2007
DOI: 10.1016/j.ibmb.2007.05.002
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Involvement of tyrosine residues, N-terminal amino acids, and β-alanine in insect cuticular sclerotization

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Cited by 25 publications
(22 citation statements)
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“…Mild acid hydrolysis of cuticles from various insect species have yielded adducts containing amino acid residues linked to the a-position of 3,4-dihydroxyacetophenone (Andersen and Roepstorff, 2007;Andersen, 2007). The amino acids include lysine, linked via its 3-amino group (XXVI), glycine and b-alanine, linked via their amino groups (XXVII and XXVIII), and tyrosine, linked via its phenolic group (XXIX).…”
Section: Adduct Formation During In Vivo Sclerotizationmentioning
confidence: 99%
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“…Mild acid hydrolysis of cuticles from various insect species have yielded adducts containing amino acid residues linked to the a-position of 3,4-dihydroxyacetophenone (Andersen and Roepstorff, 2007;Andersen, 2007). The amino acids include lysine, linked via its 3-amino group (XXVI), glycine and b-alanine, linked via their amino groups (XXVII and XXVIII), and tyrosine, linked via its phenolic group (XXIX).…”
Section: Adduct Formation During In Vivo Sclerotizationmentioning
confidence: 99%
“…As the adducts contain an amino acid linked to the a-position and a keto-group in the b-position, it was suggested that they were produced by hydrolytic degradation of NADA-derived cuticular crosslinks having both sidechain positions involved in linkage to proteins. A possible way for producing the degradation products from such crosslinks has been suggested (Andersen and Roepstorff, 2007;Andersen, 2007).…”
Section: Adduct Formation During In Vivo Sclerotizationmentioning
confidence: 99%
“…The 3,4-dihydroxyacetophenone adducts which contain an amino acid residue linked to the a-position were suggested to be degradation products of the crosslinks formed when oxidized dehydro-NADA reacted with cuticular proteins (Andersen and Roepstorff, 2007;Andersen, 2007).…”
Section: Discussionmentioning
confidence: 99%
“…Both types of quinones may react with nucleophilic groups (such as histidine) present in the cuticular proteins to give ring-substituted adducts (7) and sidechain-substituted adducts (8), respectively. The NADA p-quinone methide (3) can also be rearranged to dehydro-NADA (4), which after oxidation to quinones (5 and 6) may react with available catechols to give dihydroxyphenyl-dihydrobenzodioxine derivatives (9) or with two nucleophilic groups (HX and HY), which are thereby crosslinked (10) (Modified from Andersen, 2007).…”
Section: Methodsmentioning
confidence: 99%
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