263:
460:
665:
732:
577:
698:
2143:
750:
29:
808:
Studies have linked the anti-fungal activity of several anti-fungal agents to the inhibition of cystathionine beta-lyase; however, other studies have not observed enzyme inhibition by these. Further research is needed to characterize the full extent cystathionine beta-lyase inhibition has on
1054:
Messerschmidt A, Worbs M, Steegborn C, Wahl MC, Huber R, Laber B, Clausen T (March 2003). "Determinants of enzymatic specificity in the Cys-Met-metabolism PLP-dependent enzymes family: crystal structure of cystathionine gamma-lyase from yeast and intrafamiliar structure comparison".
496:
Contains most of the catalytically relevant residues on the enzyme. It is composed of α-helices and β-sheets with a distinct parallel seven-stranded β-sheet. These sheets form a curved structure around the PLP-binding helix. PLP is covalently attached to a lysine residue at the
746:, a time-dependent, slow-binding inhibition was observed. It is believed that the inhibitor binds to the enzyme in a similar way as the substrate; however, after the abstraction of the α-proton, the reaction proceeds to create an inactive ketimine PLP derivative.
1686:
Ejim LJ, Blanchard JE, Koteva KP, Sumerfield R, Elowe NH, Chechetto JD, Brown ED, Junop MS, Wright GD (February 2007). "Inhibitors of bacterial cystathionine beta-lyase: leads for new antimicrobial agents and probes of enzyme structure and function".
801:. Because of its necessity in DNA replication, inhibition of cystathionine beta-lyase is an attractive antibiotic target. Furthermore, the enzyme is absent in humans, decreasing the chance of harmful and unwanted
789:
Cystathionine beta-lyase catalyzes the production of homocysteine, a direct precursor to methionine. Methionine is an essential amino acid for bacteria that is required for protein synthesis and the synthesis of
693:
Cystathionine beta-lyase in plants exhibits a two-step mechanism inactivation process with AVG, in which a reversible enzyme-inhibitor complex is formed before the irreversible inactivation of the enzyme:
1530:
Clausen T, Huber R, Messerschmidt A, Pohlenz HD, Laber B (October 1997). "Slow-binding inhibition of
Escherichia coli cystathionine beta-lyase by L-aminoethoxyvinylglycine: a kinetic and X-ray study".
1357:
Clausen T, Huber R, Laber B, Pohlenz HD, Messerschmidt A (September 1996). "Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from
Escherichia coli at 1.83 A".
1098:
Alexander FW, Sandmeier E, Mehta PK, Christen P (February 1994). "Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families".
1008:
Droux M, Ravanel S, Douce R (January 1995). "Methionine biosynthesis in higher plants. II. Purification and characterization of cystathionine beta-lyase from spinach chloroplasts".
1626:"Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region"
1788:
262:
194:
778:
1181:
Holbrook EL, Greene RC, Krueger JH (January 1990). "Purification and properties of cystathionine gamma-synthase from overproducing strains of
Escherichia coli".
213:
521:
Aside from being bound to a lysine residue, PLP is fixed within the substrate binding site of the enzyme through various interactions with catalytic residues.
773:
counterpart and even higher homology (between 28% and 36%) with cystathionine Îł-synthase from plant and bacterial sources and cystathionine Îł-lyase from
463:
Cystathionine beta-lyase dimer. N-terminal domain shown in green, PLP-binding domain shown in red, and C-terminal domain shown in cyan. PDB entry: 4ITX
639:
The external aldimine is displaced by the nucleophilic attack of the lysine, regenerating the catalytically active internal aldimine and releasing
509:
Smallest domain on the enzyme, which is attached to the PLP-binding domain by a long, kinked α-helix. The domain is structured into four-stranded
1781:
580:
Key binding domain residues interacting with PLP. Residues belonging to the adjacent
Arabidopsis CBL subunit are shown in blue. PDB entry: 1IBJ
488:. This domain contains residues that interact with the active site of the neighboring subunit to facilitate substrate and cofactor binding.
2168:
536:. This phosphate group is considered to be the main contributor to securing PLP in the active site. Additionally, residues neighboring the
2173:
573:
can be found in most PLP-dependent enzymes as it plays an important role in catalyzing the reaction by facilitating transaldimination.
