Synthesising protease-stable isopeptides by proteases: an efficient biocatalytic approach on the basis of a new type of substrate mimetics.
A biocatalytic route to the 'post-synthesis' formation of Asp/Glu-derived isopeptides is illustrated on the basis of the Staphylococcus aureus V8 protease used as the biocatalyst, a new type of substrate mimetics as the donor peptides, and several acceptor peptides varying in length and sequence.
Wehofsky
N
N
Max-Planck Society, Research Unit Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Salle, Germany.
Alisch
M
M
Bordusa
F
F
D000595:Amino Acid Sequence; D001224:Aspartic Acid / Q000378:metabolism; D002384:Catalysis; D005973:Glutamine / Q000378:metabolism; D018716:Molecular Mimicry; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D012697:Serine Endopeptidases / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000201:enzymology*; D013379:Substrate Specificity
D010455:Peptides; D005973:Glutamine; D001224:Aspartic Acid; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase