Synthetic substrates of vertebrate collagenase.
The active site specificity of vertebrate collagenase was mapped with the synthesis of a variety of peptides, peptolides, and peptide esters. The enzyme was found to prefer very lipophilic sequences, and it was also found to be an esterase. The thio peptolide Ac-Pro-Leu-Gly-SCH[CH2CH(CH3)2]CO-Leu-Gly-OC2H5 was found to be an exceptional substrate. High-performance liquid chromatography and tandem mass spectrometry were used to unambiguously establish the cleavage site in several peptide substrates.
D000818:Animals; D001001:Anura; D001172:Arthritis, Rheumatoid / Q000201:enzymology; D001842:Bone and Bones / Q000201:enzymology; D005347:Fibroblasts / Q000201:enzymology; D006801:Humans; D007202:Indicators and Reagents; D051379:Mice; D003012:Microbial Collagenase / Q000378:metabolism*; D009842:Oligopeptides / Q000138:chemical synthesis*; D009924:Organ Culture Techniques; D012867:Skin / Q000201:enzymology; D013379:Substrate Specificity
D007202:Indicators and Reagents; D009842:Oligopeptides; D003012:Microbial Collagenase