959:. The "closed" position opens up the channel between CODH and ACS to allow for the transfer of CO. These two configurations are opposite one another in that access to CO blocks off interaction with CFeSP, and when methylation occurs, the active site is buried and does not allow CO transfer. A second "closed" position is needed to block off water from the reaction. Finally, the A-cluster must be rotated once more to allow for the binding of CoA and release of the product. The exact trigger of these structural changes and the mechanistic details have yet to be resolved.
648:
973:
910:
2390:
40:
816:
743:
was presented in 2002 by
Drennan and colleagues. In this paper they constructed a heterotetramer, with the active site "A-cluster" residing in the ACS subunit and the active site "C-cluster" in CODH subunit. Furthermore, they resolved the structure of the A-cluster active site and found an -X-Cu-X-Ni
1043:
to produce the metal-acetyl complex, CoA attacks to produce the final product. The order in which the carbon monoxide molecule and the methyl group bind to the nickel centre has been highly debated, but no solid evidence has demonstrated preference for one over the other. Although this mechanism is
874:
in the surrounding area in the cell. Although the proximal nickel is labile and can be replaced with a Cu of Zn centre, experimental evidence suggests that activity of ACS is limited to the presence of nickel only. In addition, some studies have shown that copper can even inhibit the enzyme under
954:
Studies in literature have been able to isolate the CODH/ACS enzyme in an "open" and "closed" configuration. This has led to the hypothesis that it undergoes four conformational changes depending on its activity. With the "open" position, the active site rotates itself to interact with the CFeSP
771:
The debate towards the absolute structure and identity of the metals in the A-cluster active site of ACS continued, with a competing model presented. The authors suggested two different forms of the ACS enzyme, an "Open" form and a "Closed" form, with different metals occupying the
945:
channel connecting the two domains to allow for the transfer of carbon monoxide from CODH to ACS. This channel is most likely to protect the carbon monoxide molecules from the outside environment of the enzyme and to increase efficiency of acetyl-CoA production.
882:
at the centre with two ACS subunits on each side. The CODH core is made up of two Ni-Fe-S clusters (C-cluster), two clusters (B-cluster) and one D-cluster. The D-cluster bridges the two subunits with one C and one B cluster in each monomer, allowing rapid
665:. Since the above two reactions are reversible, it opens up a diverse range of reactions in the carbon cycle. In addition to acetyl-CoA production, the reverse can occur with ACS producing CO and returning the methyl piece back to the corrinoid protein.
1027:
to form an intermediate complex. CoA then binds to the metal and the final product, acetyl-CoA, is formed. Some criticisms of this mechanism are that it is unbalanced in terms of electron count and the activated Ni intermediate cannot be detected with
917:
The ACS enzyme contains three main subunits. The first is the active site itself with the NiFeS centre. The second is the portion that directly interacts with CODH in the Wood–Ljungdahl pathway. This part is made up of
598:
887:. The A-cluster of ACS is in constant communication with the C-cluster in CODH. This active site is also responsible for the C-C and C-S bond formations in the product acetyl-CoA (and its reverse reaction).
465:
1486:"Gas channel rerouting in a primordial enzyme: Structural insights of the carbon-monoxide dehydrogenase/acetyl-CoA synthase complex from the acetogen Clostridium autoethanogenum"
1636:"Pulse-chase studies of the synthesis of acetyl-CoA by carbon monoxide dehydrogenase/acetyl-CoA synthase: evidence for a random mechanism of methyl and carbonyl addition"
1039:
The second proposed mechanism, the diamagnetic mechanism, involves a Ni intermediate instead of a Ni. After addition of the methyl group and carbon monoxide, followed by
193:
1312:
Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL (October 2002). "A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase".
212:
1926:
1921:
744:
centre which is highly unusual in biology. This structural representation consisted of a unit bridged to a binuclear centre, where Ni(II) resided in the
1727:
1044:
electronically balanced, the idea of a Ni species is highly unprecedented in biology. There has also been no solid evidence supporting the presence of a
672:, organisms can subsequently convert the acetate to methane. Furthermore, the Wood-Ljungdahl pathway allows for the anaerobic oxidation of acetate where
1909:
1228:
Riordan CG (July 2004). "Synthetic chemistry and chemical precedents for understanding the structure and function of acetyl coenzyme A synthase".
1366:
Drennan CL, Doukov TI, Ragsdale SW (July 2004). "The metalloclusters of carbon monoxide dehydrogenase/acetyl-CoA synthase: a story in pictures".
488:
1916:
2415:
1694:
676:
is used to convert acetate into acetyl-CoA, which is then broken down by ACS to produce carbon dioxide that is released into the atmosphere.
