Substrate mimetics-specific peptide ligases: studies on the synthetic utility of a zymogen and zymogen-like enzymes.
Although proteases are capable of synthesizing peptide bonds, they are not proficient at peptide fragment ligation. Further manipulations are needed to shift the native enzyme activity from the cleavage to the synthesis of peptides. This account reports on the synthetic potential of nonactivatable trypsinogen and zymogen-like enzymes designed to minimize proteolytic side reactions during peptide synthesis.
Rall
Kathrin
K
Research Unit Enzymology of Protein Folding, Max-Planck-Society, Weinbergweg 22, D-06120 Halle/Saale, Germany.
Bordusa
Frank
F
D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D002384:Catalysis; D004792:Enzyme Precursors / Q000737:chemistry* / Q000378:metabolism; D006868:Hydrolysis; D008025:Ligases / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D018716:Molecular Mimicry; D015394:Molecular Structure; D010455:Peptides / Q000032:analysis / Q000138:chemical synthesis* / Q000737:chemistry; D015202:Protein Engineering; D013379:Substrate Specificity; D014362:Trypsinogen / Q000737:chemistry / Q000378:metabolism
D000596:Amino Acids; D004792:Enzyme Precursors; D010455:Peptides; D014362:Trypsinogen; D008025:Ligases