Aisaka K, Masuda T, Chikamune T, Kamitori K
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Japan.
Biosci Biotechnol Biochem. 1998 Apr;62(4):782-7. doi: 10.1271/bbb.62.782.
Trehalose phosphorylase was purified from the cell extracts of Catellatospora ferruginea. The enzyme had an apparent molecular weight of 400,000 by gel filtration and 98,000 by SDS-PAGE, suggesting that the enzyme was a tetramer. The enzyme was specific for trehalose in phosphorolysis and specific for beta-D-glucose 1-phosphate in synthesis. In addition to D-glucose, D-xylose and D-fucose were also possible sugar acceptors during synthesis. Phosphate ions were a key to the activity and stability of the enzyme, controlling the equilibrium of the reversible reaction and the heat stability of the enzyme. The enzyme was strongly inhibited by p-chloromercuribenzoate and pyridoxal phosphate. The enzyme was inactivated by heat or by storage frozen with ammonium chloride and lithium chloride.
海藻糖磷酸化酶是从铁锈色卡特拉链霉菌的细胞提取物中纯化得到的。通过凝胶过滤法测得该酶的表观分子量为400,000，通过SDS-PAGE测得为98,000，这表明该酶是一种四聚体。该酶在磷酸解反应中对海藻糖具有特异性，在合成反应中对β-D-葡萄糖1-磷酸具有特异性。在合成过程中，除了D-葡萄糖外，D-木糖和D-岩藻糖也可能是糖受体。磷酸根离子是该酶活性和稳定性的关键，它控制着可逆反应的平衡以及酶的热稳定性。该酶受到对氯汞苯甲酸和磷酸吡哆醛的强烈抑制。该酶会因加热或与氯化铵和氯化锂一起冷冻保存而失活。