930:
compound which may activate the subunit during the CO transferring process from CODH to ACS. The final domain binds CoA and consists of six
1904:
2076:
2044:
780:) for each form. The general scheme of the enzyme followed closely with the first study's findings, but this new structure proposed a
2109:
1860:
1798:
336:
205:
1855:
1850:
1793:
1029:
156:
1808:
1720:
132:
2265:
1973:
1953:
1867:
325:
296:
as a result. Because of this, the exact activity of these molecules has come under intense scrutiny over the past decade.
289:
241:
2380:
1894:
1788:
1783:
826:
It is now generally accepted that the ACS active site (A-cluster) is a Ni-Ni metal centre with both nickels having a +2
795:
and stated that this proximal position in the active site of ACS was prone to substitution and could contain any one of
2056:
1830:
1032:. Furthermore, there is evidence of the ACS catalytic cycle without any external reducing complex, which refutes the
956:
305:
285:
257:
647:
2066:
1899:
1773:
2250:
972:
2366:
2353:
2340:
2327:
2314:
2301:
2288:
2014:
1990:
1941:
1825:
1778:
1753:
1713:
150:
2260:
807:. The three forms of this A-cluster most likely hold a small amount of Ni and a relatively larger amount of Cu.
2214:
2157:
2019:
1744:
866:
is in a T-shaped environment bound to three sulfur atoms, with an unknown ligand possibly creating a distorted
308:
consists of two different reactions that break down carbon dioxide. The first pathway involves CODH converting
244:(CODH), it forms the bifunctional enzyme Acetyl-CoA Synthase/Carbon Monoxide Dehydrogenase (ACS/CODH) found in
55:
137:
2162:
2061:
1968:
1274:
Ragsdale SW, Kumar M (January 1996). "Nickel-Containing Carbon
Monoxide Dehydrogenase/Acetyl-CoA Synthase".
1143:"Structure, function, and mechanism of the nickel metalloenzymes, CO dehydrogenase, and acetyl-CoA synthase"
1071:
Lindahl PA (July 2004). "Acetyl-coenzyme A synthase: the case for a Ni(p)(0)-based mechanism of catalysis".
988:
mechanism". Both are similar in terms of the binding of substrates and the general steps, but differ in the
2029:
2024:
1889:
673:
217:
898:
have been solved. While the latter shows a more extended arrangement of the ACS subunits, the complex of
125:
2183:
2102:
2009:
2004:
233:
2255:
1023:
from CODH or the methyl group donated by the CFeSP protein in no particular order. This is followed by
1528:
2071:
1958:
1945:
1845:
1321:
153:
2219:
1803:
1040:
1024:
1001:
831:
77:
1443:
Ruickoldt, Jakob; Basak, Yudhajeet; Domnik, Lilith; Jeoung, Jae-Hun; Dobbek, Holger (2022-10-21).
2152:
1485:
1391:
1345:
1253:
1096:
245:
1193:
Hegg EL (October 2004). "Unraveling the structure and mechanism of acetyl-coenzyme A synthase".
1529:"A role for nickel-iron cofactors in biological carbon monoxide and carbon dioxide utilization"
739:
The first, and one of the most comprehensive, crystal structures of ACS/CODH from the bacteria
640:
convert the acetyl-CoA into acetate and use it as an alternative source of carbon instead of CO
620:
produced can be used in a variety of ways depending on the needs of the organism. For example,
2410:
2034:
1763:
1690:
1667:
1613:
1561:
1466:
1383:
1337:
1291:
1245:
1210:
1172:
1088:
976:
Proposed diamagnetic (top) and paramagnetic (bottom) mechanisms. Adapted from
Seravalli et al.
884:
879:
144:
2198:
2193:
2167:
2095:
1999:
1963:
1657:
1647:
1603:
1595:
1551:
1543:
1507:
1497:
1456:
1425:
1375:
1329:
1283:
1237:
1202:
1162:
1154:
1080:
113:
1048:
Ni species. However, similar nickel species to ACS with a Ni centre have been made, so the
909:
2245:
2229:
2142:
2039:
1740:
1705:
1020:
827:
709:
321:
313:
89:
292:(CODH) are integral enzymes in this one pathway and can perform diverse reactions in the
60:
1325:
2394:
2283:
2224:
1662:
1635:
1608:
1583:
1556:
1167:
1142:
701:
669:
633:
309:
261:
188:
168:
2404:
2188:
2147:
1512:
1008:
923:
862:
coordination. The space next to the metal can accommodate substrates and products. Ni
859:
753:
697:
163:
1444:
1395:
1349:
1100:
2137:
1257:
1049:
981:
871:
621:
316:
through a two-electron transfer, and the second reaction involves ACS synthesizing
293:
17:
980:
Two competing mechanisms have been proposed for the formation of acetyl-CoA, the "
941:
Experiments between the C-cluster of CODH and the A-cluster of ACS reveal a long,
1502:
2361:
2296:
2132:
1978:
1736:
985:
942:
919:
867:
761:
717:
662:
172:
2389:
1547:
288:
is the predominant sink in anaerobic conditions. Acetyl-CoA Synthase (ACS) and
240:-containing enzyme involved in the metabolic processes of cells. Together with
1599:
1429:
1379:
1241:
1084:
1045:
1033:
1012:
935:
927:
878:
The overall structure of the CODH/ACS enzyme consists of the CODH enzyme as a
723:
689:
658:
651:
625:
617:
317:
265:
1470:
1461:
791:
A later review article attempted to reconcile the different observations of M
2335:
2309:
1333:
989:
870:
environment. This ligand has been hypothesized to be a water molecule or an
713:
705:
629:
593:{\displaystyle {\ce {{CO}+ {CH3-CFeSP}+ CoA <=> {acetyl-CoA}+ CFeSP}}}
1671:
1652:
1617:
1565:
1387:
1341:
1295:
1249:
1214:
1176:
1092:
1416:
Evans DJ (2005). "Chemistry relating to the nickel enzymes CODH and ACS".
