354:
469:
these atoms are modified, with O-methyltransferases representing the largest class. The methylated products of these reactions serve a variety of functions, including co-factors, pigments, signalling compounds, and metabolites. NPMTs can serve a regulatory role by modifying the reactivity and availability of these compounds. These enzymes are not highly conserved across different species, as they serve a more specific function in providing small molecules for specialized pathways in species or smaller groups of species. Reflective of this diversity is the variety of catalytic strategies, including general
485:
41:
241:
298:
681:
98:(SAH) during this process. The breaking of the SAM-methyl bond and the formation of the substrate-methyl bond happen nearly simultaneously. These enzymatic reactions are found in many pathways and are implicated in genetic diseases, cancer, and metabolic diseases. Another type of methyl transfer is the radical S-Adenosyl methionine (SAM) which is the methylation of unactivated carbon atoms in primary metabolites, proteins, lipids, and RNA.
2493:
33:
461:
655:
translational fidelity and RlmN catalyzes methylation of C2 of adenosine 2503 (A2503) in 23 S rRNA and C2 of adenosine (A37). Cfr, on the other hand, catalyzes methylation of C8 of A2503 as well and it also catalyzes C2 methylation. Class B is currently the largest class of radical SAM methylases which can methylate both
784:
In human cells, it was found that m5C was associated with abnormal tumor cells in cancer. The role and potential application of m5C includes to balance the impaired DNA in cancer both hypermethylation and hypomethylation. An epigenetic repair of DNA can be applied by changing the m5C amount in both
468:
Natural product methyltransferases (NPMTs) are a diverse group of enzymes that add methyl groups to naturally-produced small molecules. Like many methyltransferases, SAM is utilized as a methyl donor and SAH is produced. Methyl groups are added to S, N, O, or C atoms, and are classified by which of
381:
as a methyl donor and contain several highly conserved structural features between the three forms; these include the S-adenosylmethionine binding site, a vicinal proline-cysteine pair which forms a thiolate anion important for the reaction mechanism, and the cytosine substrate binding pocket. Many
654:
Based on different protein structures and mechanisms of catalysis, there are 3 different types of radical SAM (RS) methylases: Class A, B, and C. Class A RS methylases are the best characterized of the 4 enzymes and are related to both RlmN and Cfr. RlmN is ubiquitous in bacteria which enhances
667:
2-hybridized carbon atoms. The main difference that distinguishes Class B from others is the additional N-terminal cobalamin-binding domain that binds to the RS domain. Class C methylase has homologous sequence with the RS enzyme, coproporphyrinogen III oxidase (HemN), which also catalyzes the
275:, allowing other proteins to recognize methyl marks. The effect of this modification depends on the location of the modification on the histone tail and the other histone modifications around it. The location of the modifications can be partially determined by DNA sequence, as well as small
1227:
Narva, Kenneth E.; Van Etten, James L.; Slatko, Barton E.; Benner, Jack S. (1988-12-25). "The amino acid sequence of the eukaryotic DNA methyltransferase M·CviBIII, has regions of similarity with the prokaryotic isoschizomer M · TaqI and other DNA methyltransferases".
70:, and class III methyltransferases, which are membrane associated. Methyltransferases can also be grouped as different types utilizing different substrates in methyl transfer reactions. These types include protein methyltransferases, DNA/RNA methyltransferases,
448:
m6A was primarily found in prokaryotes until 2015 when it was also identified in some eukaryotes. m6A methyltransferases methylate the amino group in DNA at C-6 position specifically to prevent the host system to digest own genome through restriction enzymes.
226:
Natural product methyltransferases provide a variety of inputs into metabolic pathways, including the availability of cofactors, signalling molecules, and metabolites. This regulates various cellular pathways by controlling protein activity.
288:
condensation, while decreased transcription results from increased chromatin condensation. Methyl marks on the histones contribute to these changes by serving as sites for recruitment of other proteins that can further modify chromatin.
426:
as well as viral RNA species. Specific RNA methyltransferases are employed by cells to mark these on the RNA species according to the need and environment prevailing around the cells, which form a part of field called molecular
74:
methyltransferases, and non-SAM dependent methyltransferases. SAM is the classical methyl donor for methyltransferases, however, examples of other methyl donors are seen in nature. The general mechanism for methyl transfer is a
178:. The RCC1-chromatin interaction is also an example of a protein-DNA interaction, as another domain of RCC1 interacts directly with DNA when this protein is methylated. When RCC1 is not methylated, dividing cells have multiple
270:
substrates. Lysine amino acids can be modified with one, two, or three methyl groups, while
Arginine amino acids can be modified with one or two methyl groups. This increases the strength of the positive charge and residue
188:
methylated on lysine to regulate its activation and interaction with other proteins in the DNA damage response. This is an example of regulation of protein-protein interactions and protein activation. p53 is a known
700:. Cancer cells typically exhibit less DNA methylation activity in general, though often hypermethylation at sites which are unmethylated in normal cells; this overmethylation often functions as a way to inactivate
764:(SAM) analogs that carry alternative alkyl groups as a replacement for methyl. The development of the facile chemoenzymatic platform to generate and utilize differentially alkylated SAM analogs in the context of
1528:"Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods"
279:
and the methylation of the DNA itself. Most commonly, it is histone H3 or H4 that is methylated in vertebrates. Either increased or decreased transcription of genes around the modification can occur. Increased
827:
689:
452:
m5C plays a role to regulate gene transcription. m5C transferases are the enzymes that produce C5-methylcytosine in DNA at C-5 position of cytosine and are found in most plants and some eukaryotes.
