Peptide thioester substrates for serine peptidases and metalloendopeptidases.
Peptide thioesters are sensitive substrates of various serine peptidases and metalloendopeptidases. Thioester substrates generally have high enzymatic hydrolysis rates and low background hydrolysis rates, and the hydrolysis rates can be easily monitored in the presence of thiol reagents such as 4,4'-dithiodipyridine or 5,5'-dithiobis (2-nitrobenzoic acid). Peptide thioester substrates have been invaluable for the study of enzyme specificity and enzyme inhibitors, especially in cases where no other practical synthetic substrates are available. Tripeptide substrates of the type Boc-Ala-Ala-AA-SBzl, where AA is nearly all of the 20 common amino acids, have now been synthesized and should be useful for the subsite mapping of new serine peptidases and the study of crude cell preparations containing serine peptidases.
Powers
J C
JC
School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta 30332, USA.
Kam
C M
CM
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D007700:Kinetics; D008666:Metalloendopeptidases / Q000378:metabolism*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism; D012697:Serine Endopeptidases / Q000378:metabolism*; D013379:Substrate Specificity; D013438:Sulfhydryl Compounds / Q000378:metabolism
D009842:Oligopeptides; D013438:Sulfhydryl Compounds; D012697:Serine Endopeptidases; D008666:Metalloendopeptidases