Ontology highlight
ABSTRACT:
SUBMITTER: Wan Q
PROVIDER: S-EPMC3606583 | biostudies-literature | 2013 Mar
REPOSITORIES: biostudies-literature
Acta crystallographica. Section F, Structural biology and crystallization communications 20130227 Pt 3
Xylanase II from Trichoderma reesei catalyzes the hydrolysis of glycosidic bonds in xylan. Crystallographic studies of this commercially important enzyme have been initiated to investigate its reaction mechanism, substrate binding and dependence on basic pH conditions. The wild-type protein was heterologously expressed in an Escherichia coli host using the defined medium and four active-site amino acids were replaced to abolish its activity (E177Q and E86Q) or to change its pH optimum (N44D and ...[more]