| Revision as of 14:07, 8 August 2011 editBeetstra (talk | contribs)Edit filter managers, Administrators172,031 edits Script assisted update of identifiers for the Chem/Drugbox validation project (updated: 'DrugBank').← Previous edit |
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{{chembox |
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{{chembox |
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| verifiedrevid = 443736092 |
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| ImageFile = Dehydroalanin.svg |
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| ImageSize = 150px |
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| verifiedrevid = 399890360 |
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| ImageName = Structural formula |
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| ImageFile = Dehydroalanin.svg |
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| ImageFile1 = Dehydroalanine-zwitterion-3D-balls.png |
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| ImageSize = 150px |
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| ImageSize1 = 150px |
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| ImageName = Structural formula |
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| ImageName1 = Ball-and-stick model of the zwitterion |
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| ImageFile1 = Dehydroalanine-zwitterion-3D-balls.png |
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| PIN = 2-Aminoprop-2-enoic acid |
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| ImageSize1 = 150px |
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| OtherNames = |
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| ImageName1 = Ball-and-stick model of the zwitterion |
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| IUPACName = 2-Aminoprop-2-enoic acid |
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| OtherNames = |
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|Section1={{Chembox Identifiers |
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|Section1={{Chembox Identifiers |
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| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}} |
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| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}} |
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| ChemSpiderID = 110510 |
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| ChemSpiderID = 110510 |
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| KEGG_Ref = {{keggcite|changed|kegg}} |
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| KEGG_Ref = {{keggcite|correct|kegg}} |
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| KEGG = C02218 |
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| KEGG = C02218 |
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| InChI = 1/C3H5NO2/c1-2(4)3(5)6/h1,4H2,(H,5,6) |
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| InChI = 1/C3H5NO2/c1-2(4)3(5)6/h1,4H2,(H,5,6) |
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| StdInChIKey_Ref = {{stdinchicite|correct|chemspider}} |
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| StdInChIKey_Ref = {{stdinchicite|correct|chemspider}} |
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| StdInChIKey = UQBOJOOOTLPNST-UHFFFAOYSA-N |
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| StdInChIKey = UQBOJOOOTLPNST-UHFFFAOYSA-N |
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| CASNo_Ref = {{cascite|correct|??}} |
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| CASNo=1948-56-7 |
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| CASNo=1948-56-7 |
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| UNII_Ref = {{fdacite|correct|FDA}} |
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| PubChem=123991 |
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| UNII = 98RA387EKY |
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| ChEBI_Ref = {{ebicite|changed|EBI}} |
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| PubChem=123991 |
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| ChEBI_Ref = {{ebicite|correct|EBI}} |
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| ChEBI = 17123 |
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| ChEBI = 17123 |
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| DrugBank_Ref = {{drugbankcite|correct|drugbank}} |
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| DrugBank = DB02688 |
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| DrugBank = DB02688 |
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| SMILES=C=C(C(=O)O)N |
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| SMILES=C=C(C(=O)O)N |
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|Section2={{Chembox Properties |
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|Section2={{Chembox Properties |
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| Formula=C<sub>3</sub>H<sub>5</sub>NO<sub>2</sub> |
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| Formula=C<sub>3</sub>H<sub>5</sub>NO<sub>2</sub> |
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| MolarMass=87.08 g/mol |
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| MolarMass=87.08 g/mol |
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|Section3={{Chembox Hazards |
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'''Dehydroalanine''' ('''Cα,β-didehydroalanine''', '''α,β-di-dehydroalanine''', '''2-aminoacrylate''', or '''2,3-didehydroalanine''') is a ]. It does not exist in its free form, but it occurs naturally as a residue found in ]s of ] origin.<ref>{{cite journal |last1=Downs |first1=DM |last2=Ernst |first2=DC |title=From microbiology to cancer biology: the Rid protein family prevents cellular damage caused by endogenously generated reactive nitrogen species. |journal=Molecular Microbiology |date=April 2015 |volume=96 |issue=2 |pages=211–9 |doi=10.1111/mmi.12945 |pmid=25620221|pmc=4974816 }}</ref> As an amino acid residue, it is unusual because it has an ] backbone.<ref name=DS>{{cite journal |first= Dawid |last= Siodłak |title= α,β-Dehydroamino Acids in Naturally Occurring Peptides |journal= Amino Acids |year= 2015 |volume= 47 |issue= 1 |pages= 1–17 |doi= 10.1007/s00726-014-1846-4 |pmid= 25323736 |pmc= 4282715 }}</ref> |
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'''Dehydroalanine''' (or '''(alpha)-(beta)-di-dehydroalanine''') is an uncommon ] found in ]s of ] origin (an ] amino acid). |
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==Structure and reactivity== |