825:
Dwivedi CM, Ragin RC, Uren JR (June 1982). "Cloning, purification, and characterization of beta-cystathionase from
Escherichia coli".
1774:
1862:
1430:
Aitken SM, Lodha PH, Morneau DJ (November 2011). "The enzymes of the transsulfuration pathways: active-site characterizations".
206:
133:
2018:
157:
781:
and belong to the same class of PLP-dependent enzymes, suggesting that these enzymes were derived from a common ancestor.
2133:
609:, which abstracts a proton from the α-amino group of the substrate. In the next step, the deprotonated amine undergoes a
485:
433:
510:
1138:"Purification and properties of cystathionine beta-lyase from Arabidopsis thaliana overexpressed in Escherichia coli"
1491:"beta-Cystathionase from Bordetella avium. Role(s) of lysine 214 and cysteine residues in activity and cytotoxicity"
2003:
2119:
2106:
2093:
2080:
2067:
2054:
2041:
1819:
1811:
437:
356:
2013:
1967:
1910:
1802:
774:
429:
415:
234:
151:
44:
597:
cleavage in cystathionine with the use of a PLP cofactor bounded to a catalytic lysine residue. Initially, a
1915:
1829:
918:"The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity"
328:
138:
705:
449:
441:
1218:"Purification and Properties of Cystathionine [gamma]-Synthase from Wheat (Triticum aestivum L.)"
704:
Excess addition of cystathionine prevented the inactivation of the enzyme, suggesting that AVG acts as a
1936:
1855:
791:
743:
625:
348:
271:
218:
2008:
472:
The cystathionine beta-lyase monomer consists of three functionally and structurally distinct domains:
126:
1624:
Belfaiza J, Parsot C, Martel A, de la Tour CB, Margarita D, Cohen GN, Saint-Girons I (February 1986).
605:
optimum for the enzyme is between 8.0 and 9.0, a tyrosine residue in the catalytic pocket exists as a
1637:
1578:
916:
Breitinger U, Clausen T, Ehlert S, Huber R, Laber B, Schmidt F, Pohl E, Messerschmidt A (June 2001).
629:
61:
1972:
668:
Mechanism catalyzed by cystathionine beta-lyase. Cofactor and catalytic residues are shown in blue.
445:
360:
352:
324:
320:
279:
56:
459:
154:
1905:
1080:
766:
728:
Unlike in plants, Cystathionine beta-lyase in bacteria exhibits a one-step inhibition mechanism:
590:
453:
78:
976:
Clausen T, Laber B, Messerschmidt A (1997-03-01). "Mode of action of cystathionine beta-lyase".
636:. Subsequently, the protonation of S induces C-S bond cleavage, thereby releasing homocysteine
428:
Most of the enzyme's catalytic site residues are conserved amongst the enzymes involved in the
2163:
1753:
1704:
1665:
1606:
1547:
1512:
1447:
1412:
1374:
1334:
1296:
1247:
1198:
1163:
1115:
1072:
1025:
985:
947:
883:
842:
739:
664:
633:
384:
364:
316:
257:
145:
1951:
1946:
1920:
1848:
1743:
1735:
1696:
1655:
1645:
1596:
1586:
1539:
1502:
1439:
1404:
1366:
1326:
1286:
1278:
1237:
1229:
1190:
1153:
1145:
1107:
1064:
1017:
937:
929:
873:
834:
770:
713:
1998:
1982:
1895:
1314:
798:
753:
AVG bounded to catalytic PLP in the substrate binding site of E. coli CBL. PDB entry: 1CL2
731:
708:
with respect to cystathionine. Additionally, the enzyme has been shown to be sensitive to
544:
380:
336:
114:
1641:
1582:
90:
2147:
2036:
1977:
1748:
1723:
1291:
1266:
1158:
1137:
1111:
640:
407:
189:
49:
1660:
1625:
1330:
1242:
1217:
942:
917:
878:
861:
576:
169:
2157:
1941:
1900:
1601:
1566:
1408:
717:
678:
598:
594:
569:
sink character of the cofactor. These stacking interactions between PLP and aromatic
526:
411:
275:
164:
1317:(December 1998). "Structure, evolution and action of vitamin B6-dependent enzymes".
