Bianchetti CM Takasuka TE Deutsch S Udell HS Yik EJ Bergeman LF Fox BG Active Site and Laminarin Binding in Glycoside Hydrolase Family 55 Journal of Biological Chemistry 2015 290 1911819 ID: 912633
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Active site and laminarin hydrolysis in glycoside hydrolase family 55 (GH55)
Bianchetti
CM,
Takasuka TE, Deutsch S, Udell HS, Yik EJ, Bergeman LF, Fox BG. “Active Site and Laminarin Binding in Glycoside Hydrolase Family 55”. Journal of Biological Chemistry (2015). 290 (19):11819.
Objective Determine the structure, mechanism and breadth of natural reactivity in the GH55 enzyme family
Approach Collaboration of GLBRC and JGI; X-ray diffraction data collected at DOE Argonne National LaboratoryHigh resolution crystal structures with substrates bound and ensemble refinement suggest a simple new mechanism for promoting processive reactivityActive site architecture defines an exo-glucanase mechanism and gives high tolerance for branching found in natural b-1,3-glucans such as kelp laminarin
Result/ImpactsGene synthesis and automated protein translation assigned function to 20% of the GH55 family; this is a new way to annotate bioenergy phylogenetic spaceBroad range of properties including optima for pH, temperature and rates identified in natural enzymesBest enzymes are highly efficient in hydrolyzing laminarin (found in kelp, a potential bioenergy crop) into simple sugars
BRC Science Highlight
GLBRC
April 2015