Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1764, Issue 10, Pages 1633-1638Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2006.08.013
Keywords
4-alpha-glucanotransferase (4-alpha-GTase); site-directed mutagenesis; transglycosylation activity; hydrolysis activity; hydrophobicity
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A W229H mutant of 4-alpha-glucanotransferase (4-alpha-GTase) from Pyrococcus furiosus was constructed and its catalytic properties were studied to investigate the role of W229 in the catalytic specificities of the enzyme. Various activities and kinetic parameters were determined for the wildtype and W229H mutant enzymes. The transglycosylation factor and transglycosylation activity of the mutant enzyme markedly decreased, but its hydrolysis activity was scarcely affected. It was discovered that the k(cat)/K-m value of transglycosylation activity significantly decreased to about 15% of that of the wild type, while k(cat)/k(m) value of hydrolysis activity changed little for the mutant enzyme. The hydrophobicity of W229 was thought to be critical to the transglycosylation activity of the enzyme based on the enzyme's modeled tertiary structures. (c) 2006 Elsevier B.V. All rights reserved.
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