353:
325:, or Proline. This reaction yields a methylated protein and SAH. Known targets of these methyltransferases in humans include RCC-1 (a regulator of nuclear transport proteins) and
708:
substrates, have been found to be highly toxic due to their similarity to cytosine (see right); this similarity to the nucleotide causes the inhibitor to be incorporated into
55:
their substrates but can be split into several subclasses based on their structural features. The most common class of methyltransferases is class I, all of which contain a
1992:
1783:
934:"Lysine methylation of the NF-ÎşB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-ÎşB signaling"
812:
266:
group on histone tails. Lysine methyltransferases and
Arginine methyltransferases are unique classes of enzymes, but both bind SAM as a methyl donor for their
1184:
Kessler, Christoph; Manta, Vicentiu (1990-01-01). "Specificity of restriction endonucleases and DNA modification methyltransferases — a review (edition 3)".
785:
types of cancer cells (hypermethylation/ hypomethylation) and as well as the environment of the cancers to reach an equivalent point to inhibit tumor cells.
205:. Overall, it responds to mutations in DNA, signaling to the cell to fix them or to initiate cell death so that these mutations cannot contribute to cancer.
301:
Representative scheme of reaction catalyzed by N-alpha methyltransferases, with representative substrate. The N-terminal residue that is modified is Serine.
1624:
Singh, S; Zhang, J; Huber, TD; Sunkara, M; Hurley, K; Goff, RD; Wang, G; Zhang, W; Liu, C; Rohr, J; Van Lanen, SG; Morris, AJ; Thorson, JS (7 April 2014).
773:
1314:
Liscombe, David K.; Louie, Gordon V.; Noel, Joseph P. (2012). "Architectures, mechanisms and molecular evolution of natural product methyltransferases".
688:
As with any biological process which regulates gene expression and/or function, anomalous DNA methylation is associated with genetic disorders such as
1823:
170:
of chromosomes. This is an example of regulation of protein-protein interaction, as methylation regulates the attachment of RCC1 to histone proteins
474:
2024:
2082:
139:
to the gene itself. Though the mechanisms of this genetic control are complex, hypo- and hypermethylation of DNA is implicated in many diseases.
394:. Many of the early DNA methyltransferases have been thought to be derived from RNA methyltransferases that were supposed to be active in the
1978:
1879:
2042:
1948:
2143:
36:
SET7/9, a representative histone methyltransferase with SAM (blue) and peptide undergoing methylation (black). Rendered from PDB: 4J83.
704:. Inhibition of overall DNA methyltransferase activity has been proposed as a treatment option, but DNMT inhibitors, analogs of their
1585:"Resistance to linezolid is mediated by the cfr gene in the first report of an outbreak of linezolid-resistant Staphylococcus aureus"
2167:
1922:
1845:
1583:
Morales G, Picazo JJ, Baos E, Candel FJ, Arribi A, Peláez B, Andrade R, de la Torre MA, Fereres J, Sánchez-GarcĂa M (March 2010).
733:: defects in this gene causes toxic accumulation of thiopurine compounds, drugs used in chemotherapy and immunosuppressant therapy
1271:
Posfai, Janos; Bhagwat, Ashok S.; Roberts, Richard J. (1988-12-25). "Sequence motifs specific for cytosine methyltransferases".
2153:
1869:
553:
1771:
1816:
2107:
1777:
377:, including DNMT1, DNMT2 (renamed TRDMT1 to reflect its function methylating tRNA, not DNA), and DNMT3. These enzymes use
2179:
1899:
1895:
760:
Recent work has revealed the methyltransferases involved in methylation of naturally occurring anticancer agents to use
990:
2212:
1366:
439:
methylation, m1G methylation as well as m5C are most commonly methylation marks observed in different types of RNA.
2063:
1809:
1789:
398:
to protect many species of primitive RNA. RNA methylation has been observed in different types of RNA species viz.
2138:
2019:
329:(a tumor suppressor protein that inhibits excessive cell division). RCC-1 methylation is especially important in
317:-Lysine consensus sequence is recognized by the methyltransferase. For all known substrates, the X amino acid is
148:
2128:
2123:
2047:
1927:
2368:
1904:
1864:
565:
387:
132:
223:, making methylation of NF-ÎşB a regulatory process by which cell signaling through this pathway is reduced.
2133:
1973:
1766:
1626:"Facile chemoenzymatic strategies for the synthesis and utilization of S-adenosyl-(L)-methionine analogues"
797:
730:
672:
2-hybridized carbon centers yet it lacks the 2 cysteines required for methylation in mechanism of Class A.
573:
627:
are all methyl donors found in biology as methyl group donors, typically in enzymatic reactions using the
481:
not requiring catalytic amino acids. NPMTs are the most functionally diverse class of methyltransferases.
2148:
1098:
Lan, J; Hua, S; He, X; Zhang, Y (2010). "DNA methyltransferases and methyl-binding proteins of mammals".
152:
390:, there are a variety of protein complexes, many with implications for human health, which only bind to
44:
The SN2-like methyl transfer reaction. Only the SAM cofactor and cytosine base are shown for simplicity.
