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A series of amino acid and peptide thioesters have been synthesized as sensitive assay substrates for the serine proteases involved in blood coagulation. Each substrate had a P1 Arg residue. The thiol leaving group (P1') and the P2 amino acid residues were varied. The thioesters have much higher Kcat/KM values than the corresponding amides such as 4-nitroanilides and 7-amino-4-methylcou- marin amides. In addition, the thiol released upon enzymatic hydrolysis of the substrates, can be measured chromogenically by use of a thiol reagent such as 4,4'- dithiodipyridine contained in the assay mixture. Thioesters are among the most sensitive assay substrates for coagulation serine proteases due to the combination of a high turnover rate with the ease of detection of the hydrolysis product. In addition they can be utilized with enzymes such as factor IXa for which no other suitable synthetic substrate is currently available.

Amino Acid And Peptide Thioeters: New Sensitive Substrates For Bovine Factors IXa , Xa , XIa , XIIa , Thrombin, Plasma Kallikrein And Trypsin