The serine proteinases and their inhibitors play important roles in regulating many biological cellular events [1]. There are numerous natural protein inhibitors including some with low molecular weights [2]. The N-phosphoamino acids, contianing hte tetrahedral phosphoryl group that resembles the unstable transition state involved in the catalytic reaction of serine proteinase, and the amino acid side chains that may act as natural substrates to serine proteinase, probably inhibit proteinase by the transition-state-analog mechanism proposed by Robertu [3]. The reuslt presented in this paper indicates that N-(O,O-dialkyl) phospho amino acid (DAPaas) are novel trypsin inhibitors.
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