2483:
1795:
2469:
2456:
2443:
2430:
2417:
2404:
2391:
2353:
1958:
1874:
807:
361:
DNA methylation, a key component of genetic regulation, occurs primarily at the 5-carbon of the base
248:
92:
67:
17:
2363:
2317:
2260:
2011:
1836:
1760:
281:
116:
357:
5'-methylcytosine molecule with methyl group, added by a DNA methyltransferase, highlighted in red
2265:
748:
723:
vectors capable of transmitting this gene are a cause of potentially dangerous cross resistance.
628:
620:
1801:
2068:
326:
1756:
663:
3-hybridized carbon atoms in different sets of substrates unlike Class A which only catalyzes
2286:
2205:
1968:
802:
761:
709:
701:
378:
374:
66:(SAM). Class II methyltransferases contain a SET domain, which are exemplified by SET domain
60:
211:(a protein involved in inflammation) is a known methylation target of the methyltransferase
2518:
2358:
1963:
1526:
Sofia, H. J.; Chen, G.; Hetzler, B. G.; Reyes-Spindola, J. F.; Miller, N. E. (2001-03-01).
391:
341:. When RCC-1 is not methylated, cell division is abnormal following the formation of extra
849:"Automated identification of putative methyltransferases from genomic open reading frames"
445:
S-adenosyl-L-methionine + DNA adenine S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
386:
throughout many classes of life, from bacteria to mammals. In addition to controlling the
8:
2322:
1932:
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817:
736:
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2255:
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40:
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914:
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342:
179:
1798:
Genetic pathways involving
Histone Methyltransferases from Cell Signaling Technology
635:
2301:
2296:
2270:
2198:
1725:
1645:
1637:
1596:
1555:
1539:
1498:
1480:
1469:"Mechanistic Diversity of Radical S-Adenosylmethionine (SAM)-dependent Methylation"
1354:
1323:
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1237:
1193:
1156:
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1027:
1019:
953:
945:
904:
860:
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600:
366:
338:
190:
87:
sulfur serves as the leaving group and the methyl group attached to it acts as the
1135:"Reviving the RNA World: An Insight into the Appearance of RNA Methyltransferases"
1084:
2348:
2332:
2245:
2086:
478:
71:
2497:
2386:
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1730:
1713:
1448:
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1404:
1382:
865:
848:
765:
639:
612:
581:
557:
470:
276:
272:
128:
345:. The function of Retinoblastoma protein N-terminal methylation is not known.
244:
General scheme of the reaction catalyzed by a lysine histone methyltransferase
2507:
2291:
2250:
1996:
1772:
A novel methyltransferase : the 7SK snRNA Methylphosphate
Capping Enzyme
1690:
1551:
1494:
1292:
1249:
1205:
1151:
693:
624:
608:
484:
240:
91:
that transfers the methyl group to the enzyme substrate. SAM is converted to
56:
1543:
1485:
719:
causes cross-resistance to other antibiotics that act on the ribosomal RNA.
2240:
1914:
1739:
1659:
1641:
1610:
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1512:
1335:
1170:
1119:
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1041:
967:
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561:
529:
334:
220:
88:
76:
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1300:
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1213:
1111:
715:
A methylase which alters the ribosomal RNA binding site of the antibiotic
2464:
2399:
2235:
1832:
744:
631:
604:
509:
464:
The reaction converting norepinephrine to epinephrine, catalyzed by PNMT.
428:
370:
297:
252:
175:
171:
112:
52:
1467:
Bauerle, Matthew R.; Schwalm, Erica L.; Booker, Squire J. (2015-02-13).
1449:"Catalysis of methyl group transfers involving tetrahydrofolate and B12"
1068:
1008:"Histone methylation: a dynamic mark in health, disease and inheritance"
680:
488:
SAM donates a methyl group through a radical mechanism in production of
215:, which turns off NF-ÎşB signaling by inhibiting of one of its subunits,
1327:
1313:
310:
306:
202:
194:
167:
84:
684:
biological methyl donors with relevant methyl group highlighted in red
2438:
2412:
2092:
716:
569:
395:
285:
263:
198:
124:
1023:
949:
634:. These substrates contribute to methyl transfer pathways including
2492:
1601:
1584:
705:
596:
585:
489:
362:
305:
N-alpha methyltransferases transfer a methyl group from SAM to the
260:
136:
1784:"Nutrition and Depression: Nutrition, Methylation, and Depression"
1353:. Advances in Botanical Research. Vol. 68. pp. 111–138.
886:
884:
208:
127:
structure and can modulate gene transcription, or even completely
2171:
1831:
755:
720:
330:
318:
314:
267:
163:
2451:
2221:
2001:
1953:
881:
442:
6A is an enzyme that catalyzes chemical reaction as following:
411:
322:
256:
1525:
983:
Chromatin and gene regulation : mechanisms in epigenetics
2425:
423:
419:
415:
212:
726:
Examples of methyltransferase enzymes relevant to disease:
407:
403:
399:
216:
2190:
1226:
552:
Important examples of this enzyme class in humans include
460:
436:
185:
32:
1349:
Ashihara, Hiroshi; Yokota, Takao; Crozier, Alan (2013).
1582:
1055:
Clarke, Paul (May 2007). "Anchoring RCC1 by the tail".