39:
1768:
931:
851:
839:
773:
757:
253:
101:
249:
120:
1206:
1158:
2348:
2118:
2049:
1877:
1872:
1813:
1287:
804:
796:
781:
765:
745:
237:
200:
96:
84:
72:
815:
1629:
1627:
654:
growth via the Wood–Ljungdahl pathway. Adapted from
Ragsdale et al.
324:
from CODH together with coenzyme-A (CoA) and a methyl group from a
2322:
1931:
1818:
997:
971:
908:
855:
814:
646:
1019:
atom, reducing it from Ni to Ni. The nickel then binds to either
1835:
1136:
1134:
1132:
1130:
1128:
1126:
1124:
800:
785:
684:
It has been discovered that the CODH/ACS enzyme in the bacteria
108:
2091:
1709:
1445:"On the Kinetics of CO 2 Reduction by Ni, Fe-CO Dehydrogenases"
996:
is believed to be the substrate binding centre which undergoes
890:
Furthermore, the crystal structures of the CODH/ACS complex of
460:{\displaystyle {\ce {{CO2}+ {2H+}+ 2e^- <=> {CO}+ H2O}}}
1689:. Chichester, West Sussex, England: Wiley. pp. 377–380.
1361:
1359:
2087:
1307:
1305:
512:
450:
352:
1577:
1575:
1269:
1267:
328:, CFeSP. The two main overall reactions are as follows:
551:
413:
2378:
1582:
Boer JL, Mulrooney SB, Hausinger RP (February 2014).
1484:
Lemaire, Olivier N.; Wagner, Tristan (January 2021).
491:
339:
1188:
1186:
280:
In nature, there are six different pathways where CO
2274:
2238:
2207:
2176:
2125:
1989:
1940:
1752:
1490:
Biochimica et
Biophysica Acta (BBA) - Bioenergetics
211:
199:
187:
182:
162:
143:
131:
119:
107:
95:
83:
71:
66:
54:
49:
32:
592:
459:
256:. The ACS/CODH enzyme works primarily through the
661:bacteria use this method to generate acetate and
559:
558:
541:
540:
421:
420:
403:
402:
1411:
1409:
1407:
1405:
1141:Can M, Armstrong FA, Ragsdale SW (April 2014).
1004:are not thought to be involved in the process.
1066:
1064:
2103:
1721:
8:
1927:2-acylglycerol-3-phosphate O-acyltransferase
1922:1-acylglycerol-3-phosphate O-acyltransferase
1052:mechanism is not an implausible hypothesis.
756:conformation and a Cu(I) ion resided in the
955:protein in the methyl transfer step of the
2110:
2096:
2088:
1728:
1714:
1706:
1687:Nickel and its surprising impact in nature
268:. The recommended name for this enzyme is
236:or acetate-CoA ligase (ADP forming), is a
179:
38:
1661:
1651:
1607:
1555:
1511:
1501:
1460:
1368:Journal of Biological Inorganic Chemistry
1230:Journal of Biological Inorganic Chemistry
1166:
1073:Journal of Biological Inorganic Chemistry
913:Acetyl-CoA Synthase active site structure
574:
570:
560:
553:
552:
550:
542:
535:
533:
532:
530:
515:
511:
506:
501:
493:
492:
490:
449:
444:
432:
422:
415:
414:
412:
404:
397:
395:
394:
392:
386:
381:
368:
363:
359:
351:
346:
341:
340:
338:
2385:
1634:Seravalli J, Ragsdale SW (March 2008).
1588:Archives of Biochemistry and Biophysics
1060:
534:
396:
1917:Glycerol-3-phosphate O-acyltransferase
29:
1910:Lecithin—cholesterol acyltransferase
1000:. The farther nickel centre and the
926:. It also appears to interact with a
7:
1905:Glyceronephosphate O-acyltransferase
482:
330:
2077:Sulfoacetaldehyde acetyltransferase
1769:Acetyl-Coenzyme A acetyltransferase
1685:Sigel A, Sigel H, Sigel RK (2006).
