Dynamics of loops surrounding the active site architecture in GH5_2 subfamily TfCel5A for cellulose degradation.

ABSTRACT:

Background

Lignocellulose is the most abundant natural biomass resource for the production of biofuels and other chemicals. The efficient degradation of cellulose by cellulases is a critical step for the lignocellulose bioconversion. Understanding the structure-catalysis relationship is vital for rational design of more stable and highly active enzymes. Glycoside hydrolase (GH) family 5 is the largest and most functionally diverse group of cellulases, with a conserved TIM barrel structure. The important roles of the various loop regions of GH5 enzymes in catalysis, however, remain poorly understood.

Results

In the present study, we investigated the relationship between the loops surrounding active site architecture and its catalytic efficiency, taking TfCel5A, an enzyme from

SUBMITTER: Wu X 

PROVIDER: S-EPMC10583438 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature