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- W2007350561 abstract "Starch branching enzyme (SBE) catalyzes the cleavage of alpha-1.4-linkages and the subsequent transfer of alpha-1.4 glucan to form an alpha-1.6 branch point in amylopectin. We overproduced rice branching enzyme I (BEI) in Escherichia coli cells, and the resulting enzyme (rBEI) was characterized with respect to biochemical and crystallographic properties. Specific activities were calculated to be 20.8 units/mg and 2.5 units/mg respectively when amylose and amylopectin were used as substrates. Site-directed mutations of Tyr235, Asp270, His275, Arg342, Asp344, Glu399, and His467 conserved in the alpha-amylase family enzymes drastically reduced catalytic activity of rBEI. This result suggests that the structures of BEI and the other alpha-amylase family enzymes are similar and that they share common catalytic mechanisms. Crystals of rBEI were grown under appropriate conditions and the crystals diffracted to a resolution of 3.0 A on a synchrotron X-ray source." @default.
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- W2007350561 date "2008-11-23" @default.
- W2007350561 modified "2023-10-01" @default.
- W2007350561 title "Biochemical and Crystallographic Characterization of the Starch Branching Enzyme I (BEI) from<i>Oryza sativa</i>L" @default.
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- W2007350561 doi "https://doi.org/10.1271/bbb.80325" @default.
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