813:
5-Methyltetrahydrofolate-homocysteine methyltransferase
591:
1623:
890:
2481:
1348:
846:
455:
1466:
1270:
166:
protein, is methylated so that it can interact with
779:
1630:Angewandte Chemie International Edition in English
219:. This reduces the transcriptional activation and
847:Katz, J. E.; Dlakic, M; Clarke S (18 July 2003).
712:, causing non-functioning DNA to be synthesized.
649:
147:Methylation of proteins has a regulatory role in
2505:
2025:3-methyl-2-oxobutanoate hydroxymethyltransferase
292:
1351:Biosynthesis and catabolism of purine alkaloids
1005:
756:Applications in drug discovery and development
580:(COMT) degrades a class of molecules known as
382:features of DNA methyltransferases are highly
2206:
1979:Cyclopropane-fatty-acyl-phospholipid synthase
1817:
1383:"PNMT phenylethanolamine N-methyltransferase"
1097:
348:
313:is first cleaved by another enzyme and the X-
235:
1880:Phosphatidylethanolamine N-methyltransferase
1790:"DNA Methylation - What is DNA Methylation?"
1778:"The Role of Methylation in Gene Expression"
1576:
1183:
309:nitrogen on protein targets. The N-terminal
2043:Phosphoribosylglycinamide formyltransferase
1949:Phosphatidyl ethanolamine methyltransferase
333:as it coordinates the localization of some
251:are critical for genetic regulation at the
2213:
2199:
2144:3-hydroxymethylcephem carbamoyltransferase
1824:
1810:
1714:"Hallmarks of Cancer: The Next Generation"
1133:Rana, Ajay K.; Ankri, Serge (2016-01-01).
1006:Greer, Eric L.; Shi, Yang (3 April 2012).
932:Levy, Dan; et al. (5 December 2010).
1759:at the U.S. National Library of Medicine
1729:
1649:
1600:
1559:
1502:
1484:
1160:
1150:
1132:
1031:
957:
908:
864:
679:
675:
572:in the process of histamine metabolism.
483:
459:
296:
239:
39:
31:
1712:D, Hanahan; Ra, Weinberg (2011-03-04).
891:Siedlecki, P; Zielenkiewicz, P (2006).
14:
2506:
2154:N-acetylornithine carbamoyltransferase
1923:Betaine-homocysteine methyltransferase
1870:Phenylethanolamine N-methyltransferase
1767:3-D Structure of DNA Methyltransferase
1054:
980:
554:phenylethanolamine N-methyltransferase
51:are a large group of enzymes that all
2194:
1805:
1672:
1462:
1460:
142:
2108:methylmalonyl-CoA carboxytransferase
1405:"HNMT histamine N-methyltransferase"
1100:Acta Biochimica et Biophysica Sinica
931:
592:Non-SAM dependent methyltransferases
588:, epinephrine, and norepenepherine.
83:-like nucleophilic attack where the
2180:Arginine:glycine amidinotransferase
1900:Acetylserotonin O-methyltransferase
1896:5-hydroxyindole-O-methyltransferase
1711:
1675:"DNA Methylation Errors and Cancer"
1473:The Journal of Biological Chemistry
1427:"COMT catechol-O-methyltransferase"
853:Molecular & Cellular Proteomics
747:deficiency, is caused by a lack of
24:
1750:
1457:
1359:10.1016/B978-0-12-408061-4.00004-3
893:"Mammalian DNA methyltransferases"
751:for the methionine synthase enzyme
456:Natural product methyltransferases
352:
25:
2530:
985:. Malden, MA: Blackwell Science.
2491:
2064:Glutamate formimidoyltransferase
780:Applications in cancer treatment
392:methylated DNA recognition sites
2139:Putrescine carbamoyltransferase
2020:Serine hydroxymethyltransferase
1705:
1666:
1617:
1519:
1441:
1429:. NCBI Genetic Testing Registry
1419:
1407:. NCBI Genetic Testing Registry
1397:
1385:. NCBI Genetic Testing Registry
1375:
1342:
1307:
1264:
1220:
337:proteins in the absence of the
2129:Ornithine carbamoyltransferase
2124:Aspartate carbamoyltransferase
2048:Inosine monophosphate synthase
1928:Homocysteine methyltransferase
1673:Jones, Peter A. (1996-06-01).
1177:
1126:
1091:
1048:
999:
974:
925:
840:
650:Radical SAM methyltransferases
369:(see left). Methylation is an
111:Methylation, as well as other
13:
1:
1905:Catechol-O-methyl transferase
1865:Histamine N-methyltransferase
833:
828:corrinoid-iron sulfur protein
621:methyltetrahydromethanopterin
566:histamine N-methyltransferase
375:DNA methyltransferase enzymes
293:N-terminal methyltransferases
2134:Oxamate carbamoyltransferase
1974:Thiopurine methyltransferase
1796:"Histone Lysine Methylation"
1285:10.1016/0378-1119(88)90299-5
1242:10.1016/0378-1119(88)90298-3
1198:10.1016/0378-1119(90)90486-B
798:Catechol-O-methyltransferase
731:thiopurine methyltransferase
182:and usually cannot survive.
