{{Distinguish|Lenthionine|Lanthanide}} {{chembox | Watchedfields = changed |IUPACName=''S''-[(2''R'')-2-Amino-2-carboxyethyl]-<small>L</small>-cysteine | verifiedrevid = 443916395 | Name = Lanthionine | ImageFile = Lanthionin.svg |Section1={{Chembox Identifiers | PubChem = 256406 | ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}} | ChemSpiderID = 88959 | InChI = 1/C6H12N2O4S/c7-3(5(9)10)1-13-2-4(8)6(11)12/h3-4H,1-2,7-8H2,(H,9,10)(H,11,12)/t3-,4-/m0/s1 | InChIKey = DWPCPZJAHOETAG-IMJSIDKUBX | ChEBI_Ref = {{ebicite|correct|EBI}} | ChEBI = 21347 | SMILES = O=C(O)[C@@H](N)CSC[C@H](N)C(=O)O | StdInChI_Ref = {{stdinchicite|correct|chemspider}} | StdInChI = 1S/C6H12N2O4S/c7-3(5(9)10)1-13-2-4(8)6(11)12/h3-4H,1-2,7-8H2,(H,9,10)(H,11,12)/t3-,4-/m0/s1 | StdInChIKey_Ref = {{stdinchicite|correct|chemspider}} | StdInChIKey = DWPCPZJAHOETAG-IMJSIDKUSA-N | CASNo_Ref = {{cascite|correct|??}} | CASNo = 922-55-4 | UNII_Ref = {{fdacite|correct|FDA}} | UNII = JO78O46X3K }} |Section2={{Chembox Properties | Formula = C<sub>6</sub>H<sub>12</sub>N<sub>2</sub>O<sub>4</sub>S | MolarMass = 208.2318 g/mol | MeltingPtC = 280 to 283 | MeltingPt_notes = }} }} '''Lanthionine''' is a nonproteinogenic amino acid with the chemical formula (HOOC-CH(NH<sub>2</sub>)-CH<sub>2</sub>-S-CH<sub>2</sub>-CH(NH<sub>2</sub>)-COOH). It is typically formed by a cysteine residue and a dehydrated serine residue. Despite its name, lanthionine does not contain the element lanthanum.
==Background==
In 1941, lanthionine was first isolated by treating wool with sodium carbonate. It was found to be a sulfur-containing amino acid; accordingly it was given the name lanthionine [wool (Latin: ''Lana''), sulfur (Greek: ''theîon'')].<ref>Horn, M. J.; Jones, D. B.; Ringel, S. J. (1941) Isolation of a New Sulfur-Containing Amino Acid (Lanthionine) from Sodium Carbonate-Treated Wool. ''Journal of Biological Chemistry'', ''138'', 141-149.</ref> Lanthionine was first synthesized by alkylation of cysteine with β-chloroalanine.<ref>Brown, G. B.; du Vigneaud, V. (1941) The Stereoisomeric Forms of Lanthionine. ''Journal of Biological Chemistry'', ''140'', 767-771.</ref> Lanthionines are found widely in nature. They have been isolated from human hair, lactalbumin, and feathers. Lanthionines have also been found in bacterial cell walls and are the components of a group of gene-encoded peptide antibiotics called lantibiotics, which includes nisin (a food preservative), subtilin, epidermin (effective against ''Staphylococcus'' and ''Streptococcus''), and ancovenin (an enzyme inhibitor).<ref>Paul, M.; van der Donk, W. A. (2005) Chemical and Enzymatic Synthesis of Lanthionines. ''Mini-Reviews in Organic Chemistry'', ''2'', 23-37.</ref><ref name="shao">Shao, H.; Wang, S. H. H.; Lee, C.-W.; Ösapay, G.; Goodman, M. (1995) A Facile Synthesis of Orthogonally Protected Stereoisomeric Lanthionines by Regioselective Ring Opening of Serine β-Lactone Derivatives. ''Journal of Organic Chemistry'', ''60'', 2956-2957.</ref> Lanthionine is listed among novel uremic toxins, compounds elevated in blood of chronic kidney failure and uremic patiens.