1640:The Journal of Biological Chemistry
1536:Current Opinion in Chemical Biology
1993:: converted into alkyl on transfer
834:is bridged to the closer nickel, N
270:CO-methylating acetyl-CoA synthase
33:CO-methylating acetyl-CoA synthase
25:
1799:Chloramphenicol acetyltransferase
1584:"Nickel-dependent metalloenzymes"
1527:Kung Y, Drennan CL (April 2011).
1117:. Vol. 30. pp. 459–466.
1011:mechanism, some type of complex (
892:Carboxydothermus hydrogenoformans
2388:
1851:Carnitine O-palmitoyltransferase
842:bridge to the farther nickel, Ni
1794:Beta-galactoside transacetylase
1030:electron paramagnetic resonance
1015:, for example) activates the Ni
232:(ACS), not to be confused with
1809:Serotonin N-acetyl transferase
1756:: other than amino-acyl groups
1418:Coordination Chemistry Reviews
819:Bifunctional CODH/ACS unit in
561:
536:
423:
398:
1:
1974:Keratinocyte transglutaminase
1954:Gamma-glutamyl transpeptidase
1868:Serine C-palmitoyltransferase
1195:Accounts of Chemical Research
992:state of the metal centre. Ni
784:ion in the "open" form and a
326:corrinoid iron-sulfur protein
290:carbon monoxide dehydrogenase
242:carbon monoxide dehydrogenase
44:Monomeric Acetyl-CoA synthase
2416:Enzymes of unknown structure
1895:Aminolevulinic acid synthase
1789:Acetyl-CoA C-acyltransferase
1784:Dihydrolipoyl transacetylase
1503:10.1016/j.bbabio.2020.148330
1115:Springer handbook of enzymes
2057:2-hydroxyglutarate synthase
902:is very similar to that of
896:Clostridium autoethanogenum
854:molecules and two backbone
704:. It can also catalyze the
2432:
2067:2-isopropylmalate synthase
1900:Beta-ketoacyl-ACP synthase
1774:N-Acetylglutamate synthase
1548:10.1016/j.cbpa.2010.11.005
788:ion in the "closed" form.
668:Along with the process of
2266:Michaelis–Menten kinetics
2015:Decylhomocitrate synthase
1826:Histone acetyltransferase
1779:Choline acetyltransferase
1600:10.1016/j.abb.2013.09.002
1513:21.11116/0000-0007-F1AD-6
1430:10.1016/j.ccr.2004.09.012
1380:10.1007/s00775-004-0563-y
1242:10.1007/s00775-004-0567-7
1085:10.1007/s00775-004-0564-x
838:which is connected via a
702:electron-donating species
178:
37:
2158:Diffusion-limited enzyme
2020:2-methylcitrate synthase
1462:10.1021/acscatal.2c02221
776:metal site (denoted as M
760:position in a distorted
622:acetate-forming bacteria
284:is fixed. Of these, the
246:anaerobic microorganisms
2062:3-propylmalate synthase
1969:Tissue transglutaminase
1334:10.1126/science.1075843
858:compounds, and is in a
748:position (denoted as Ni
712:(TNT) and catalyze the
2030:3-ethylmalate synthase
2025:2-ethylmalate synthase
1890:Acyltransferase like 2
1653:10.1074/jbc.M709470200
977:
957:Wood–Ljungdahl pathway
950:Conformational changes
914:
850:is coordinated to two
823:
811:Present (2014 onwards)
700:in the presence of an
655:
638:Methanocarcina barkeri
632:growth processes, and
594:
461:
306:Wood–Ljungdahl pathway
300:Wood–Ljungdahl pathway
286:Wood–Ljungdahl pathway
258:Wood–Ljungdahl pathway
2251:Eadie–Hofstee diagram
2184:Allosteric regulation
2010:Citrate (Re)-synthase
2005:Decylcitrate synthase
1946:Aminoacyltransferases
1846:palmitoyltransferases
975:
912:
818:
768:of unknown identity.
710:2,4,6-trinitrotoluene
650:
595:
462:
234:acetyl-CoA synthetase
2261:Lineweaver–Burk plot
2072:Homocitrate synthase
1959:Peptidyl transferase
1424:(15–16): 1582–1595.
984:mechanism" and the "
875:certain conditions.
489:
337:
1804:N-acetyltransferase
1455:(20): 13131–13142.
