| 词条 | Radical SAM |
| 释义 |
| Symbol = Radical_SAM | Name = Radical_SAM | image = | width = | caption = | Pfam = PF04055 | Pfam_clan = | InterPro = IPR007197 | SMART = | PROSITE = | MEROPS = | SCOP = 102114 | TCDB = | OPM family = | OPM protein = | CAZy = | PDB = }} Radical SAM is a designation for a superfamily of enzymes that use a [4Fe-4S]+ cluster to reductively cleave S-adenosyl-L-methionine (SAM) to generate a radical, usually a 5′-deoxyadenosyl radical, as a critical intermediate.[1][2] These enzymes utilize this potent radical intermediate to perform an array of unusual (from the perspective of organic chemistry) transformations, often to functionalize unactivated C-H bonds. More than 110,000 enzymes use adomet.[3] Radical SAM enzymes are involved in cofactor biosynthesis, enzyme activation, peptide modification, post-transcriptional and post-translational modifications, metalloprotein cluster formation, tRNA modification, lipid metabolism, biosynthesis of antibiotics and natural products etc. The vast majority of known radical SAM enzymes belong to the radical SAM superfamily,[4][5] and have a cysteine-rich motif that matches or resembles CxxxCxxC. Some radical SAMs release methyl radicals.[6] ExamplesRadicalExamples of radical SAM enzymes found within the radical SAM superfamily include: {{div col|colwidth=30em}}
Non-canonicalIn addition, several non-canonical radical SAM enzymes have been described. These cannot be recognized by the Pfam hidden Markov model PF04055, but still use three Cys residues as ligands to a 4Fe4S cluster and produce a radical from S-adenosylmethionine. These include {{div col|colwidth=30em}}
References1. ^{{cite journal | vauthors = Broderick JB, Duffus BR, Duschene KS, Shepard EM | title = Radical S-adenosylmethionine enzymes | journal = Chemical Reviews | volume = 114 | issue = 8 | pages = 4229–317 | date = April 2014 | pmid = 24476342 | pmc = 4002137 | doi = 10.1021/cr4004709 }} 2. ^{{cite journal | vauthors = Booker SJ, Grove TL | title = Mechanistic and functional versatility of radical SAM enzymes | journal = F1000 Biology Reports | volume = 2 | pages = 52 | date = July 2010 | pmid = 21152342 | pmc = 2996862 | doi = 10.3410/B2-52 }} 3. ^{{cite journal|year=2018|journal=Annual Review of Biochemistry|title=A Rich Man, Poor Man Story of S-Adenosylmethionine and Cobalamin Revisited|authors=Jennifer Bridwell-Rabb, Tsehai A. J. Grell, Catherine L. Drennan|volume=87|pages=555–84|doi=10.1146/annurev-biochem-062917-012500|pmid=29925255}} 4. ^{{cite journal | vauthors = Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE | title = 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 | journal = Nucleic Acids Research | volume = 29 | issue = 5 | pages = 1097–106 | date = March 2001 | pmid = 11222759 | pmc = 29726 | doi = 10.1093/nar/29.5.1097 }} 5. ^{{cite journal | vauthors = Frey PA, Hegeman AD, Ruzicka FJ | title = The Radical SAM Superfamily | journal = Critical Reviews in Biochemistry and Molecular Biology | volume = 43 | issue = 1 | pages = 63–88 | year = 2008 | pmid = 18307109 | doi = 10.1080/10409230701829169 }} 6. ^{{cite journal | vauthors = Ribbe MW, Hu Y, Hodgson KO, Hedman B | title = Biosynthesis of nitrogenase metalloclusters | journal = Chemical Reviews | volume = 114 | issue = 8 | pages = 4063–80 | date = April 2014 | pmid = 24328215 | doi = 10.1021/cr400463x | pmc = 3999185 }} 7. ^{{cite journal | vauthors = Zhang Q, Li Y, Chen D, Yu Y, Duan L, Shen B, Liu W | title = Radical-mediated enzymatic carbon chain fragmentation-recombination | journal = Nature Chemical Biology | volume = 7 | issue = 3 | pages = 154–60 | date = March 2011 | pmid = 21240261 | pmc = 3079562 | doi = 10.1038/nchembio.512 }} 8. ^{{cite journal | vauthors = Bruender NA, Wilcoxen J, Britt RD, Bandarian V | title = Biochemical and Spectroscopic Characterization of a Radical S-Adenosyl-L-methionine Enzyme Involved in the Formation of a Peptide Thioether Cross-Link | journal = Biochemistry | volume = 55 | issue = 14 | pages = 2122–34 | date = April 2016 | pmid = 27007615 | doi = 10.1021/acs.biochem.6b00145 | pmc = 4829460 }} 9. ^{{cite journal | vauthors = Chatterjee A, Li Y, Zhang Y, Grove TL, Lee M, Krebs C, Booker SJ, Begley TP, Ealick SE | title = Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily | journal = Nature Chemical Biology | volume = 4 | issue = 12 | pages = 758–65 | date = December 2008 | pmid = 18953358 | pmc = 2587053 | doi = 10.1038/nchembio.121 }} 10. ^{{cite journal | vauthors = Zhang Y, Zhu X, Torelli AT, Lee M, Dzikovski B, Koralewski RM, Wang E, Freed J, Krebs C, Ealick SE, Lin H | title = Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme | journal = Nature | volume = 465 | issue = 7300 | pages = 891–6 | date = June 2010 | pmid = 20559380 | pmc = 3006227 | doi = 10.1038/nature09138 }} 11. ^{{cite journal | vauthors = Kamat SS, Williams HJ, Raushel FM | title = Intermediates in the transformation of phosphonates to phosphate by bacteria | journal = Nature | volume = 480 | issue = 7378 | pages = 570–3 | date = November 2011 | pmid = 22089136 | pmc = 3245791 | doi = 10.1038/nature10622 }} External links
1 : Enzymes |
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