Raso V, Stollar B D
Biochemistry. 1975 Feb 11;14(3):591-9. doi: 10.1021/bi00674a020.
Reduced Schiff base compounds of pyridoxal-P and tyrosine, which were used to induce specific antibodies described in the preceding article (V. Raso and B. D. Stolar, Biochemistry, 1975), caused active site-directed inhibition of tyrosine transaminase and tyrosine decarboxylase. The antibodies, studied as analogs of enzymes, were able to bind an unsaturated Schiff base catalytic intermediate, as shown by equilibrium dialysis and absorbance difference spectroscopy. Schiff base formation can proceed while the pyridoxal-P and tyrosine are within the antibody combining site, but the rate of this bimolecular condensation within the sites was not greater than the rate in free solution. Antibody did effect a small rate enhancement for the pyridoxal-P-catalyzed transamination of L-tyrosine. These results are discussed in light of current ideas in the mechanisms of enzyme catalysis.
吡哆醛 - 磷酸(pyridoxal-P)与酪氨酸的还原席夫碱化合物,用于诱导前文(V. 拉索和B. D. 斯托拉尔,《生物化学》,1975年)所述的特异性抗体,可引起酪氨酸转氨酶和酪氨酸脱羧酶的活性位点定向抑制。作为酶类似物进行研究的抗体,能够结合不饱和席夫碱催化中间体,这通过平衡透析和吸光度差光谱法得以证明。当吡哆醛 - 磷酸和酪氨酸处于抗体结合位点内时,席夫碱形成可以进行,但位点内这种双分子缩合的速率不大于自由溶液中的速率。抗体确实对吡哆醛 - 磷酸催化的L - 酪氨酸转氨作用有小幅的速率增强。根据当前关于酶催化机制的观点对这些结果进行了讨论。