1084:
697:
1890:
548:
313:
287:
283:
323:. The enzyme belongs to the Îł-family of PLP-dependent enzymes due to its use of a
1443:
2114:
2049:
1885:
1766:
1397:
Biochimica et
Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
802:
762:
682:
658:
614:
610:
601:
amino group is needed to perform the transaldimination reaction. Given that the
559:
555:
423:
392:
173:
2142:
1630:
Proceedings of the
National Academy of Sciences of the United States of America
1571:
Proceedings of the
National Academy of Sciences of the United States of America
1739:
749:
655:
624:
The released lysine can now abstract the proton from the C and form a quinoid
570:
498:
481:
419:
399:
344:
310:
2088:
2062:
1591:
1507:
1490:
530:
253:
1757:
1708:
1567:"The specific features of methionine biosynthesis and metabolism in plants"
1451:
1370:
1282:
1251:
1076:
1021:
951:
887:
1669:
1650:
1610:
1551:
1516:
1416:
1378:
1338:
1300:
1267:"Modeling of the spatial structure of eukaryotic ornithine decarboxylases"
1233:
1202:
1167:
1119:
1029:
989:
846:
529:-containing residues are located in hydrogen bonding distance to the four
933:
647:
618:
566:
562:
540:
537:
388:
376:
302:
1194:
1068:
838:
644:
403:
291:
237:
121:
102:
1700:
1543:
1465:
1149:
730:
696:
456:
and active sites composed of residues belonging to adjacent subunits.
418:, whereas the tetramer is stabilized through interactions between the
261:
2101:
1871:
606:
533:
396:
249:
201:
97:
85:
73:
341:
L-cystathionine L-homocysteine-lyase (deaminating; pyruvate-forming)
677:
Plant and bacterial cystathionine beta-lyases are inhibited by the
2075:
1798:
748:
709:
663:
651:
575:
522:
332:
331:
to cleave cystathionine. The enzyme also belongs to the family of
306:
298:
109:
1844:
1770:
1395:
John RA (April 1995). "Pyridoxal phosphate-dependent enzymes".
28:
795:
565:
residue. It is believed that this configuration increases the
1724:"Inhibitors of amino acids biosynthesis as antifungal agents"
1432:
Biochimica et
Biophysica Acta (BBA) - Proteins and Proteomics
319:
as homocysteine can be directly converted into methionine by
602:
1840:
1216:
Kreft BD, Townsend A, Pohlenz HD, Laber B (April 1994).
335:, specifically the class of carbon-sulfur lyases. The
309:, cystathionine beta-lyase is an essential part of the
2131:
681:
amino acid, L-aminoethoxyvinylglycine (AVG), and the
1489:
Gentry-Weeks CR, Spokes J, Thompson J (March 1995).
1049:
1047:
1045:
1043:
1041:
1039:
593:
below, cystathionine beta-lyase facilitates the S-C
2027:
1991:
1960:
1929:
1878:
1810:
1265:Grishin NV, Phillips MA, Goldsmith EJ (July 1995).
212:
200:
188:
183:
163:
144:
132:
120:
108:
96:
84:
72:
67:
55:
43:
38:
21:
1565:Ravanel S, Gakière B, Job D, Douce R (June 1998).
911:
909:
907:
905:
903:
901:
899:
897:
1352:
1350:
1348:
452:(AAT) family, characterized by homodimers with
1131:
1129:
971:
969:
967:
965:
963:
961:
862:"Cystathionine Cleavage Enzymes of Neurospora"
266:Reaction catalyzed by cystathionine beta-lyase
1856:
1782:
794:; thus, the amino acid is directly linked to
632:of the negative charge over PLP's conjugated
8:
1722:Jastrzębowska K, Gabriel I (February 2015).
1681:
1679:
1390:
1388:
1003:
1001:
999:
1136:Ravanel S, Job D, Douce R (December 1996).
777:. All of these enzymes are involved in the
444:. Additionally, these structures exhibit a
1863:
1849:
1841:
1789:
1775:
1767:
613:attack and displaces the lysine to form a
180:
1747:
1659:
1649:
1600:
1590:
1506:
1290:
1241:
1157:
941:
877:
33:Cystathionine beta-lyase tetramer, E.Coli
484:that contribute to the formation of the
458:
2138:
1010:Archives of Biochemistry and Biophysics
817:
765:cystathionine beta-lyase possesses 22%
558:in PLP is fixed in place by an almost
18:
1319:Current Opinion in Structural Biology
7:
480:Composed of three α-helices and one
387:of dimers, each associated with one
1495:The Journal of Biological Chemistry
866:The Journal of Biological Chemistry
860:Flavin M, Slaughter C (July 1964).