1326:2002Sci...298..567D
1025:migratory insertion
900:C. hydrogenoformans
547:
514:
452:
409:
354:
230:Acetyl-CoA synthase
18:Acetyl-CoA synthase
2220:Enzyme superfamily
2153:Enzyme promiscuity
1764:acetyltransferases
978:
915:
824:
708:of the pollutant,
656:
590:
566:
502:
457:
440:
428:
342:
2376:
2375:
2085:
2084:
2035:ATP citrate lyase
1696:978-0-470-01671-8
1207:10.1021/ar040002e
1159:10.1021/cr400461p
1036:activation step.
885:electron transfer
614:
613:
588:
581:
573:
568:
529:
522:
505:
496:
481:
480:
455:
443:
435:
430:
385:
367:
345:
227:
226:
223:
222:
126:metabolic pathway
16:(Redirected from
2423:
2393:
2392:
2384:
2256:Hanes–Woolf plot
2199:Enzyme activator
2194:Enzyme inhibitor
2168:Enzyme catalysis
2112:
2105:
2098:
2089:
2045:HMG-CoA synthase
2000:Citrate synthase
1964:Transglutaminase
1741:acyltransferases
1730:
1723:
1716:
1707:
1701:
1700:
1682:
1676:
1675:
1665:
1655:
1631:
1622:
1621:
1611:
1579:
1570:
1569:
1559:
1533:
1524:
1518:
1517:
1515:
1505:
1481:
1475:
1474:
1464:
1440:
1434:
1433:
1413:
1400:
1399:
1363:
1354:
1353:
1320:(5593): 567–72.
1309:
1300:
1299:
1288:10.1021/cr950058
1282:(7): 2515–2540.
1276:Chemical Reviews
1271:
1262:
1261:
1225:
1219:
1218:
1190:
1181:
1180:
1170:
1147:Chemical Reviews
1138:
1119:
1118:
1111:
1105:
1104:
1068:
934:residues with a
904:M. thermoacetica
741:M. thermoacetica
686:M. theroaceticum
608:
599:
597:
596:
591:
589:
586:
582:
579:
578:
571:
569:
567:
565:
564:
557:
549:
548:
546:
539:
531:
527:
523:
520:
519:
513:
510:
503:
497:
494:
483:
475:
466:
464:
463:
458:
456:
453:
451:
448:
441:
436:
433:
431:
429:
427:
426:
419:
411:
410:
408:
401:
393:
391:
390:
383:
374:
373:
372:
365:
355:
353:
350:
343:
331:
180:
42:
30:
21:
2431:
2430:
2426:
2425:
2424:
2422:
2421:
2420:
2401:
2400:
2399:
2387:
2379:
2377:
2372:
2284:Oxidoreductases
2270:
2246:Enzyme kinetics
2234:
2230:List of enzymes
2203:
2172:
2143:Catalytic triad
2121:
2116:
2086:
2081:
2040:Malate synthase
1985:
1936:
1748:
1734:
1704:
1697:
1684:
1683:
1679:
1646:(13): 8384–94.
1633:
1632:
1625:
1581:
1580:
1573:
1531:
1526:
1525:
1521:
1483:
1482:
1478:
1442:
1441:
1437:
1415:
1414:
1403:
1365:
1364:
1357:
1311:
1310:
1303:
1273:
1272:
1265:
1227:
1226:
1222:
1192:
1191:
1184:
1140:
1139:
1122:
1113:
1112:
1108:
1070:
1069:
1062:
1058:
1021:carbon monoxide
1018:
995:
970:
965:
952:
922:that go into a
865:
849:
845:
837:
828:oxidation state
821:M.thermoacetica
813:
794:
779:
751:
737:
732:
695:
682:
680:Other reactions
643:
636:archae such as
606:
487:
486:
473:
382:
364:
335:
334:
322:carbon monoxide
314:carbon monoxide
302:
283:
278:
260:which converts
45:
28:
23:
22:
15:
12:
11:
5:
2429:
2427:
2419:
2418:
2413:
2403:
2402:
2398:
2397:
2374:
2373:
2371:
2370:
2357:
2344:
2331:
2318:
2305:
2292:
2278:
2276:
2272:
2271:
2269:
2268:
2263:
2258:
2253:
2248:
2242:
2240:
2236:
2235:
2233:
2232:
2227:
2222:
2217:
2211:
2209:
2208:Classification
2205:
2204:
2202:
2201:
2196:
2191:
2186:
2180:
2178:
2174:
2173:
2171:
2170:
2165:
2160:
2155:
2150:
2145:
2140:
2135:
2129:
2127:
2123:
2122:
2117:
2115:
2114:
2107:
2100:
2092:
2083:
2082:
2080:
2079:
2074:
2069:
2064:
2059:
2054:
2053:
2052:
2042:
2037:
2032:
2027:
2022:
2017:
2012:
2007:
2002:
1996:
1994:
1987:
1986:
1984:
1983:
1982:
1981:
1976:
1971:
1961:
1956:
1950:
1948:
1938:
1937:
1935:
1934:
1929:
1924:
1919:
1913:
1912:
1907:
1902:
1897:
1892:
1883:
1882:
1881:
1880:
1875:
1865:
1864:
1863:
1858:
1841:
1840:
1839:
1838:
1833:
1823:
1822:
1821:
1816:
1811:
1801:
1796:
1791:
1786:
1781:
1776:
1771:
1759:
1757:
1750:
1749:
1735:
1733:
1732:
1725:
1718:
1710:
1703:
1702:
1695:
1677:
1623:
1571:
1519:
1476:
1435:
1401:
1355:
1301:
1263:
1220:
1201:(10): 775–83.