149:protein–protein interactions
29:Group of methylating enzymes
7:
2220:
2149:Lysine carbamoyltransferase
1835:: one carbon transferases (
788:
388:expression of certain genes
106:
101:
10:
2535:
1731:10.1016/j.cell.2011.02.013
866:10.1074/mcp.M300037-MCP200
512:(alkaloid in chocolate) (R
373:modification catalyzed by
349:DNA/RNA methyltransferases
259:on the ε-nitrogen and the
255:level. They modify mainly
249:Histone methyltransferases
236:Histone methyltransferases
155:, and protein activation.
68:histone methyltransferases
2377:
2369:Michaelis–Menten kinetics
2341:
2310:
2279:
2228:
2166:
2116:
2100:
2081:
2056:
2033:
2010:
1991:
1959:Histone methyltransferase
1941:
1913:
1888:
1875:Amine N-methyltransferase
1857:
1844:
981:Turner, Bryan M. (2001).
808:Histone methyltransferase
568:(HNMT), which methylates
284:is a result of decreased
2261:Diffusion-limited enzyme
2012:Hydroxymethyltransferase
1761:Medical Subject Headings
1152:10.3389/fgene.2016.00099
897:Acta Biochimica Polonica
230:
153:protein–DNA interactions
1486:10.1074/jbc.R114.607044
1316:Natural Product Reports
1012:Nature Reviews Genetics
636:methionine biosynthesis
601:methyl tetrahydrofolate
556:(PNMT), which converts
115:modifications, affects
2069:Aminomethyltransferase
1642:10.1002/anie.201308272
1532:Nucleic Acids Research
910:10.18388/abp.2006_3337
702:tumor-suppressor genes
685:
549:
465:
358:
327:Retinoblastoma protein
302:
245:
123:. It directly impacts
119:, gene stability, and
96:-Adenosyl homocysteine
45:
37:
2354:Eadie–Hofstee diagram
2287:Allosteric regulation
1969:DNA methyltransferase
1792:from News-Medical.net
1544:10.1093/nar/29.5.1097
1452:Vitamins and Hormones
1139:Frontiers in Genetics
803:DNA methyltransferase
762:S-Adenosyl methionine
683:
676:Clinical significance
487:
475:metal-based catalysis
463:
356:
300:
243:
221:inflammatory response
43:
35:
2364:Lineweaver–Burk plot
1964:Thymidylate synthase
477:, and proximity and
379:S-adenosylmethionine
197:pathways, initiates
64:-Adenosyl methionine
1933:Methionine synthase
1786:on Psychology Today
1774:as seen on Flintbox
1112:10.1093/abbs/gmq015
1069:10.1038/ncb0507-485
1057:Nature Cell Biology
823:methionine synthase
818:O-methyltransferase
737:methionine synthase
479:desolvation effects
471:acid-base catalysis
121:parental imprinting
2323:Enzyme superfamily
2256:Enzyme promiscuity
1780:on Nature Scitable
1757:Methyltransferases
1328:10.1039/c2np20029e
793:Examples include:
774:alkylrandomization
698:Fragile X syndrome
686:
578:-methyltransferase
550:
466:
359:
303:
246:
143:Protein regulation
49:Methyltransferases
46:
38:
2479:
2478:
2188:
2187:
2162:
2161:
2077:
2076:
2035:Formyltransferase
1987:
1986:
1685:(11): 2463–2467.
1589:Clin. Infect. Dis
938:Nature Immunology
741:pernicious anemia
659:2-hybridized and
201:, and pauses the
16:(Redirected from
2526:
2496:
2495:
2487:
2359:Hanes–Woolf plot
2302:Enzyme activator
2297:Enzyme inhibitor
2271:Enzyme catalysis
2215:
2208:
2201:
2192:
2191:
2098:
2097:
2008:
2007:
1855:
1854:
1826:
1819:
1812:
1803:
1802:
1744:
1743:
1733:
1709:
1703:
1702:
1670:
1664:
1663:
1653:
1621:
1615:
1614:
1604:
1580:
1574:
1573:
1563:
1538:(5): 1097–1106.
1523:
1517:
1516:
1506:
1488:
1479:(7): 3995–4002.
1464:
1455:
1445:
1439:
1438:
1436:
1434:
1423:
1417:
1416:
1414:
1412:
1401:
1395:
1394:
1392:
1390:
1379:
1373:
1372:
1346:
1340:
1339:
1311:
1305:
1304:
1268:
1262:
1261:
1224:
1218:
1217:
1181:
1175:
1174:
1164:
1154:
1130:
1124:
1123:
1095:
1089:
1088:
1052:
1046:
1045:
1035:
1003:
997:
996:
978:
972:
971:
961:
929:
923:
922:
912:
888:
879:
878:
868:
844:
770:drug development
433:2'-O-methylation
367:5’methylcytosine
339:nuclear envelope
191:tumor suppressor
21:
2534:
2533:
2529:
2528:
2527:
2525:
2524:
2523:
2504:
2503:
2502:
2490:
2482:
2480:
2475:
2387:Oxidoreductases
2373:
2349:Enzyme kinetics
2337:
2333:List of enzymes
2306:
2275:
2246:Catalytic triad
2224:
2219:
2189:
2184:
2158:
2112:
2090:
2073:
2052:
2029:
2000:
1983:
1937:
1909:
1884:
1840:
1830:
1753:
1751:Further reading
1748:
1747:
1710:
1706:
1679:Cancer Research
1671:
1667:
1622:
1618:
1581:
1577:
1524:
1520:
1465:
1458:
1447:Ragsdale, S.W.
