Palladium--a new inhibitor of cellulase activities.
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.
Shultz
M D
MD
Chemical Technology Division, Oak Ridge National Laboratory, Tennessee 37831-6194, USA.
Lassig
J P
JP
Gooch
M G
MG
Evans
B R
BR
Woodward
J
J
D001665:Binding Sites; D002480:Cellulase / Q000037:antagonists & inhibitors* / Q000302:isolation & purification; D043366:Cellulose 1,4-beta-Cellobiosidase; D002851:Chromatography, High Pressure Liquid; D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D007700:Kinetics; D010165:Palladium / Q000494:pharmacology*; D014242:Trichoderma / Q000201:enzymology*; D001617:beta-Glucosidase / Q000037:antagonists & inhibitors
D010165:Palladium; D006026:Glycoside Hydrolases; C056373:endoglucanase 2; D001617:beta-Glucosidase; D002480:Cellulase; D043366:Cellulose 1,4-beta-Cellobiosidase