1182:
1153:(8): 4149–74.
1120:
1106:
1059:
1057:
1054:
1016:
993:
969:
966:
964:
961:
951:
948:
863:
847:
843:
835:
812:
809:
792:
777:
764:position with
749:
736:
733:
731:
728:
693:
681:
678:
670:methanogenesis
641:
612:
611:
602:
600:
585:
577:
563:
556:
545:
538:
526:
518:
509:
500:
479:
478:
469:
467:
447:
439:
425:
418:
407:
400:
389:
380:
377:
371:
362:
358:
349:
310:carbon dioxide
301:
298:
281:
277:
274:
262:carbon dioxide
225:
224:
221:
220:
215:
209:
208:
203:
197:
196:
191:
185:
184:
176:
175:
166:
160:
159:
148:
141:
140:
135:
129:
128:
123:
117:
116:
111:
105:
104:
99:
93:
92:
87:
81:
80:
75:
69:
68:
64:
63:
58:
52:
51:
47:
46:
43:
35:
34:
26:
24:
14:
13:
10:
9:
6:
4:
3:
2:
2428:
2417:
2414:
2412:
2409:
2408:
2406:
2396:
2391:
2386:
2382:
2368:
2364:
2363:
2358:
2355:
2351:
2350:
2345:
2342:
2338:
2337:
2332:
2329:
2325:
2324:
2319:
2316:
2312:
2311:
2306:
2303:
2299:
2298:
2293:
2290:
2286:
2285:
2280:
2279:
2277:
2273:
2267:
2264:
2262:
2259:
2257:
2254:
2252:
2249:
2247:
2244:
2243:
2241:
2237:
2231:
2228:
2226:
2225:Enzyme family
2223:
2221:
2218:
2216:
2213:
2212:
2210:
2206:
2200:
2197:
2195:
2192:
2190:
2189:Cooperativity
2187:
2185:
2182:
2181:
2179:
2175:
2169:
2166:
2164:
2161:
2159:
2156:
2154:
2151:
2149:
2148:Oxyanion hole
2146:
2144:
2141:
2139:
2136:
2134:
2131:
2130:
2128:
2124:
2120:
2113:
2108:
2106:
2101:
2099:
2094:
2093:
2090:
2078:
2075:
2073:
2070:
2068:
2065:
2063:
2060:
2058:
2055:
2051:
2048:
2047:
2046:
2043:
2041:
2038:
2036:
2033:
2031:
2028:
2026:
2023:
2021:
2018:
2016:
2013:
2011:
2008:
2006:
2003:
2001:
1998:
1997:
1995:
1992:
1988:
1980:
1977:
1975:
1972:
1970:
1967:
1966:
1965:
1962:
1960:
1957:
1955:
1952:
1951:
1949:
1947:
1943:
1939:
1933:
1930:
1928:
1925:
1923:
1920:
1918:
1915:
1914:
1911:
1908:
1906:
1903:
1901:
1898:
1896:
1893:
1891:
1888:
1885:
1884:
1879:
1876:
1874:
1871:
1870:
1869:
1866:
1862:
1859:
1857:
1854:
1853:
1852:
1849:
1847:
1843:
1842:
1837:
1834:
1832:
1829:
1828:
1827:
1824:
1820:
1817:
1815:
1812:
1810:
1807:
1806:
1805:
1802:
1800:
1797:
1795:
1792:
1790:
1787:
1785:
1782:
1780:
1777:
1775:
1772:
1770:
1767:
1765:
1761:
1760:
1758:
1755:
1751:
1746:
1742:
1738:
1731:
1726:
1724:
1719:
1717:
1712:
1711:
1708:
1698:
1692:
1688:
1681:
1678:
1673:
1669:
1664:
1659:
1654:
1649:
1645:
1641:
1637:
1630:
1628:
1624:
1619:
1615:
1610:
1605:
1601:
1597:
1593:
1589:
1585:
1578:
1576:
1572:
1567:
1563:
1558:
1553:
1549:
1545:
1542:(2): 276–83.
1541:
1537:
1530:
1523:
1520:
1514:
1509:
1504:
1499:
1496:(1): 148330.
