Shultz M D, Lassig J P, Gooch M G, Evans B R, Woodward J
Chemical Technology Division, Oak Ridge National Laboratory, Tennessee 37831-6194, USA.
Biochem Biophys Res Commun. 1995 Apr 26;209(3):1046-52. doi: 10.1006/bbrc.1995.1603.
Palladium complexes have been shown to strongly inhibit cellobiohydrolase I (CBH I) and endoglucanase II (EG II), two cellulases produced by Trichoderma reesei. Also inhibited were total cellulase (Avicelase) and beta-glucosidase (cellobiase) activities. The catalytic domain of CBH II, the second most abundant component of this cellulase, appeared less susceptible to inhibition by palladium. The inhibition was irreversible and could be prevented if histidine, cysteine or cystine was added to the enzyme reaction mixture simultaneously with the inhibitor. The binding of CBH I to microcrystalline cellulose (Avicel) was unaffected by palladium.
钯配合物已被证明能强烈抑制里氏木霉产生的两种纤维素酶,即纤维二糖水解酶I(CBH I)和内切葡聚糖酶II(EG II)。总纤维素酶(微晶纤维素酶)和β-葡萄糖苷酶(纤维二糖酶)的活性也受到抑制。CBH II的催化结构域是这种纤维素酶中第二丰富的成分,似乎对钯的抑制作用不太敏感。这种抑制是不可逆的,如果在酶反应混合物中同时加入组氨酸、半胱氨酸或胱氨酸,则可以防止这种抑制。CBH I与微晶纤维素(微晶纤维素)的结合不受钯的影响。