394:
1392:
1388:
1383:
1379:
1374:
1369:
1366:(2): 847–56.
1365:
1361:
1357:
1350:
1347:
1342:
1338:
1333:
1328:
1324:
1320:
1316:
1309:
1307:
1305:
1303:
1301:
1297:
1291:
1289:
1287:
1283:
1279:
1275:
1271:
1267:
1263:
1262:acetylalanine
1259:
1258:heterodimeric
1255:
1251:
1248:sequence and
1247:
1243:
1239:
1235:
1227:
1225:
1223:
1219:
1215:
1211:
1207:
1203:
1199:
1195:
1191:
1187:
1186:batch reactor
1183:
1180:. While this
1179:
1175:
1171:
1167:
1163:
1160:of these two
1159:
1155:
1151:
1148:specific for
1147:
1143:
1139:
1131:
1129:
1127:
1123:
1120:
1116:
1112:
1109:
1105:
1104:chromosome 17
1101:
1099:
1094:
1090:
1087:- is another
1086:
1082:
1078:
1076:
1072:
1068:
1064:
1060:
1056:
1052:
1048:
1044:
1040:
1036:
1032:
1028:
1024:
1023:
1018:
1015:
1011:
1008:
1005:caused by an
1004:
1000:
996:
989:
987:
985:
978:
974:
971:
967:
963:
958:
956:
952:
945:
941:
937:
930:
926:
922:
915:
911:
907:
900:
896:
892:
889:
885:
881:
877:
872:
870:
866:
862:
858:
857:L-amino acids
854:
850:
846:
842:
838:
834:
831:
827:
826:L-amino acids
823:
819:
817:
816:L-amino acids
813:
809:
800:
793:
791:
789:
785:
782:
778:
774:
770:
763:
756:
749:
745:
741:
738:
729:
725:
723:
719:
715:
711:
707:
703:
699:
695:
691:
688:
684:
681:
678:
677:electrophilic
674:
670:
669:hydroxide ion
666:
663:
659:
658:deprotonation
655:
651:
648:
645:
641:
637:
633:
629:
625:
622:
618:
614:
610:
606:
597:
590:
588:
586:
582:
578:
574:
571:
567:
563:
559:
556:and allowing
555:
551:
548:
544:
540:
537:
533:
529:
524:
522:
518:
514:
510:
506:
503:. It is this
502:
499:
495:
491:
487:
484:
480:
476:
475:aminoacylases
472:
468:
464:
460:
456:
452:
448:
439:
432:
430:
428:
424:
420:
416:
412:
411:
405:
401:
397:
393:
389:
385:
381:
377:
373:
369:
365:
361:
359:
354:
350:
346:
342:
341:peptide bonds
338:
334:
330:
325:
323:
319:
315:
311:
303:
299:
289:
285:
284:
281:
271:
261:
247:
244:
243:
242:
241:
237:
233:
229:
226:
222:
218:
205:
202:
200:
196:
193:
190:
188:
184:
181:
178:
176:
172:
167:
163:
160:
156:
153:
151:
150:Gene Ontology
147:
144:
141:
138:
135:
132:
128:
125:
122:
120:
116:
113:
110:
108:
104:
101:
98:
96:
92:
89:
88:NiceZyme view
86:
84:
80:
77:
74:
72:
68:
65:
62:
60:
56:
51:
48:
45:
43:
39:
36:
33:
31:
27:
22:
17:
2765:Translocases
2762:
2749:
2736:
2723:
2710:
2700:Transferases
2697:
2684:
2541:Binding site
2257:Aminoacylase
2256:
2237:Asparaginase
2157:(2): 201–3.
2154:
2150:
2144:
2117:
2113:
2103:
2078:
2074:
2068:
2041:
2037:
2027:
2000:
1964:
1960:
1954:
1921:
1915:
1890:
1886:
1844:
1840:
1799:(3): 401–9.
1796:
1792:
1754:
1750:
1743:
1729:
1694:
1690:
1680:
1647:
1643:
1637:
1612:
1608:
1574:Biochemistry
1573:
1535:
1531:
1496:(1): 71–84.
