Sebastian J F, Lo W Y
Can J Biochem. 1978 May;56(5):329-33. doi: 10.1139/o78-051.
3,3-Diphenylpropanoate (DPP) activates the carboxypeptidase A catalyzed hydrolysis of benzoylglycyl-L-phenylalanine (BzGly-L-Phe) (Ka = 2.1 x 10 (-3) M) and inhibits ester hydrolysis uncompetitively (K1 =2.1 X 10 (-3) M). A common modifier binding site located adjacent to the peptide and ester substrate binding sites is proposed. The forms of the pathways proposed for activation and inhibition are remarkably similar.
3,3-二苯基丙酸酯(DPP)可激活羧肽酶A催化的苯甲酰甘氨酰-L-苯丙氨酸(BzGly-L-Phe)的水解反应(Ka = 2.1×10⁻³ M),并以非竞争性方式抑制酯水解反应(K1 = 2.1×10⁻³ M)。研究提出,在肽和酯底物结合位点附近存在一个共同的修饰剂结合位点。所提出的激活和抑制途径形式非常相似。