1112:10.1111/j.1432-1033.1994.tb18577.x
513:β-sheet with neighboring helices.
14:
2141:
1100:European Journal of Biochemistry
343:. This enzyme participates in 5
240:), also commonly referred to as
27:
1689:Journal of Medicinal Chemistry
712:-blocking inhibitors, such as
661:to form pyruvate and ammonia.
628:, which is facilitated by the
375:Cystathionine beta-lyase is a
256:the following α,β-elimination
1:
1331:10.1016/s0959-440x(98)80096-1
879:10.1016/S0021-9258(20)82222-4
809:microbial and fungal growth.
402:. The dimer is formed by two
1444:10.1016/j.bbapap.2011.03.006
1409:10.1016/0167-4838(95)00025-p
1359:Journal of Molecular Biology
779:Cys/Met biosynthetic pathway
434:cystathionine gamma-synthase
2169:Pyridoxal phosphate enzymes
1144:. 320 ( Pt 2) (2): 383–92.
685:amino acid, rhizobitoxine.
406:associated through several
357:selenoamino acid metabolism
2190:
2174:Enzymes of known structure
543:in PLP help stabilize its
450:aspartate aminotransferase
383:, and is constructed as a
2019:Michaelis–Menten kinetics
1820:Cystathionine gamma-lyase
1740:10.1007/s00726-014-1873-1
547:, thereby increasing its
438:cystathionine gamma-lyase
179:
26:
1911:Diffusion-limited enzyme
1825:Cystathionine beta-lyase
775:Saccharomyces cerevisiae
432:. Other members include
430:transsulfuration pathway
416:hydrophobic interactions
339:of this enzyme class is
231:Cystathionine beta-lyase
22:cystathionine beta-lyase
1830:Leukotriene C4 synthase
1592:10.1073/pnas.95.13.7805
1508:10.1074/jbc.270.13.7695
1142:The Biochemical Journal
1466:"ENZYME entry 4.4.1.8"
1371:10.1006/jmbi.1996.0508
1283:10.1002/pro.5560040705
1022:10.1006/abbi.1995.1078
754:
735:
701:
669:
617:, forming an internal
581:
464:
442:methionine gamma lyase
379:composed of identical
325:pyridoxal-5'-phosphate
267:
2004:Eadie–Hofstee diagram
1937:Allosteric regulation
1651:10.1073/pnas.83.4.867
1234:10.1104/pp.104.4.1215
752:
744:X-ray crystallography
734:
706:competitive inhibitor
700:
667:
579:
462:
349:methionine metabolism
265:
2014:Lineweaver–Burk plot
1057:Biological Chemistry
978:Biological Chemistry
934:10.1104/pp.126.2.631
792:S-adenosylmethionine
785:Industrial relevance
486:quaternary structure
391:of PLP bound to the
1642:1986PNAS...83..867B
1583:1998PNAS...95.7805R
1195:10.1021/bi00454a019
1069:10.1515/BC.2003.043
839:10.1021/bi00256a005
361:nitrogen metabolism
353:cysteine metabolism
321:methionine synthase
274:of this enzyme is
1973:Enzyme superfamily
1906:Enzyme promiscuity
755:
736:
702:
670:
582:
492:PLP-binding domain
465:
448:and belong to the
345:metabolic pathways
268:
2129:
2128:
1838:
1837:
1701:10.1021/jm061132r
1544:10.1021/bi970630m
1470:enzyme.expasy.org
1150:10.1042/bj3200383
505:C-terminal domain
476:N-terminal domain
454:dihedral symmetry
365:sulfur metabolism
228:
227:
224:
223:
127:metabolic pathway
2181:
2146:
2145:
2137:
2009:Hanes–Woolf plot
1952:Enzyme activator
1947:Enzyme inhibitor
1921:Enzyme catalysis
1865:
1858:
1851:
1842:
1791:
1784:
1777:
1768:
1762:
1761:
1751:
1719:
1713:
1712:
1683:
1674:
1673:
1663:
1653:
1621:
1615:
1614:
1604:
1594:
1562:
1556:
1555:
1538:(41): 12633–43.