1446:
1442:
1432:
1430:
1425:
1424:
1420:
1410:
1408:
1403:
1402:
1398:
1388:
1386:
1381:
1380:
1376:
1369:
1347:
1343:
1322:(10): 1238–50.
1312:
1308:
1269:
1265:
1225:
1221:
1182:
1178:
1131:
1127:
1096:
1092:
1053:
1049:
1024:10.1038/nrg3173
1004:
1000:
993:
979:
975:
950:10.1038/ni.1968
930:
926:
889:
882:
845:
841:
836:
791:
782:
758:
710:DNA translation
678:
668:methylation of
652:
594:
547:
543:
539:
535:
527:
523:
519:
515:
507:
503:
499:
495:
458:
351:
295:
277:non-coding RNAs
238:
233:
193:that activates
162:, an important
145:
135:genes, without
109:
104:
80:
72:natural product
30:
23:
22:
15:
12:
11:
5:
2532:
2522:
2521:
2516:
2501:
2500:
2477:
2476:
2474:
2473:
2460:
2447:
2434:
2421:
2408:
2395:
2381:
2379:
2375:
2374:
2372:
2371:
2366:
2361:
2356:
2351:
2345:
2343:
2339:
2338:
2336:
2335:
2330:
2325:
2320:
2314:
2312:
2311:Classification
2308:
2307:
2305:
2304:
2299:
2294:
2289:
2283:
2281:
2277:
2276:
2274:
2273:
2268:
2263:
2258:
2253:
2248:
2243:
2238:
2232:
2230:
2226:
2225:
2218:
2217:
2210:
2203:
2195:
2186:
2185:
2183:
2182:
2176:
2174:
2164:
2163:
2160:
2159:
2157:
2156:
2151:
2146:
2141:
2136:
2131:
2126:
2120:
2118:
2114:
2113:
2111:
2110:
2104:
2102:
2095:
2079:
2078:
2075:
2074:
2072:
2071:
2066:
2060:
2058:
2054:
2053:
2051:
2050:
2045:
2039:
2037:
2031:
2030:
2028:
2027:
2022:
2016:
2014:
2005:
1989:
1988:
1985:
1984:
1982:
1981:
1976:
1971:
1966:
1961:
1956:
1951:
1945:
1943:
1939:
1938:
1936:
1935:
1930:
1925:
1919:
1917:
1911:
1910:
1908:
1907:
1902:
1892:
1890:
1886:
1885:
1883:
1882:
1877:
1872:
1867:
1861:
1859:
1852:
1842:
1841:
1829:
1828:
1821:
1814:
1806:
1800:
1799:
1793:
1787:
1781:
1775:
1769:
1764:
1752:
1749:
1746:
1745:
1704:
1665:
1636:(15): 3965–9.
1616:
1602:10.1086/650574
1575:
1518:
1456:
1440:
1418:
1396:
1374:
1367:
1341:
1306:
1279:(1): 261–265.
1263:
1236:(1): 253–259.
1219:
1176:
1125:
1090:
1063:(5): 485–487.
1047:
1018:(5): 343–357.
998:
992:978-0865427433
991:
973:
924:
880:
838:
837:
835:
832:
831:
830:
825:
820:
815:
810:
805:
800:
790:
787:
781:
778:
766:drug discovery
757:
754:
753:
752:
734:
677:
674:
651:
648:
640:methanogenesis
613:trimethylamine
593:
590:
584:that includes
558:norepinephrine
545:
541:
537:
533:
525:
521:
517:
513:
505:
501:
497:
493:
457:
454:
350:
347:
294:
291:
273:hydrophobicity
237:
234:
232:
229:
144:
141:
108:
105:
103:
100:
78:
28:
9:
6:
4:
3:
2:
2531:
2520:
2517:
2515:
2512:
2511:
2509:
2499:
2494:
2489:
2488:
2485:
2471:
2467:
2466:
2461:
2458:
2454:
2453:
2448:
2445:
2441:
2440:
2435:
2432:
2428:
2427:
2422:
2419:
2415:
2414:
2409:
2406:
2402:
2401:
2396:
2393:
2389:
2388:
2383:
2382:
2380:
2376:
2370:
2367:
2365:
2362:
2360:
2357:
2355:
2352:
2350:
2347:
2346:
2344:
2340:
2334:
2331:
2329:
2328:Enzyme family
2326:
2324:
2321:
2319:
2316:
2315:
2313:
2309:
2303:
2300:
2298:
2295:
2293:
2292:Cooperativity
2290:
2288:
2285:
2284:
2282:
2278:
2272:
2269:
2267:
2264:
2262:
2259:
2257:
2254:
2252:
2251:Oxyanion hole
2249:
2247:
2244:
2242:
2239:
2237:
2234:
2233:
2231:
2227:
2223:
2216:
2211:
2209:
2204:
2202:
2197:
2196:
2193:
2181:
2178:
2177:
2175:
2173:
2169:
2165:
2155:
2152:
2150:
2147:
2145:
2142:
2140:
2137:
2135:
2132:
2130:
2127:
2125:
2122:
2121:
2119:
2115:
2109:
2106:
2105:
2103:
2099:
2096:
2094:
2088:
2084:
2080:
2070:
2067:
2065:
2062:
2061:
2059:
2055:
2049:
2046:
2044:
2041:
2040:
2038:
2036:
2032:
2026:
2023:
2021:
2018:
2017:
2015:
2013:
2009:
2006:
2004:- and Related
2003:
1998:
1997:Hydroxymethyl
1994:
1990:
1980:
1977:
1975:
1972:
1970:
1967:
1965:
1962:
1960:
1957:
1955:
1952:
1950:
1947:
1946:
1944:
1940:
1934:
1931:
1929:
1926:
1924:
1921:
1920:
1918:
1916:
1912:
1906:
1903:
1901:
1897:
1894:
1893:
1891:
1887:
1881:
1878:
1876:
1873:
1871:
1868:
1866:
1863:
1862:
1860:
1856:
1853:
1851:
1847:
1843:
1838:
1834:
1827:
1822:
1820:
1815:
1813:
1808:
1807:
1804:
1797:
1794:
1791:
1788:
1785:
1782:
1779:
1776:
1773:
1770:
1768:
1765:
1762:
1758:
1755:
1754:
1741:
1737:
1732:
1727:
1724:(5): 646–74.