1493:
1489:
1451:
1447:
1407:
1404:Biochemistry
1403:
1363:
1359:
1349:
1322:
1318:
1231:
1135:
1097:
1091:caused by a
1089:rare disease
1079:
1020:
1001:) is a rare
993:
959:
897:, a crucial
873:
865:biosynthesis
861:L-amino acid
820:
805:
734:
692:. The exact
673:nucleophilic
660:by a nearby
602:
564:exists in a
541:, causing a
525:
507:that allows
505:dimerization
494:dimerization
444:
418:
414:
407:
403:
399:
395:
391:
387:
383:
379:
375:
371:
367:
363:
356:
326:
322:L-amino acid
295:
280:L-amino acid
221:aminoacylase
220:
214:
76:BRENDA entry
19:aminoacylase
2536:Active site
2445:: Nitriles/
2325:Barbiturase
2252:Biotinidase
2242:Glutaminase
1288:over time.
1218:amino acids
1202:amino acids
1166:enantiomers
1138:amino acids
1049:, muscular
828:have their
714:coordinates
687:substrate's
607:that needs
513:active site
376:benzamidase
372:hippuricase
339:other than
318:carboxylate
270:carboxylate
64:IntEnz view
24:Identifiers
2808:Categories
2739:Isomerases
2713:Hydrolases
2580:Regulation
2363:Agmatinase
2280:Ceramidase
2211:Hydrolases
1734:EntrezGene
1292:References
1246:amino acid
1174:solubility
1045:including
1039:urea cycle
1033:caused by
977:urea cycle
964:, causing
962:starvation
955:catabolism
929:amino acid
910:urea cycle
888:allosteric
880:urea cycle
876:regulation
845:amino acid
841:acyl group
837:acyl group
830:N-terminus
708:, another
698:amide bond
690:acyl group
560:to occur.
467:structures
447:structures
333:hydrolases
298:substrates
217:enzymology
133:structures
100:KEGG entry
47:9012-37-7
2618:EC number
2456:Nitrilase
1841:Neurology
1286:structure
1274:structure
1228:Evolution
1162:reactants
1146:substrate
1119:hydrolyze
1051:hypotonia
906:molecules
891:activator
740:mechanism
737:catalytic
706:mechanism
694:mechanism
650:polarizes
636:aspartate
632:glutamate
628:histidine
558:catalysis
554:substrate
547:protein's
539:substrate
509:catalysis
410:hydrolase
384:hippurase
380:acylase I
368:histozyme
355:class is
236:catalyzes
53:Databases
2814:EC 3.5.1
2642:Kinetics
2566:Cofactor
2529:Activity
2358:Arginase
2136:16244442
2060:14927637
1981:12824065
1946:13374954
1938:20480396
1907:16274666
1869:43376960
1861:17562838
1823:16465618
1751:Genomics
1672:24017306
1664:24117009
1629:21414403
1510:15581567
1424:18341290
1382:13061423
1341:12933810
1170:products
1152:and not
1128:cannot.
1093:mutation
1047:seizures
1010:mutation
853:proteins
788:products
702:products
680:carbonyl
617:cofactor
550:subunits
519:binding
465:. These
421:. This
351:of this
314:products
230:) is an
228:3.5.1.14
204:proteins
192:articles
180:articles
137:RCSB PDB
35:3.5.1.14
2798:Biology
2752:Ligases
2522:Enzymes
2468:: Other
2300:Sirtuin
2171:8357837
2095:8821711
1814:1380284
1771:1707030
1721:2542383
1552:5160398
1468:1284246
1282:protein
1278:enzymes
1266:Porcine
1238:century
1206:process
1196:that N-
1190:process
1182:process
1158:mixture
1095:in the
1012:in the
1003:disease
914:ammonia
908:to the
878:of the
742:. This
685:of the
665:residue
615:) as a
577:domains
534:of the
532:binding
521:domains
490:domains
479:domains
453:, with
451:enzymes
396:acylase
347:. The
159:QuickGO
124:profile
107:MetaCyc
42:CAS no.
2784:Portal
2726:Lyases
2466:3.5.99
2269:(ACY2)
2247:Urease
2169:
2134:
2093:
2058:
2015:
1979:
1944:
1936:
1905:
1867:
1859:
1821:
1811:
1769:
1719:
1712:303939
1709:
1670:
1662:
1627:
1580:
1550:
1508:
1466:
1422:
1380:
1339:
1244:. The
1242:enzyme
1220:in an
1194:column
1124:while
1108:enzyme
1067:autism
1057:, and
899:enzyme
886:is an
869:energy
839:. The
835:to an
808:kidney
784:enzyme
775:, and
722:enzyme
683:carbon
642:. The
638:, and
526:Bound
423:enzyme
417:, and
353:enzyme
345:amides
329:enzyme
277:
273:
267:
263:
253:
249:
232:enzyme
187:PubMed
169:Search
155:AmiGO
143:PDBsum
83:ExPASy
71:BRENDA
59:IntEnz
30:EC no.
