Effect of Single Active-Site Cleft Mutation on Product Specificity in a Thermostable Bacterial Cellulase View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2002

AUTHORS

Tauna R. Rignall , John O. Baker , Suzanne L. McCarter , William S. Adney , Todd B. Vinzant , Stephen R. Decker , Michael E. Himmel

ABSTRACT

Mutation of a single active-site cleft tyrosyl residue to a glycyl residue significantly changes the mixture of products released from phosphoric acid-swollen cellulose (PSC) by EIcd, the catalytic domain of the endoglucanase-I from Acidothermus cellulolyticus. The percentage of glucose in the product stream is almost 40% greater for the Y245G mutant (and for an additional double mutant, Y245G/Q204A) than for the wild type enzyme. Comparisons of results for digestion PSC and of pretreated yellow poplar suggest that the observed shifts in product specificity are connected to the hydrolysis of a more easily digestible fraction of both substrates. A model is presented that relates the changes in product specificity to a mutation-driven shift in indexing of the polymeric substrate along the extended binding-site cleft. More... »

PAGES

383-394

Book

TITLE

Biotechnology for Fuels and Chemicals

ISBN

978-1-4612-6621-1
978-1-4612-0119-9

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4612-0119-9_32

DOI

http://dx.doi.org/10.1007/978-1-4612-0119-9_32

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1019719086


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