Gerstner E, Kiel U
Hoppe Seylers Z Physiol Chem. 1975 Dec;356(12):1853-7.
Mandelonitrile lyase has been isolated from the seeds of Prunus laurocerasus and characterized. The enzyme is a glycoprotein and contains FAD as prosthetic group. It has an absorption spectrum of the hydrophobic type. The molecular weight is 60000. The new mandelonitrile lyase catalyses both formation and cleavage of D-(+)-benzaldehyde cyanohydrin. Despite the existence of marked morphologic and biochemical differences between P. laurocerasus and P. amygdalus (var. sativa) (sweet almond) the enzymes isolated from the seeds of the two Prunoideae species are closely related, as judged from their immunological properties. However they exhibit specific differences in the isoelectric points and quantitative distribution of the three isoenzymes.
扁桃腈裂解酶已从月桂樱桃种子中分离出来并进行了特性鉴定。该酶是一种糖蛋白，含有黄素腺嘌呤二核苷酸（FAD）作为辅基。它具有疏水型吸收光谱。分子量为60000。新的扁桃腈裂解酶催化D-(+)-苯甲醛氰醇的形成和裂解。尽管月桂樱桃和扁桃（栽培变种）（甜杏仁）在形态学和生物化学上存在明显差异，但从这两种李亚科植物种子中分离出的酶在免疫学性质上密切相关。然而，它们在三种同工酶的等电点和定量分布上表现出特定差异。