1495:
1491:
1487:
1480:
1477:
1472:
1468:
1463:
1458:
1454:
1450:
1449:ACS Catalysis
1446:
1439:
1436:
1431:
1427:
1423:
1419:
1412:
1410:
1408:
1406:
1402:
1397:
1393:
1389:
1385:
1381:
1377:
1373:
1369:
1362:
1360:
1356:
1351:
1347:
1343:
1339:
1335:
1331:
1327:
1323:
1319:
1315:
1308:
1306:
1302:
1297:
1293:
1289:
1285:
1281:
1277:
1270:
1268:
1264:
1259:
1255:
1251:
1247:
1243:
1239:
1235:
1231:
1224:
1221:
1216:
1212:
1208:
1204:
1200:
1196:
1189:
1187:
1183:
1178:
1174:
1169:
1164:
1160:
1156:
1152:
1148:
1144:
1137:
1135:
1133:
1131:
1129:
1127:
1125:
1121:
1116:
1110:
1107:
1102:
1098:
1094:
1090:
1086:
1082:
1079:(5): 516–24.
1078:
1074:
1067:
1065:
1061:
1055:
1053:
1051:
1047:
1042:
1037:
1035:
1031:
1026:
1022:
1014:
1010:
1005:
1003:
999:
991:
987:
983:
974:
967:
962:
960:
958:
949:
947:
944:
939:
937:
933:
929:
925:
924:Rossmann fold
921:
911:
907:
905:
901:
897:
893:
888:
886:
881:
876:
873:
869:
861:
860:square-planar
857:
853:
841:
833:
829:
822:
817:
810:
808:
806:
802:
798:
789:
787:
783:
775:
769:
767:
763:
759:
755:
754:square-planar
747:
742:
734:
729:
727:
725:
722:
720:
715:
711:
707:
703:
699:
698:nitrous oxide
691:
687:
679:
677:
675:
671:
666:
664:
660:
653:
649:
645:
639:
635:
631:
627:
623:
619:
610:
603:
601:
583:
575:
554:
543:
524:
516:
507:
498:
485:
484:
477:
470:
468:
445:
437:
416:
405:
387:
378:
375:
369:
360:
356:
347:
333:
332:
329:
327:
323:
319:
315:
311:
307:
299:
297:
295:
291:
287:
275:
273:
271:
267:
263:
259:
255:
251:
247:
243:
239:
235:
231:
219:
216:
214:
210:
207:
204:
202:
198:
195:
192:
190:
186:
181:
177:
174:
170:
167:
165:
164:Gene Ontology
161:
158:
155:
152:
149:
146:
142:
139:
136:
134:
130:
127:
124:
122:
118:
115:
112:
110:
106:
103:
102:NiceZyme view
100:
98:
94:
91:
88:
86:
82:
79:
76:
74:
70:
65:
62:
59:
57:
53:
48:
41:
36:
31:
19:
2362:Translocases
2359:
2346:
2333:
2320:
2307:
2297:Transferases
2294:
2281:
2138:Binding site
1886:
1844:
1762:
1737:Transferases
1686:
1680:
1643:
1639:
1591:
1587:
1539:
1535:
1522:
1493:
1489:
1479:
1452:
1448:
1438:
1421:
1417:
1374:(5): 511–5.
1371:
1367:
1317:
1313:
1279:
1275:
1236:(5): 542–9.
1233:
1229:
1223:
1198:
1194:
1150:
1146:
1114:
1109:
1076:
1072:
1038:
1009:paramagnetic
1006:
982:paramagnetic
979:
953:
940:
916:
903:
899:
895:
891:
889:
877:
872:acetyl group
825:
820:
790:
770:
740:
738:
718:
685:
683:
667:
657:
637:
634:methanogenic
615:
604:
471:
303:
294:carbon cycle
279:
269:
229:
228:
90:BRENDA entry
2133:Active site
1979:Factor XIII
1050:diamagnetic
986:diamagnetic
943:hydrophobic
868:tetrahedral
762:tetrahedral
663:acetic acid
652:Autotrophic
630:autotrophic
78:IntEnz view
50:Identifiers
2405:Categories
2336:Isomerases
2310:Hydrolases
2177:Regulation
1594:: 142–52.
1056:References
1046:zerovalent
1034:ferrodoxin
1013:ferrodoxin
938:molecule.