1527:
1521:
1520:
1510:
1501:(13): 7695–702.
1486:
1480:
1479:
1477:
1476:
1462:
1456:
1455:
1427:
1421:
1420:
1392:
1383:
1382:
1354:
1343:
1342:
1311:
1305:
1304:
1294:
1262:
1256:
1255:
1245:
1228:(4): 1215–1220.
1222:Plant Physiology
1213:
1207:
1206:
1178:
1172:
1171:
1161:
1133:
1124:
1123:
1095:
1089:
1088:
1051:
1034:
1033:
1005:
994:
993:
973:
956:
955:
945:
922:Plant Physiology
913:
892:
891:
881:
857:
851:
850:
822:
771:Escherichia coli
714:N-ethylmaleimide
589:As shown in the
422:domains and key
412:hydrogen bonding
278:, whereas its 3
181:
31:
19:
2189:
2188:
2184:
2183:
2182:
2180:
2179:
2178:
2154:
2153:
2152:
2140:
2132:
2130:
2125:
2037:Oxidoreductases
2023:
1999:Enzyme kinetics
1987:
1983:List of enzymes
1956:
1925:
1896:Catalytic triad
1874:
1869:
1839:
1834:
1806:
1795:
1765:
1721:
1720:
1716:
1685:
1684:
1677:
1623:
1622:
1618:
1577:(13): 7805–12.
1564:
1563:
1559:
1529:
1528:
1524:
1488:
1487:
1483:
1474:
1472:
1464:
1463:
1459:
1429:
1428:
1424:
1394:
1393:
1386:
1356:
1355:
1346:
1313:
1312:
1308:
1277:(7): 1291–304.
1271:Protein Science
1264:
1263:
1259:
1215:
1214:
1210:
1180:
1179:
1175:
1135:
1134:
1127:
1097:
1096:
1092:
1053:
1052:
1037:
1007:
1006:
997:
975:
974:
959:
915:
914:
895:
859:
858:
854:
824:
823:
819:
815:
787:
760:
740:kinetic methods
726:
691:
675:
654:that undergoes
587:
545:positive charge
519:
507:
494:
478:
470:
373:
337:systematic name
276:L-cystathionine
252:that primarily
246:β-cystathionase
34:
17:
12:
11:
5:
2187:
2185:
2177:
2176:
2171:
2166:
2156:
2155:
2151:
2150:
2127:
2126:
2124:
2123:
2110:
2097:
2084:
2071:
2058:
2045:
2031:
2029:
2025:
2024:
2022:
2021:
2016:
2011:
2006:
2001:
1995:
1993:
1989:
1988:
1986:
1985:
1980:
1975:
1970:
1964:
1962:
1961:Classification
1958:
1957:
1955:
1954:
1949:
1944:
1939:
1933:
1931:
1927:
1926:
1924:
1923:
1918:
1913:
1908:
1903:
1898:
1893:
1888:
1882:
1880:
1876:
1875:
1870:
1868:
1867:
1860:
1853:
1845:
1836:
1835:
1833:
1832:
1827:
1822:
1816:
1814:
1808:
1807:
1797:Carbon–sulfur
1796:
1794:
1793:
1786:
1779:
1771:
1764:
1763:
1714:
1675:
1616:
1557:
1522:
1481:
1457:
1438:(11): 1511–7.
1422:
1384:
1344:
1306:
1257:
1208:
1173:
1125:
1090:
1035:
995:
984:(3–4): 321–6.
957:
893:
852:
833:(13): 3064–9.
816:
814:
811:
786:
783:
759:
756:
725:
722:
690:
687:
674:
671:
643:. Lastly, the
641:dehydroalanine
630:delocalization
586:
583:
518:
517:Catalytic site
515:
506:
503:
501:of the sheet.