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Dehydroalanine (DHA) is also found in food proteins, including ], that have been heated and/or treated with an ''alkali'' such as ] (NaOH). These treatments can ] ] in the protein chain. In food, DHA frequently ] ] to yield the crosslinking aminoacid ] (LAL). Lysinoalanine, N6-(DL-2-amino-2-carboxyethyl)-L-lysine, an unusual amino acid implicated as a renal toxic factor in laboratory rats (kidney damage), has been found in proteins of home-cooked and commercial foods and ingredients. Although it had been reported to occur in both edible and non-food proteins only after alkali treatment (such as occurs in soybean processing), it has also been identified in food proteins that had not been subjected to alkali. Lysinoalanine can also be generated in a variety of proteins when heated under non-alkaline conditions. |
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Like most primary ]s, dehydroalanine is unstable. Dehydroalanine hydrolyzes to ]. |
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Many dehydroalanine-containing peptides are toxic or ] and constitute parts of ] or ]s. |
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''N''-Acylated derivatives of dehydroalanine, such as peptides and related compounds, are stable. For example, ] is the N-acetylated derivative of the ester. As a residue in a peptide, it is generated by a ]. The required precursors are ] or ] residues, which undergo enzyme-mediated loss of water and ], respectively. |
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==See also== |
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* ] |
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Most amino acid residues are unreactive toward ]s, but those containing dehydroalanine or some other dehydroamino acids are exceptions. These are ] due to the ],<ref name=DS/> and can, for example, ] other amino acids.<!-- see next section for example --> This activity has made DHA useful synthetically to prepare ]. |
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==References== |
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{{PubChem|123991}} |
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==Occurrence== |
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] |
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The dehydroalanine residue was first detected in ], a ] with antimicrobial activity.<ref name=DS/> Dehydroalanine is also present in some ] and ]s. |
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DHA can be formed from ] or ] by simple base catalysis without the need for an enzyme, which can happen during cooking and ] food preparation processes. It can then alkylate other amino acid residues, such as ], forming lysinoalanine ]s and ] of the original alanine. The resulting proteins have lower nutritional quality for some species but higher nutritional quality for others. Some lysinoalanines may also cause kidney enlargement in rats.<ref>{{cite book |title= Impact of Processing on Food Safety |year= 1999 |volume= 459 |pages= 145–159 |chapter= Lysinoalanine in food and in antimicrobial proteins |first= Mendel |last= Friedman |pmid= 10335374 |doi= 10.1007/978-1-4615-4853-9_10 |editor1-first= Lauren S. |editor1-last= Jackson |editor2-first= Mark G. |editor2-last= Knize |editor3-first= Jeffrey N. |editor3-last= Morgan |publisher= Springer |isbn= 978-1-4615-4853-9 |series= Advances in Experimental Medicine and Biology }}</ref> |
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Many dehydroalanine-containing peptides are toxic.<ref name=DS/> |
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] contains three dehydro amino acid residues, two of which are dehydroalanine residues.]] |
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A dehydroalanine residue was long thought to be an important electrophilic catalytic residue in ] and ] enzymes, but the active residue was later found instead to be a different unsaturated alanine derivative — ] — that is even more electrophilic.<ref>{{cite journal |journal= Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics |title= Discovery and role of methylidene imidazolone, a highly electrophilic prosthetic group |first=János |last= Rétey |year= 2003 |volume= 1647 |issue= 1–2 |pages= 179–184 |doi= 10.1016/S1570-9639(03)00091-8 |pmid= 12686130 }}</ref><ref>{{cite journal | vauthors = Calabrese JC, Jordan DB, Boodhoo A, Sariaslani S, Vannelli T | title = Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis | journal = Biochemistry | volume = 43 | issue = 36 | pages = 11403–16 | date = September 2004 | pmid = 15350127 | doi = 10.1021/bi049053+ }}</ref> |
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== Chemical synthesis == |
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N-Acyl dehydroalanine derivatives have been synthesized by dehydration of serines using a ] leaving group,<ref>{{Cite journal |last1=Ferreira |first1=Paula M. T. |last2=Maia |first2=Hernâni L. S. |last3=Monteiro |first3=Luís S. |last4=Sacramento |first4=Joana |date=1999 |title=High yielding synthesis of dehydroamino acid and dehydropeptide derivatives |url=http://xlink.rsc.org/?DOI=a904730a |journal=Journal of the Chemical Society, Perkin Transactions 1 |issue=24 |pages=3697–3703 |doi=10.1039/a904730a|hdl=1822/2188 |hdl-access=free }}</ref> or by conversion of ] derivatives using various reagents for the elimination of the ]-group.<ref>{{Cite journal |last1=Chalker |first1=Justin M. |last2=Gunnoo |first2=Smita B. |last3=Boutureira |first3=Omar |last4=Gerstberger |first4=Stefanie C. |last5=Fernández-González |first5=Marta |last6=Bernardes |first6=Gonçalo J. L. |last7=Griffin |first7=Laura |last8=Hailu |first8=Hanna |last9=Schofield |first9=Christopher J. |last10=Davis |first10=Benjamin G. |date=2011 |title=Methods for converting cysteine to dehydroalanine on peptides and proteins |url=http://xlink.rsc.org/?DOI=c1sc00185j |journal=Chemical Science |language=en |volume=2 |issue=9 |pages=1666 |doi=10.1039/c1sc00185j |issn=2041-6520}}</ref> |
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Newest methods allow the gram-scale synthesis of various protected dehydroamino acids by ] oxidation of the respective amino acid derivative in methanol, followed by acid-catalyzed elimination of methanol.<ref>{{Cite journal |last1=Gausmann |first1=Marcel |last2=Kreidt |first2=Nadine |last3=Christmann |first3=Mathias |date=2023-04-07 |title=Electrosynthesis of Protected Dehydroamino Acids |url=https://pubs.acs.org/doi/10.1021/acs.orglett.3c00403 |journal=Organic Letters |language=en |volume=25 |issue=13 |pages=2228–2232 |doi=10.1021/acs.orglett.3c00403 |pmid=36952622 |s2cid=257716096 |issn=1523-7060}}</ref> |
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==References== |
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<references /> |
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] |
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