936:tryptophan
928:ferredoxin
724:isocyanide
690:dinitrogen
659:Acetogenic
628:for their
626:acetyl-CoA
618:acetyl-CoA
320:using the
318:acetyl-CoA
266:Acetyl-CoA
147:structures
114:KEGG entry
2215:EC number
1471:2155-5435
1041:insertion
990:oxidation
968:Mechanism
920:α-helices
730:Structure
714:oxidation
706:reduction
688:can make
576:−
562:⇀
555:−
544:−
537:↽
517:−
424:⇀
417:−
406:−
399:↽
388:−
276:Chemistry
67:Databases
61:2.3.1.169
2411:EC 2.3.1
2239:Kinetics
2163:Cofactor
2126:Activity
1831:P300/CBP
1672:18203715
1618:24036122
1566:21130022
1396:23263180
1388:15221484
1350:39880131
1342:12386327
1296:11848835
1250:15221481
1215:15491124
1177:24521136
1101:21597571
1093:15221478
963:Activity
932:arginine
852:cysteine
840:thiolate
774:proximal
758:proximal
254:bacteria
248:such as
218:proteins
206:articles
194:articles
151:RCSB PDB
2395:Biology
2349:Ligases
2119:Enzymes
1663:2820341
1609:3946514
1557:3061974
1322:Bibcode
1314:Science
1258:6536992
1168:4002135
1007:In the
1002:cluster
832:cluster
830:. The
766:ligands
752:) in a
735:History
696:) from
250:archaea
173:QuickGO
138:profile
121:MetaCyc
2381:Portal
2323:Lyases
2050:HMGCS2
1887:other:
1878:SPTLC2
1873:SPTLC1
1814:HGSNAT
1693:
1670:
1660:
1616:
1606:
1564:
1554:
1469:
1394:
1386:
1348:
1340:
1294:
1256:
1248:
1213:
1175:
1165:
1099:
1091:
782:nickel
746:distal
721:-butyl
572:acetyl
238:nickel
201:PubMed
183:Search
169:AmiGO
157:PDBsum
97:ExPASy
85:BRENDA
73:IntEnz
56:EC no.
27:Enzyme
2275:Types
1991:2.3.3
1942:2.3.2
1932:ABHD5
1819:ARD1A
1754:2.3.1
1532:(PDF)
1392:S2CID
1346:S2CID
1254:S2CID
1097:S2CID
998:redox
880:dimer
856:amide
587:CFeSP
521:CFeSP
312:into
133:PRIAM
2367:list
2360:EC7
2354:list
2347:EC6
2341:list
2334:EC5
2328:list
2321:EC4
2315:list
2308:EC3
2302:list
2295:EC2
2289:list
2282:EC1
1861:CPT2
1856:CPT1
1836:NAT2
1747:2.3)
1691:ISBN
1668:PMID
1614:PMID
1562:PMID
1494:1862
1467:ISSN
1384:PMID
1338:PMID
1292:PMID
1246:PMID
1211:PMID
1173:PMID
1089:PMID
894:and
846:. Ni
803:and
786:zinc
624:use
616:The
304:The
252:and
213:NCBI
154:PDBe
109:KEGG
1658:PMC
1648:doi
1644:283
1604:PMC
1596:doi
1592:544
1552:PMC
1544:doi
1508:hdl
1498:doi
1457:doi
1426:doi
1422:249
1376:doi
1330:doi
1318:298
1284:doi
1238:doi
1203:doi
1163:PMC
1155:doi
1151:114
1081:doi
716:of
674:ATP
580:CoA
528:CoA
264:to
189:PMC
145:PDB
2407::
1944::
1745:EC
1739::
1666:.
1656:.
1642:.
1638:.
1626:^
1612:.
1602:.
1590:.
1586:.
1574:^
1560:.
1550:.
1540:15
1538:.
1534:.
1506:.
1492:.
1488:.
1465:.
1453:12
1451:.
1447:.
1420:.
1404:^
1390:.
1382:.
1370:.
1358:^
1344:.
1336:.
1328:.
1316:.
1304:^
1290:.
1280:96
1278:.
1266:^
1252:.
1244:.
1232:.
1209:.
1199:37
1197:.
1185:^
1171:.
1161:.
1149:.
1145:.
1123:^
1095:.
1087:.
1075:.
1063:^
906:.
805:Ni
801:Zn
799:,
797:Cu
726:.
692:(N
644:.
504:CH
495:CO
434:CO
344:CO
272:.
171:/
2383::
2369:)
2365:(
2356:)
2352:(
2343:)
2339:(
2330:)
2326:(
2317:)
2313:(
2304:)
2300:(
2291:)
2287:(
2111:e
2104:t
2097:v
1848::
1766::
1743:(
1729:e
1722:t
1715:v
1699:.
1674:.
1650::
1620:.
1598::
1568:.
1546::
1516:.
1510::
1500::
1473:.
1459::
1432:.
1428::
1398:.
1378::
1372:9
1352:.
1332::
1324::
1298:.
1286::
1260:.
1240::
1234:9
1217:.
1205::
1179:.
1157::
1103:.
1083::
1077:9
1017:p
994:p
864:p
848:d
844:d
836:p
793:p
778:p
750:d
719:n
694:2
642:2
609:)
607:2
605:(
584:+
525:+
508:3
499:+
476:)
474:1
472:(
454:O
446:2
442:H
438:+
384:e
379:2
376:+
370:+
366:H
361:2
357:+
348:2
282:2
20:)
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
