Matching Sentences: [ Sen. 2, subscore: 2.00 ]: Characteristics of two rice alpha-amylases Amy1A and Amy3D , and those of two chimeric enzymes Amy1A/3D and Amy3D/1A , engineered from the two isozymes , were compared in the light of the functional roles of protein domains in alpha-amylase . The enzymes that have an Amy1A-type N-terminal domain , Amy1A and Amy1A/3D , showed high activity against soluble starch , while the enzymes that have an Amy3D-type barrel structure , Amy3D and Amy1A/3D , showed high activity in oligosaccharide hydrolysis . Rigidity of protein folding also significantly affected the enzyme activity in both soluble starch and oligosaccharide hydrolysis . Thus , the present work suggests that the structure of the N-terminal domain is important for stability and soluble starch hydrolysis , while the barrel structure that forms the active site significantly affects enzyme activities in oligosaccharide degradation . We have already characterized two rice alpha-amylase isozymes , Amy1A and Amy3D , and a chimeric enzyme engineered from these two isozymes , Amy1A/3D ( Terashima et al 1995 , 1996a , b ) . In spite of the high homology ( 70% ) of their amino acid sequences , Amy1A and Amy3D showed distinct differences in their enzymatic characteristics . [ Sen. 1, subscore: 1.00 ]: Characteristics of two rice alpha-amylases Amy1A and Amy3D , and those of two chimeric enzymes Amy1A/3D and Amy3D/1A , engineered from the two isozymes , were compared in the light of the functional roles of protein domains in alpha-amylase . The enzymes that have an Amy1A-type N-terminal domain , Amy1A and Amy1A/3D , showed high activity against soluble starch , while the enzymes that have an Amy3D-type barrel structure , Amy3D and Amy1A/3D , showed high activity in oligosaccharide hydrolysis . Rigidity of protein folding also significantly affected the enzyme activity in both soluble starch and oligosaccharide hydrolysis . Thus , the present work suggests that the structure of the N-terminal domain is important for stability and soluble starch hydrolysis , while the barrel structure that forms the active site significantly affects enzyme activities in oligosaccharide degradation . We have already characterized two rice alpha-amylase isozymes , Amy1A and Amy3D , and a chimeric enzyme engineered from these two isozymes , Amy1A/3D ( Terashima et al 1995 , 1996a , b ) . [ Sen. 5, subscore: 1.00 ]: Characteristics of two rice alpha-amylases Amy1A and Amy3D , and those of two chimeric enzymes Amy1A/3D and Amy3D/1A , engineered from the two isozymes , were compared in the light of the functional roles of protein domains in alpha-amylase . The enzymes that have an Amy1A-type N-terminal domain , Amy1A and Amy1A/3D , showed high activity against soluble starch , while the enzymes that have an Amy3D-type barrel structure , Amy3D and Amy1A/3D , showed high activity in oligosaccharide hydrolysis . Rigidity of protein folding also significantly affected the enzyme activity in both soluble starch and oligosaccharide hydrolysis . Thus , the present work suggests that the structure of the N-terminal domain is important for stability and soluble starch hydrolysis , while the barrel structure that forms the active site significantly affects enzyme activities in oligosaccharide degradation . We have already characterized two rice alpha-amylase isozymes , Amy1A and Amy3D , and a chimeric enzyme engineered from these two isozymes , Amy1A/3D ( Terashima et al 1995 , 1996a , b ) . In spite of the high homology ( 70% ) of their amino acid sequences , Amy1A and Amy3D showed distinct differences in their enzymatic characteristics . The chimeric enzyme Amy1A/3D , which consists of an Amy1A-type N-terminal domain and an Amy3D-type barrel structure , inherited enzymatic characteristics from the both isozymes . In this work , one other chimeric enzyme , Amy3D/1A , which is the counterpart of Amy1A/3D , has been characterized . The characteristics of these four enzymes are discussed in the light of the functional roles of protein domains . [ Sen. 6, subscore: 1.00 ]: The enzymes that have an Amy1A-type N-terminal domain , Amy1A and Amy1A/3D , showed high activity against soluble starch , while the enzymes that have an Amy3D-type barrel structure , Amy3D and Amy1A/3D , showed high activity in oligosaccharide hydrolysis . Rigidity of protein folding also significantly affected the enzyme activity in both soluble starch and oligosaccharide hydrolysis . Thus , the present work suggests that the structure of the N-terminal domain is important for stability and soluble starch hydrolysis , while the barrel structure that forms the active site significantly affects enzyme activities in oligosaccharide degradation . We have already characterized two rice alpha-amylase isozymes , Amy1A and Amy3D , and a chimeric enzyme engineered from these two isozymes , Amy1A/3D ( Terashima et al 1995 , 1996a , b ) . In spite of the high homology ( 70% ) of their amino acid sequences , Amy1A and Amy3D showed distinct differences in their enzymatic characteristics . The chimeric enzyme Amy1A/3D , which consists of an Amy1A-type N-terminal domain and an Amy3D-type barrel structure , inherited enzymatic characteristics from the both isozymes . In this work , one other chimeric enzyme , Amy3D/1A , which is the counterpart of Amy1A/3D , has been characterized . The characteristics of these four enzymes are discussed in the light of the functional roles of protein domains . [ Sen. 7, subscore: 1.00 ]: Rigidity of protein folding also significantly affected the enzyme activity in both soluble starch and oligosaccharide hydrolysis . Thus , the present work suggests that the structure of the N-terminal domain is important for stability and soluble starch hydrolysis , while the barrel structure that forms the active site significantly affects enzyme activities in oligosaccharide degradation . We have already characterized two rice alpha-amylase isozymes , Amy1A and Amy3D , and a chimeric enzyme engineered from these two isozymes , Amy1A/3D ( Terashima et al 1995 , 1996a , b ) . In spite of the high homology ( 70% ) of their amino acid sequences , Amy1A and Amy3D showed distinct differences in their enzymatic characteristics . The chimeric enzyme Amy1A/3D , which consists of an Amy1A-type N-terminal domain and an Amy3D-type barrel structure , inherited enzymatic characteristics from the both isozymes . In this work , one other chimeric enzyme , Amy3D/1A , which is the counterpart of Amy1A/3D , has been characterized . The characteristics of these four enzymes are discussed in the light of the functional roles of protein domains .
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