1723:
1719:
1715:
1708:
1700:
1696:
1692:
1688:
1684:
1680:
1676:
1669:
1661:
1657:
1652:
1647:
1643:
1639:
1635:
1631:
1627:
1620:
1612:
1608:
1603:
1598:
1594:
1590:
1586:
1579:
1571:
1567:
1562:
1557:
1553:
1549:
1545:
1541:
1537:
1533:
1529:
1522:
1514:
1510:
1505:
1500:
1496:
1492:
1487:
1482:
1478:
1474:
1470:
1463:
1461:
1453:
1450:
1444:
1428:
1422:
1406:
1400:
1384:
1378:
1370:
1368:9780124080614
1364:
1360:
1356:
1352:
1345:
1337:
1333:
1329:
1325:
1321:
1317:
1310:
1302:
1298:
1294:
1290:
1286:
1282:
1278:
1274:
1267:
1259:
1255:
1251:
1247:
1243:
1239:
1235:
1231:
1223:
1215:
1211:
1207:
1203:
1199:
1195:
1191:
1187:
1180:
1172:
1168:
1163:
1158:
1153:
1148:
1144:
1140:
1136:
1129:
1121:
1117:
1113:
1109:
1106:(4): 243–52.
1105:
1101:
1094:
1086:
1082:
1078:
1074:
1070:
1066:
1062:
1058:
1051:
1043:
1039:
1034:
1029:
1025:
1021:
1017:
1013:
1009:
1002:
994:
988:
984:
977:
969:
965:
960:
955:
951:
947:
943:
939:
935:
928:
920:
916:
911:
906:
903:(2): 245–56.
902:
898:
894:
887:
885:
876:
872:
867:
862:
859:(8): 525–40.
858:
854:
850:
843:
839:
829:
826:
824:
821:
819:
816:
814:
811:
809:
806:
804:
801:
799:
796:
795:
794:
786:
777:
775:
771:
767:
763:
750:
746:
742:
738:
735:
732:
729:
728:
727:
724:
722:
718:
713:
711:
707:
703:
699:
695:
694:Rett syndrome
691:
682:
673:
671:
666:
662:
658:
647:
645:
641:
637:
633:
630:
626:
625:chloromethane
622:
618:
614:
610:
606:
602:
598:
589:
587:
583:
582:catcholamines
579:
577:
571:
567:
563:
559:
555:
531:
511:
491:
486:
482:
480:
476:
472:
462:
453:
450:
446:
443:
440:
438:
434:
430:
425:
421:
417:
413:
409:
405:
401:
397:
393:
389:
385:
380:
376:
372:
368:
364:
355:
346:
344:
343:spindle poles
340:
336:
332:
328:
324:
320:
316:
312:
308:
299:
290:
287:
283:
282:transcription
278:
274:
269:
265:
262:
258:
254:
250:
242:
228:
224:
222:
218:
214:
210:
206:
204:
200:
196:
192:
187:
183:
181:
180:spindle poles
177:
173:
169:
165:
161:
156:
154:
150:
140:
138:
134:
130:
126:
122:
118:
117:transcription
114:
99:
97:
95:
90:
86:
82:
73:
69:
65:
63:
58:
57:Rossmann fold
54:
50:
42:
34:
27:
19:
2465:Translocases
2462:
2449:
2436:
2423:
2410:
2400:Transferases
2397:
2384:
2241:Binding site
1915:Homocysteine
1849:
1721:
1717:
1707:
1682:
1678:
1668:
1633:
1629:
1619:
1595:(6): 821–5.
1592:
1588:
1578:
1535:
1531:
1521:
1476:
1472:
1451:
1443:
1431:. Retrieved
1421:
1409:. Retrieved
1399:
1387:. Retrieved
1377:
1350:
1344:
1319:
1315:
1309:
1276:
1272:
1266:
1233:
1229:
1222:
1192:(1): 1–240.
1189:
1185:
1179:
1142:
1138:
1128:
1103:
1099:
1093:
1060:
1056:
1050:
1015:
1011:
1001:
982:
976:
944:(1): 29–36.