493:
490:
477:
474:
469:
466:
393:catalytic site
372:
369:
226:
225:
222:
221:
216:
210:
209:
204:
198:
197:
192:
186:
185:
177:
176:
167:
161:
160:
149:
142:
141:
136:
130:
129:
124:
118:
117:
112:
106:
105:
100:
94:
93:
88:
82:
81:
76:
70:
69:
65:
64:
59:
53:
52:
47:
41:
40:
36:
35:
32:
24:
23:
15:
13:
10:
9:
6:
4:
3:
2:
2186:
2175:
2172:
2170:
2167:
2165:
2162:
2161:
2159:
2149:
2144:
2139:
2135:
2121:
2117:
2116:
2111:
2108:
2104:
2103:
2098:
2095:
2091:
2090:
2085:
2082:
2078:
2077:
2072:
2069:
2065:
2064:
2059:
2056:
2052:
2051:
2046:
2043:
2039:
2038:
2033:
2032:
2030:
2026:
2020:
2017:
2015:
2012:
2010:
2007:
2005:
2002:
2000:
1997:
1996:
1994:
1990:
1984:
1981:
1979:
1978:Enzyme family
1976:
1974:
1971:
1969:
1966:
1965:
1963:
1959:
1953:
1950:
1948:
1945:
1943:
1942:Cooperativity
1940:
1938:
1935:
1934:
1932:
1928:
1922:
1919:
1917:
1914:
1912:
1909:
1907:
1904:
1902:
1901:Oxyanion hole
1899:
1897:
1894:
1892:
1889:
1887:
1884:
1883:
1881:
1877:
1873:
1866:
1861:
1859:
1854:
1852:
1847:
1846:
1843:
1831:
1828:
1826:
1823:
1821:
1818:
1817:
1815:
1813:
1809:
1804:
1800:
1792:
1787:
1785:
1780:
1778:
1773:
1772:
1769:
1759:
1755:
1750:
1745:
1741:
1737:
1734:(2): 227–49.
1733:
1729:
1725:
1718:
1715:
1710:
1706:
1702:
1698:
1695:(4): 755–64.
1694:
1690:
1682:
1680:
1676:
1671:
1667:
1662:
1657:
1652:
1647:
1643:
1639:
1636:(4): 867–71.
1635:
1631:
1627:
1620:
1617:
1612:
1608:
1603:
1598:
1593:
1588:
1584:
1580:
1576:
1572:
1568:
1561:
1558:
1553:
1549:
1545:
1541:
1537:
1533:
1526:
1523:
1518:
1514:
1509:
1504:
1500:
1496:
1492:
1485:
1482:
1471:
1467:
1461:
1458:
1453:
1449:
1445:
1441:
1437:
1433:
1426:
1423:
1418:
1414:
1410:
1406:
1402:
1398:
1391:
1389:
1385:
1380:
1376:
1372:
1368:
1365:(2): 202–24.
1364:
1360:
1353:
1351:
1349:
1345:
1340:
1336:
1332:
1328:
1325:(6): 759–69.
1324:
1320:
1316:
1315:Jansonius, JN
1310:
1307:
1302:
1298:
1293:
1288:
1284:
1280:
1276:
1272:
1268:
1261:
1258:
1253:
1249:
1244:
1239:
1235:
1231:
1227:
1223:
1219:
1212:
1209:
1204:
1200:
1196:
1192:
1189:(2): 435–42.
1188:
1184:
1177:
1174:
1169:
1165:
1160:
1155:
1151:
1147:
1143:
1139:
1132:
1130:
1126:
1121:
1117:
1113:
1109:
1106:(3): 953–60.
1105:
1101:
1094:
1091:
1086:
1082:
1078:
1074:
1070:
1066:
1063:(3): 373–86.
1062:
1058:
1050:
1048:
1046:
1044:
1042:
1040:
1036:
1031:
1027:
1023:
1019:
1016:(1): 585–95.
1015:
1011:
1004:
1002:
1000:
996:
991:
987:
983:
979:
972:
970:
968:
966:
964:
962:
958:
953:
949:
944:
939:
935:
931:
928:(2): 631–42.
927:
923:
919:
912:
910:
908:
906:
904:
902:
900:
898:
894:
889:
885:
880:
875:
872:(7): 2212–9.
