Abstract
α, β-Unsaturated amino acids are potential precursors for the formation of crosslinkages in peptides and proteins. DEHYDROALANINE and DEHYDROBUTYRINE are constituents of NISIN (from Streptococcus lactis) and SUBTILIN (from Bacillus subtilis). Both peptides are crosslinked via sulfide bridges of no fewer than one residue of lanthionine and four residues of β-methyllanthionine presumably formed by the addition of the sulfhydryl group of cysteine residues across the double bond of dehydroalanine and dehydrobutyrine, respectively. CINNAMYCIN (from Streptomyces cinnamoneus) and DURAMYCIN (from Streptomyces cinnamoneus forma azacoluta) also display the crosslinking features of lanthionine and β-methyllanthionine. The reactive double bond of α, β-unsaturated amino acids is no longer seen in these two peptides. The presence of LYSINOALANINE in cinnamycin and duramycin establishes the imino bridge as a novel type of naturally occurring cross-linkage. The formation of the imino bridge is attributed to the addition of the ε-amino group of a lysine residue across the α, βunsaturation of dehydroalanine, a reaction that takes place in nisin, nisin fragments, and subtilin under controlled alkaline conditions. The crypticity of α, β-unsaturated amino acids constitutes a continued impediment to their easy analytical detection. A more broadly based role for α, β-unsaturated amino acids in the physiological environment must not be ruled out at the present time.
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Gross, E. (1977). α, β-Unsaturated and Related Amino Acids in Peptides and Proteins. In: Friedman, M. (eds) Protein Crosslinking. Advances in Experimental Medicine and Biology, vol 86. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9113-6_9
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DOI: https://doi.org/10.1007/978-1-4757-9113-6_9
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