941:
937:
927:
900:
896:
856:
852:
842:
792:
783:
772:is known as
759:
743:, caused by
725:
714:
687:
669:
664:
660:
656:
653:
644:acetogenesis
617:methanethiol
595:
575:
551:
530:theophylline
467:
451:
447:
444:
441:
360:
304:
247:
225:
207:
184:
157:
146:
110:
93:
89:electrophile
61:
59:for binding
48:
47:
26:
2519:Methylation
2236:Active site
1833:Transferase
1433:18 February
1411:18 February
1389:18 February
745:Vitamin B12
632:vitamin B12
562:epinephrine
510:theobromine
429:epigenetics
264:guanidinium
168:centromeres
2508:Categories
2439:Isomerases
2413:Hydrolases
2280:Regulation
834:References
371:epigenetic
365:, forming
311:methionine
307:N-terminal
253:epigenetic
203:cell cycle
195:DNA repair
158:Examples:
113:epigenetic
85:methionine
2318:EC number
2117:Carbamoyl
2093:Carbamoyl
1691:0008-5472
1552:1362-4962
1495:0021-9258
1293:0378-1119
1250:0378-1119
1206:0378-1119
717:linezolid
574:Catechol-
570:histamine
396:RNA world
384:conserved
286:chromatin
199:apoptosis
125:chromatin
53:methylate
18:Methylase
2514:EC 2.1.1
2342:Kinetics
2266:Cofactor
2229:Activity
1740:21376230
1660:24616228
1611:20144045
1570:11222759
1513:25477520
1336:22850796
1171:27375676
1120:20383462
1077:17473856
1042:22473383
968:21131967
919:16582985
875:12872006
789:Examples
749:cofactor
706:cytosine
629:cofactor
597:Methanol
586:dopamine
490:caffeine
363:cytosine
261:arginine
137:mutation
133:activate
107:Genetics
102:Function
2498:Biology
2452:Ligases
2222:Enzymes
2172:Amidine
2101:Carboxy
2087:Carboxy
1850:Methyl-
1699:8653676
1651:4076696
1504:4326810
1454:, 2008.
1301:3248729
1258:3248728
1214:2172084
1162:4893491
1033:4073795
959:3074206
721:Plasmid
335:nuclear
331:mitosis
319:Alanine
315:Proline
268:histone
164:mitotic
129:silence
2484:Portal
2426:Lyases
2002:Formyl
1954:DNMT3B
1763:(MeSH)
1738:
1697:
1689:
1658:
1648:
1609:
1568:
1558:
1550:
1511:
1501:
1493:
1365:
1334:
1299:
1291:
1256:
1248:
1212:
1204:
1169:
1159:
1145:: 99.
1118:
1085:711645
1083:
1075:
1040:
1030:
989:
966:
956:
917:
873:
696:, and
642:, and
623:, and
611:, and
564:, and
528:) and
516:= H, R
412:snoRNA
323:Serine
257:lysine
2378:Types
2168:2.1.4
2083:2.1.3
2057:Other
1993:2.1.2
1942:Other
1846:2.1.1
1561:29726
1081:S2CID
605:mono-
548:= H).
424:tmRNA
420:miRNA
416:snRNA
231:Types
213:SETD6
209:NF-ÎşB
2470:list
2463:EC7
2457:list
2450:EC6
2444:list
2437:EC5
2431:list
2424:EC4
2418:list
2411:EC3
2405:list
2398:EC2
2392:list
2385:EC1
2091:and
1839:2.1)
1736:PMID
1718:Cell
1695:PMID
1687:ISSN
1656:PMID
1607:PMID
1566:PMID
1548:ISSN
1509:PMID
1491:ISSN
1435:2014
1413:2014
1391:2014
1363:ISBN
1332:PMID
1297:PMID
1289:ISSN
1273:Gene
1254:PMID
1246:ISSN
1230:Gene
1210:PMID
1202:ISSN
1186:Gene
1167:PMID
1116:PMID
1073:PMID
1038:PMID
987:ISBN
964:PMID
915:PMID
871:PMID
768:and
540:= CH
524:= CH
504:= CH
408:tRNA
404:rRNA
400:mRNA
217:RelA
174:and
160:RCC1
1726:doi
1722:144
1646:PMC
1638:doi
1597:doi
1556:PMC
1540:doi
1499:PMC
1481:doi
1477:290
1355:doi
1324:doi
1281:doi
1238:doi
1194:doi
1157:PMC
1147:doi
1108:doi
1065:doi
1028:PMC
1020:doi
954:PMC
946:doi
905:doi
861:doi
690:ICF
609:di-
560:to
544:, R
536:= R
520:= R
508:),
500:= R
496:= R
437:m6A
186:p53
176:H2B
172:H2A
131:or
2510::
2170::
2085::
1999:-,
1995::
1889:O-
1858:N-
1848::
1837:EC
1734:.
1720:.
1716:.
1693:.
1683:56
1681:.
1677:.
1654:.
1644:.
1634:53
1632:.
1628:.
1605:.
1593:50
1591:.
1587:.
1564:.
1554:.
1546:.
1536:29
1534:.
1530:.
1507:.
1497:.
1489:.
1475:.
1471:.
1459:^
1361:.
1330:.
1320:29
1318:.
1295:.
1287:.
1277:74
1275:.
1252:.
1244:.
1234:74
1232:.
1208:.
1200:.
1190:92
1188:.
1165:.
1155:.
1141:.
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