871:
867:
863:
856:
853:
848:
844:
840:
836:
832:
828:
821:
818:
812:
810:
806:
804:
800:
797:
793:
784:
782:
780:
776:
772:
768:
764:
757:
751:
747:
745:
741:
733:
729:
723:
721:
719:
718:iodoacetamide
715:
711:
707:
699:
695:
688:
686:
684:
683:antibacterial
680:
679:antimicrobial
672:
666:
662:
660:
657:
653:
649:
646:
642:
637:
635:
631:
627:
622:
620:
616:
612:
608:
604:
600:
596:
592:
584:
578:
574:
572:
568:
564:
561:
557:
556:aromatic ring
552:
550:
549:electrophilic
546:
542:
539:
535:
532:
528:
524:
516:
514:
512:
504:
502:
500:
491:
489:
487:
483:
475:
473:
467:
461:
457:
455:
451:
447:
443:
439:
435:
431:
426:
425:
421:
417:
413:
409:
408:electrostatic
405:
401:
398:
394:
390:
386:
382:
378:
370:
368:
366:
362:
358:
354:
350:
346:
342:
338:
334:
330:
326:
322:
318:
315:
312:
308:
304:
300:
295:
293:
289:
285:
281:
277:
273:
264:
260:
259:
255:
251:
247:
243:
239:
236:
232:
220:
217:
215:
211:
208:
205:
203:
199:
196:
193:
191:
187:
182:
178:
175:
171:
168:
166:
165:Gene Ontology
162:
159:
156:
153:
150:
147:
143:
140:
137:
135:
131:
128:
125:
123:
119:
116:
113:
111:
107:
104:
103:NiceZyme view
101:
99:
95:
92:
89:
87:
83:
80:
77:
75:
71:
66:
63:
60:
58:
54:
51:
48:
46:
42:
37:
30:
25:
20:
2115:Translocases
2112:
2099:
2086:
2073:
2060:
2050:Transferases
2047:
2034:
1891:Binding site
1824:
1731:
1727:
1717:
1692:
1688:
1633:
1629:
1619:
1574:
1570:
1560:
1535:
1532:Biochemistry
1531:
1525:
1498:
1494:
1484:
1473:. Retrieved
1469:
1460:
1435:
1431:
1425:
1403:(2): 81–96.
1400:
1396:
1362:
1358:
1322:
1318:
1309:
1274:
1270:
1260:
1225:
1221:
1211:
1186:
1183:Biochemistry
1182:
1176:
1141:
1103:
1099:
1093:
1060:
1056:
1013:
1009:
981:
977:
925:
921:
869:
865:
855:
830:
827:Biochemistry
826:
820:
807:
803:side effects
788:
761:
737:
727:
703:
692:
676:
648:tautomerizes
638:
626:intermediate
623:
611:nucleophilic
599:deprotonated
588:
553:
520:
511:antiparallel
508:
495:
479:
471:
427:
374:
340:
314:biosynthesis
296:
284:homocysteine
269:
245:
241:
230:
229:
91:BRENDA entry
1886:Active site
1728:Amino Acids
799:replication
763:Arabidopsis
659:deamination
615:Schiff base
571:side chains
551:character.
482:beta-strand
446:type I fold
79:IntEnz view
39:Identifiers
2158:Categories
2089:Isomerases
2063:Hydrolases
1930:Regulation
1475:2017-03-09
813:References
673:Inhibition
656:hydrolytic
499:C-terminus
424:α-helices.
420:N-terminal
311:methionine
270:Thus, the
148:structures
115:KEGG entry
62:9055-05-4
1968:EC number
769:with its
758:Evolution
607:phenolate
591:mechanism
585:Mechanism
531:phosphate
371:Structure
297:Found in
272:substrate
254:catalyzes
68:Databases
2164:EC 4.4.1
1992:Kinetics
1916:Cofactor
1879:Activity
1758:25408465
1709:17300162
1452:21435402
1252:12232160
1085:24552794
1077:12715888
952:11402193
888:14209950
767:homology
738:Through
724:Bacteria
650:into an
634:p-system
619:aldimine
567:electron
563:tyrosine
560:coplanar
541:nitrogen
538:pyridine
527:hydroxyl
404:monomers
389:molecule
381:subunits
377:tetramer
329:cofactor
303:bacteria
288:pyruvate
280:products
258:reaction
248:, is an
219:proteins
207:articles
195:articles
152:RCSB PDB
2148:Biology
2102:Ligases
1872:Enzymes
1749:4302243
1670:3513164
1638:Bibcode
1611:9636232
1579:Bibcode
1552:9376370
1517:7706318
1417:7748903
1379:8831789
1339:9914259
1301:7670372
1292:2143167
1203:2405903
1168:8973544
1159:1217943
1120:8112347
1030:7840670
990:9165088
847:7049234
645:enamine
534:oxygens
468:Monomer
400:residue
317:pathway
292:ammonia
238:4.4.1.8
174:QuickGO
139:profile
122:MetaCyc
57:CAS no.
