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Controlling Substrate Preference and Transglycosylation Activity of Neopullulanase by Manipulating Steric Constraint and Hydrophobicity in Active Center*
The substrate specificity and the transglycosylation activity of neopullulanase was altered by site-directed mutagenesis on the basis of information from a three-dimensional structure predicted byExpand
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Importin alpha subtypes determine differential transcription factor localization in embryonic stem cells maintenance.
We recently demonstrated that the expression of the importin α subtype is switched from α2 to α1 during neural differentiation in mouse embryonic stem cells (ESCs) and that this switching has a majorExpand
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Introduction of Raw Starch-Binding Domains intoBacillus subtilis α-Amylase by Fusion with the Starch-Binding Domain of Bacillus Cyclomaltodextrin Glucanotransferase
ABSTRACT We constructed two types of chimeric enzymes, Ch1 Amy and Ch2 Amy. Ch1 Amy consisted of a catalytic domain of Bacillus subtilis X-23 α-amylase (Ba-S) and the raw starch-binding domainExpand
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Characteristics of Two Forms of α-Amylases and Structural Implication
ABSTRACT Complete (Ba-L) and truncated (Ba-S) forms of α-amylases fromBacillus subtilis X-23 were purified, and the amino- and carboxyl-terminal amino acid sequences of Ba-L and Ba-S were determined.Expand
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Characteristics of two forms of alpha-amylases and structural implication.
Complete (Ba-L) and truncated (Ba-S) forms of alpha-amylases from Bacillus subtilis X-23 were purified, and the amino- and carboxyl-terminal amino acid sequences of Ba-L and Ba-S were determined. TheExpand
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Calcium‐binding analysis and molecular modeling reveal echis coagulation factor IX/factor X‐binding protein has the Ca‐binding properties and Ca ion‐independent folding of other C‐type lectin‐like
Many biologically active heterodimeric proteins of snake venom consist of two C‐type lectin‐like subunits. One of these proteins, habu IX/X‐bp, is a Gla domain‐binding protein whose subunits bothExpand
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X-ray structures of Aerococcus viridans lactate oxidase and its complex with D-lactate at pH 4.5 show an alpha-hydroxyacid oxidation mechanism.
L-Lactate oxidase (LOX) belongs to a family of flavin mononucleotide (FMN)-dependent alpha-hydroxy acid-oxidizing enzymes. Previously, the crystal structure of LOX (pH 8.0) from Aerococcus viridansExpand
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Function of second glucan binding site including tyrosines 54 and 101 in Thermus aquaticus amylomaltase.
Amylomaltase from Thermus aquaticus catalyzes three types of transglycosylation reaction, as well as a weak hydrolytic reaction of alpha-1,4 glucan. From our previous study [Fujii et al., Appl.Expand
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Use of Random and Saturation Mutageneses To Improve the Properties of Thermus aquaticus Amylomaltase for Efficient Production of Cycloamyloses
ABSTRACT Amylomaltase from Thermus aquaticus catalyzes intramolecular transglycosylation of α-1,4 glucans to produce cyclic α-1,4 glucans (cycloamyloses) with degrees of polymerization of 22 andExpand
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