2678:Types
2443:3.5.5
2426:AICDA
2378:3.5.4
2345:3.5.3
2312:3.5.2
2224:3.5.1
1942:S2CID
1865:S2CID
1668:S2CID
1605:(PDF)
1270:human
1232:Many
1168:into
1075:birth
1025:) on
953:from
927:, as
716:with
710:water
662:basic
654:water
640:water
327:This
234:that
219:, an
119:PRIAM
2770:list
2763:EC7
2757:list
2750:EC6
2744:list
2737:EC5
2731:list
2724:EC4
2718:list
2711:EC3
2705:list
2698:EC2
2692:list
2685:EC1
2273:ACY3
2262:ACY1
2217:3.5)
2167:PMID
2155:1174
2132:PMID
2091:PMID
2056:PMID
2013:ISBN
1977:PMID
1934:PMID
1903:PMID
1857:PMID
1819:PMID
1767:PMID
1717:PMID
1660:PMID
1625:PMID
1613:1812
1578:ISBN
1548:PMID
1506:PMID
1464:PMID
1420:PMID
1378:PMID
1337:PMID
1198:acyl
1102:(on
1100:gene
1098:ASPA
1022:ACY1
1017:gene
718:Zinc
652:the
644:Zinc
624:ions
621:Zinc
609:Zinc
570:Zinc
528:Zinc
517:Zinc
498:Zinc
483:Zinc
473:for
463:1YSJ
461:and
459:1Q7L
320:and
316:are
304:and
238:the
199:NCBI
140:PDBe
95:KEGG
2159:doi
2122:doi
2083:doi
2046:doi
2042:194
2005:doi
1969:doi
1926:doi
1895:doi
1891:338
1849:doi
1809:PMC
1801:doi
1759:doi
1707:PMC
1699:doi
1652:doi
1617:doi
1540:doi
1498:doi
1494:433
1456:doi
1452:112
1412:doi
1368:doi
1364:201
1327:doi
1323:278
1216:to
1140:in
1071:A1D
1063:A1D
1035:A1D
999:A1D
893:of
814:as
768:max
761:cat
671:is
647:ion
583:'s
496:of
455:PDB
275:+
265:⇌
215:In
175:PMC
131:PDB
2810::
2215:EC
2165:.
2153:.
2130:.
2118:69
2116:.
2112:.
2089:.
2079:48
2077:.
2054:.
2040:.
2036:.
2011:.
1989:^
1975:.
1965:35
1963:.
1940:.
1932:.
1901:.
1889:.
1877:^
1863:.
1855:.
1845:68
1843:.
1831:^
1817:.
1807:.
1797:78
1795:.
1791:.
1779:^
1765:.
1753:.
1737:95
1715:.
1705:.
1695:83
1693:.
1689:.
1666:.
1658:.
1648:86
1646:.
1623:.
1611:.
1607:.
1592:^
1560:^
1546:.
1536:44
1534:.
1518:^
1504:.
1492:.
1476:^
1462:.
1450:.
1432:^
1418:.
1408:47
1406:.
1390:^
1376:.
1362:.
1358:.
1335:.
1321:.
1317:.
1299:^
1113:.
1061:.
1053:,
981:NH
957:.
948:NH
933:NH
918:NH
882:.
871:.
790:.
771:,
764:,
757:,
634:,
630:,
613:Zn
587:.
523:.
429:.
413:,
406:,
402:,
398:,
394:,
390:,
386:,
382:,
378:,
374:,
370:,
366:,
324:.
251:+
225:EC
157:/
2786::
2772:)
2768:(
2759:)
2755:(
2746:)
2742:(
2733:)
2729:(
2720:)
2716:(
2707:)
2703:(
2694:)
2690:(
2514:e
2507:t
2500:v
2203:e
2196:t
2189:v
2173:.
2161::
2138:.
2124::
2097:.
2085::
2062:.
2048::
2021:.
2007::
1983:.
1971::
1948:.
1928::
1909:.
1897::
1871:.
1851::
1825:.
1803::
1773:.
1761::
1755:8
1723:.
1701::
1674:.
1654::
1631:.
1619::
1586:.
1554:.
1542::
1512:.
1500::
1470:.
1458::
1426:.
1414::
1384:.
1370::
1343:.
1329::
1200:-
1019:(
997:(
983:4
950:4
935:4
920:4
916:(
903:4
766:V
759:K
754:M
752:K
611:(
310:O
308:2
306:H
260:O
258:2
256:H
223:(
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.