50:4.4.1.8
2134:Portal
2076:Lyases
1799:lyases
1756:
1746:
1707:
1668:
1661:322971
1658:
1609:
1599:
1550:
1515:
1450:
1415:
1377:
1337:
1299:
1289:
1250:
1243:159283
1240:
1201:
1166:
1156:
1118:
1083:
1075:
1028:
988:
950:
943:111155
940:
886:
845:
689:Plants
525:- and
440:, and
414:, and
397:lysine
363:, and
333:lyases
327:(PLP)
305:, and
299:plants
290:, and
250:enzyme
202:PubMed
184:Search
170:AmiGO
158:PDBsum
98:ExPASy
86:BRENDA
74:IntEnz
45:EC no.
16:Enzyme
2028:Types
1812:4.4.1
1602:22764
1081:S2CID
710:thiol
652:imine
523:Amine
395:by a
385:dimer
307:yeast
134:PRIAM
2120:list
2113:EC7
2107:list
2100:EC6
2094:list
2087:EC5
2081:list
2074:EC4
2068:list
2061:EC3
2055:list
2048:EC2
2042:list
2035:EC1
1805:4.4)
1754:PMID
1705:PMID
1666:PMID
1607:PMID
1548:PMID
1513:PMID
1448:PMID
1436:1814
1413:PMID
1401:1248
1375:PMID
1335:PMID
1297:PMID
1248:PMID
1199:PMID
1164:PMID
1116:PMID
1073:PMID
1026:PMID
986:PMID
948:PMID
884:PMID
843:PMID
742:and
716:and
595:bond
554:The
282:are
214:NCBI
155:PDBe
110:KEGG
1744:PMC
1736:doi
1697:doi
1656:PMC
1646:doi
1597:PMC
1587:doi
1540:doi
1503:doi
1499:270
1440:doi
1405:doi
1367:doi
1363:262
1327:doi
1287:PMC
1279:doi
1238:PMC
1230:doi
1226:104
1191:doi
1154:PMC
1146:doi
1108:doi
1104:219
1065:doi
1061:384
1018:doi
1014:316
982:378
938:PMC
930:doi
926:126
874:doi
870:239
835:doi
796:DNA
244:or
242:CBL
190:PMC
146:PDB
2160::
1803:EC
1752:.
1742:.
1732:47
1730:.
1726:.
1703:.
1693:50
1691:.
1678:^
1664:.
1654:.
1644:.
1634:83
1632:.
1628:.
1605:.
1595:.
1585:.
1575:95
1573:.
1569:.
1546:.
1536:36
1534:.
1511:.
1497:.
1493:.
1468:.
1446:.
1434:.
1411:.
1399:.
1387:^
1373:.
1361:.
1347:^
1333:.
1321:.
1295:.
1285:.
1273:.
1269:.
1246:.
1236:.
1224:.
1220:.
1197:.
1187:29
1185:.
1162:.
1152:.
1140:.
1128:^
1114:.
1102:.
1079:.
1071:.
1059:.
1038:^
1024:.
1012:.
998:^
980:.
960:^
946:.
936:.
924:.
920:.
896:^
882:.
868:.
864:.
841:.
831:21
829:.
805:.
720:.
621:.
603:pH
436:,
410:,
367:.
359:,
355:,
351:,
347::
301:,
294:.
286:,
235:EC
172:/
2136::
2122:)
2118:(
2109:)
2105:(
2096:)
2092:(
2083:)
2079:(
2070:)
2066:(
2057:)
2053:(
2044:)
2040:(
1864:e
1857:t
1850:v
1801:(
1790:e
1783:t
1776:v
1760:.
1738::
1711:.
1699::
1672:.
1648::
1640::
1613:.
1589::
1581::
1554:.
1542::
1519:.
1505::
1478:.
1454:.
1442::
1419:.
1407::
1381:.
1369::
1341:.
1329::
1323:8
1303:.
1281::
1275:4
1254:.
1232::
1205:.
1193::
1170:.
1148::
1122:.
1110::
1087:.
1067::
1032:.
1020::
992:.
954:.
932::
890:.
876::
849:.
837::
233:(
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