Shibatani T, Kakimoto T, Chibata I
Int J Vitam Nutr Res. 1975;45(2):144-52.
Pyridoxal phosphate N-oxide and 2'-hydroxypyridoxal phosphate served as the coenzyme for aspartate beta-decarboxylase (EC 4.1.1.12) from Pseudomonas dacunhae. Reconstituted enzymes with those pyridoxal phosphate analogues exhibited an absorption band near 370 nm. Close to 1 mole of vitamin B6 derivative is bound per minimal catalytic unit with high affinity. The decarboxylase, desulfinase, and transaminase activites of the both pyridoxal phosphate derivate-enzymes are relatively low. But the Km values for aspartate and cysteine sulfinate are not affected.
磷酸吡哆醛N-氧化物和2'-羟基磷酸吡哆醛作为来自达库尼亚假单胞菌的天冬氨酸β-脱羧酶（EC 4.1.1.12）的辅酶。用那些磷酸吡哆醛类似物重构的酶在370nm附近呈现一个吸收带。每个最小催化单位以高亲和力结合近1摩尔的维生素B6衍生物。两种磷酸吡哆醛衍生物 - 酶的脱羧酶、脱亚硫酸酶和转氨酶活性相对较低。但是天冬氨酸和半胱氨酸亚磺酸盐的Km值不受影响。
