Bertini I, Luchinat C, Scozzafava A
Bioinorg Chem. 1977;7(3):225-31. doi: 10.1016/s0006-3061(00)80096-4.
The results of a study on the interaction between cobalt(II) bovine carbonic anhydrase and the alpha-amino acids L(+) and D(-)alanine, glycine and betaine are reported. L(+)alanine and glycine have been found to have larger affinity for the enzyme than D(-)alanine whereas no sizable affinity is shown by betaine. The electronic spectra indicate that these systems are similar to that containing the acetate ion. Utilizing the inhibition properties of L(+)alanine at various pH an analysis of the species involved in the inhibition reaction is presented.
报道了一项关于钴(II)牛碳酸酐酶与α-氨基酸L(+)和D(-)丙氨酸、甘氨酸和甜菜碱之间相互作用的研究结果。已发现L(+)丙氨酸和甘氨酸对该酶的亲和力比D(-)丙氨酸大,而甜菜碱未表现出可观的亲和力。电子光谱表明这些体系与含有醋酸根离子的体系相似。利用L(+)丙氨酸在不同pH下的抑制特性,对抑制反应中涉及的物种进行了分析。