Circular dichroism studies in conformation of cellobiohydrolase and endoglucanase from Trichoderma pseudokiningii S-38: effects of pH and ligand binding.
Effects of pH and ligand binding upon the conformation of cellobiohydrolase I (CBHI) and endoglucanase I (EGI) from Trichoderma pseudokiningii S-38 have been studied by circular dichroism measurements. In the high-pH range (6-9), increasing pH resulted in a similar conformational change occurring in free CBHI and EGI, while such treatment gave different changes of the two enzyme conformations in the presence of cellobiose. On the other hand, in the low-pH region, with both CBHI an EGI in the active form, decreasing pH resulted in a large conformational change of free EGI compared to that of free CBHI, whereas ligand binding resulted in a similar change of both CBHI and EGI, independent of pH change.
Yan
B
B
National Laboratory of Microbial Technology, Shandong University, Jinan, China.
Sun
Y Q
YQ
D002475:Cellobiose / Q000378:metabolism; D002480:Cellulase / Q000737:chemistry*; D043366:Cellulose 1,4-beta-Cellobiosidase; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D011487:Protein Conformation; D014242:Trichoderma / Q000201:enzymology*
D008024:Ligands; D002475:Cellobiose; D002480:Cellulase; D043366:Cellulose 1,4-beta-Cellobiosidase