<ref>Garcia-Martinez Y, et al. Does gut microbiota dysbiosis impact the metabolic alterations of hydrogen sulfide and lanthionine in patients with chronic kidney disease ? BMC Microbiology 2024 10.1186/s12866-024-03590-0</ref> It likely contributes to hyperhomocysteinemia and impaired hydrogen sulfide biosynthesis.<ref>Perna AF, Di Nunzio A, Amoresano A, Pane F, Fontanarosa C, Pucci P, et al. Divergent behavior of hydrogen sulfide pools and of the sulfur metabolite lanthionine, a novel uremic toxin, in dialysis patients. Biochimie. 2016;126:97–107</ref> Lanthionine retention may also be linked to adverse cardiovascular outcomes as it can induce heart tissue fibrosis and promote vascular calcification.<ref>Coppola A, Vigorito C, Lombari P, Martínez YG, Borriello M, Trepiccione F, et al. Uremic Toxin Lanthionine induces endothelial cell mineralization in Vitro. Biomed. 2022;10:444.</ref>
==Preparation==
A variety of syntheses of lanthionine have been published including sulfur extrusion from cystine,<ref>Harpp, D. N.; Gleason, J. G. (1971) Preparation and Mass Spectral Properties of Cystine and Lanthionine Derivatives. Novel Synthesis of L-Lanthionine by Selective Desulfurization. ''Journal of Organic Chemistry'', ''36'', 73-80.</ref> ring opening of serine β-lactone,<ref name="shao"/> and hetero-conjugate addition of cysteine to dehydroalanine.<ref>Probert, J. M.; Rennex, D.; Bradley, M. (1996) Lanthionines for Solid Phase Synthesis. ''Tetrahedron Letters'', ''37'', 1101-1104.</ref> The sulfur extrusion method is, however, the only pathway for lanthionine that has been employed in the total synthesis of a lantibiotic.
Biosynthesis of the lanthionine bridge in peptidic natural products can be accomplished through a number of different pathways. For example, the lanthionine bridges in the antibiotic nisin are the result of a dedicated dehydratase (NisB) and a dedicated cyclase (NisC).<ref>{{cite journal |vauthors=Arnison PG, Bibb MJ, Bierbaum G, Bowers AA, Bugni TS, Bulaj G, Camarero JA, Campopiano DJ, Challis GL, Clardy J, Cotter PD, Craik DJ, Dawson M, Dittmann E, Donadio S, Dorrestein PC, Entian KD, Fischbach MA, Garavelli JS, Göransson U, Gruber CW, Haft DH, Hemscheidt TK, Hertweck C, Hill C, Horswill AR, Jaspars M, Kelly WL, Klinman JP, Kuipers OP, Link AJ, Liu W, Marahiel MA, Mitchell DA, Moll GN, Moore BS, Müller R, Nair SK, Nes IF, Norris GE, Olivera BM, Onaka H, Patchett ML, Piel J, Reaney MJ, Rebuffat S, Ross RP, Sahl HG, Schmidt EW, Selsted ME, Severinov K, Shen B, Sivonen K, Smith L, Stein T, Süssmuth RD, Tagg JR, Tang GL, Truman AW, Vederas JC, Walsh CT, Walton JD, Wenzel SC, Willey JM, van der Donk WA |author56-link=Roderich D. Süssmuth |title=Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature |journal=Nat Prod Rep |volume=30 |issue=1 |pages=108–60 |year=2013 |pmid=23165928 |pmc=3954855 |doi=10.1039/c2np20085f }}</ref><ref>{{cite journal |vauthors=Knerr PJ, van der Donk WA |title=Discovery, biosynthesis, and engineering of lantipeptides |journal=Annu. Rev. Biochem. |volume=81 |pages=479–505 |year=2012 |pmid=22404629 |doi=10.1146/annurev-biochem-060110-113521 }}</ref>
==References== <references/>
{{Non-proteinogenic amino acids}}
Category:Alpha-Amino acids Category:Sulfur amino acids Category:Thioethers Category:Non-proteinogenic amino acids