Endo Y
Biochim Biophys Acta. 1978 Mar 14;523(1):207-14. doi: 10.1016/0005-2744(78)90023-2.
An enzyme deacylating preferentially N-acyl-L-aromatic amino acids was partially purified from rat kidney. The purification procedure included DEAE-cellulose column chromatography, (NH4)2SO4 fractionation, gel-filtration on a Sephadex G-200 column and further DEAE-cellulose chromatography. The enzyme was thus separated from aminoacylase (N-acylamino-acid amidohydrolase, EC 3.5.1.14) (acylase I). Although the enzyme preparation contained other acylases, the experimental data (effect of p-chloromercuric benzoate, heat stability and inhibition between substrates) suggest that the enzyme acts preferentially on N-acyl derivatives of L-tryptophan, L-tyrosine, L-phenylalanine and L-histidine. This enzyme appears to be present in many animal tissues.
一种优先使N-酰基-L-芳香族氨基酸脱酰基的酶从大鼠肾脏中得到部分纯化。纯化步骤包括DEAE-纤维素柱层析、硫酸铵分级分离、在Sephadex G-200柱上进行凝胶过滤以及进一步的DEAE-纤维素层析。该酶因此与氨基酰化酶（N-酰基氨基酸酰胺水解酶，EC 3.5.1.14）（酰化酶I）分离。尽管酶制剂中含有其他酰化酶，但实验数据（对氯汞苯甲酸的作用、热稳定性和底物间的抑制作用）表明该酶优先作用于L-色氨酸、L-酪氨酸、L-苯丙氨酸和L-组氨酸的N-酰基衍生物。这种酶似乎存在于许多动物组织中。
