2.4.1.18 A310D the mutant shows strongly reduced activity compared to the wild type enzyme -, 756972 2.4.1.18 A310E the mutant shows strongly reduced activity compared to the wild type enzyme -, 756972 2.4.1.18 A310G the mutant shows strongly reduced activity compared to the wild type enzyme -, 756972 2.4.1.18 A310I the mutant shows strongly reduced activity compared to the wild type enzyme 756972 2.4.1.18 A310N the mutant shows strongly reduced activity compared to the wild type enzyme -, 756972 2.4.1.18 A310Q the mutant shows strongly reduced activity compared to the wild type enzyme -, 756972 2.4.1.18 D15A D15A-PvSBE2 enzyme shows 13.1% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value. 676385 2.4.1.18 D15E D15E-PvSBE2 enzyme shows 31.3% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value. 676385 2.4.1.18 D270A mutant with about 10% relative enzyme activity compared to wild-type enzyme 702734 2.4.1.18 D344A mutant without enzyme activity 702734 2.4.1.18 delN238-S247 loop-truncated mutant exhibits a 2-fold increase in activity relative to the wild type enzyme. The branching activity of the deletion variant is decreased. In the wild type enzyme, the degree of polymerization of the reaction products has peaks ranging from 7 to 12, while the loop-truncated mutant has peaks in the range of degree of polymerization 10 to 13, indicating that the chain lengths of the reaction products are slightly longer than that of the wild type enzyme. The flexible loop is associated with the catalytic process of GH57 glycogen branching enzymes and plays an important role in the branching activity and the variable lengths of the branches 744241 2.4.1.18 DELTA1-112 the wild-type enzyme transfers mainly chains with a degree of polymerization of 8-14, the mutant enzyme DELTA1-112 transfers a greater propertion of chains with higher degree of polymerization, 15-20 657658 2.4.1.18 DELTA1-112 truncated enzyme transferrs a greater amount of longer chains than the wild-type enzyme 657642 2.4.1.18 DELTA1-63 the wild-type enzyme transfers mainly chains with a degree of polymerization of 8-14, mutant enzyme has a pattern of transferred chains, 10-20 657658 2.4.1.18 DELTA1-83 the wild-type enzyme transfers mainly chains with a degree of polymerization of 8-14, mutant enzyme has a pattern of transferred chains, 10-20 657658 2.4.1.18 E185Q enzymatic activity is abolished 744241 2.4.1.18 E399A mutant with about 5% relative enzyme activity compared to wild-type enzyme 702734 2.4.1.18 E399Q supposed general acid/base residue, crystallization data 718762 2.4.1.18 E513D site-directed mutagenesis, the mutant shows a much lower activity compared to wild-type enzyme mSBEIIa 737078 2.4.1.18 G468D mutant with about 95% relative enzyme activity compared to wild-type enzyme 702734 2.4.1.18 H24A H24A-PvSBE2 enzyme shows 38.3% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value. 676385 2.4.1.18 H275A mutant without enzyme activity 702734 2.4.1.18 H467A mutant without enzyme activity 702734 2.4.1.18 I571D the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme -, 756760 2.4.1.18 M349H the mutant shows a slight decrease in specific activity compared with that of wild type enzyme -, 757039 2.4.1.18 M349S the mutant shows 21.1% increase in specific activity compared with that of wild type enzyme. The mutant displays 24.2% enhancement in the alpha-1,6-glycosidic linkage ratio of potato starch samples -, 757039 2.4.1.18 M349T the mutant shows 24.5% increase in specific activity compared with that of wild type enzyme. The mutant displays 24.2% enhancement in the alpha-1,6-glycosidic linkage ratio of potato starch samples -, 757039 2.4.1.18 M349Y the mutant displays a significant (33.9%) reduction in specific activity compared with that of wild type enzyme -, 757039 2.4.1.18 additional information a mutant lacking the N1 domain, i.e. lacking N-terminal residues 1-108, shows about 30% decrease in specific activity -, 719870 2.4.1.18 additional information ae mutant, BEIIb-deficient mutant 706172 2.4.1.18 additional information application of RNAi technology for improving amylose content in maize endosperm through the suppression of the ZmSBEIIa and ZmSBEIIb genes by hairpin SBEIIRNAi constructs. These SBEIIRNAi transgenes lead to the downregulation of ZmSBEII expression and SBE activity to various degrees and altered the morphology of starch granule 737052 2.4.1.18 additional information be1-1 (DYK140), T-DNA insertion mutant line for BE1. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type. 676422 2.4.1.18 additional information be1-1 be2-1, T-DNA insertion double mutant in enzyme BE1 and BE2. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type. 676422 2.4.1.18 additional information be1-1 be3-2, T-DNA insertion double mutant in enzyme BE1 and BE3. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type. 676422 2.4.1.18 additional information be1-2 (N637880), T-DNA insertion mutant line for BE1. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type. 676422 2.4.1.18 additional information be2-1 (EFH20), T-DNA insertion mutant line for BE2. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type. 676422 2.4.1.18 additional information be2-1 be3-2, T-DNA insertion double mutant in enzyme BE2 and BE3. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type. The be2-1 be3-2 double mutant is free of starch, coupled with an accumulation of very high levels of water-soluble glucans, that are not observable in other lines. Moreover, this double mutant displays a lower growth rate, a pale color and a general wilting of the inflorescence. 676422 2.4.1.18 additional information be2-2 (DSA16), T-DNA insertion mutant line for BE2. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type. 676422 2.4.1.18 additional information be3-1 (N548089), T-DNA insertion mutant line for BE3. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type. 676422 2.4.1.18 additional information be3-2 (EQJ13), T-DNA insertion mutant line for BE3. The amount of amylose and the branching level of amylopectin are not significantly different in the mutants when compared with the wild type. 676422 2.4.1.18 additional information chimeric enzymes of PvSBE2: only one chimeric recombinant protein ((I Na/2Nb)-II) has enzyme activity. It shows 6.1% of the specific activity of the wild type enzyme. 676385 2.4.1.18 additional information compared with the wild type enzyme, a truncation mutant made by removing the last 26 residues from its C-terminal end has enhanced thermostability and recovery ability without compromising enzymatic activity -, 756935 2.4.1.18 additional information concominant reduction in SBE IIb with suppression of SBE IIa 704889 2.4.1.18 additional information construction of chimeric enzymes of the isoenzymes PvSBE1 and PvSBE2 660279 2.4.1.18 additional information construction of domain-truncated (N1 and N) and N1-domain-swapped (with VvGBE N1 replacing the counter part of Escherichia coli GBE) mutants. The truncation mutants synthesize branched products with a greatly reduced proportion of short chains compared to the wild-type. The swapping mutant exhibit a branching pattern of the short chain region similar to that of the ewild-type enzyme -, 736108 2.4.1.18 additional information construction of enzyme point mutants by site-directed mutagenesis to change the chain-length distribution CLD by changing activity of enzyme SBE. The enzyme mutants show no or only a slight change in degree of polymerization of branched glucans 737078 2.4.1.18 additional information CT Dg, truncated at 3' end 701786 2.4.1.18 additional information CTT Dr, tuncated at 3' end -, 701786 2.4.1.18 additional information enzyme overexpression results in decrease cell proliferation when treated by deltamethrin 706066 2.4.1.18 additional information generation of N- and C-terminally truncated enzyme mutants. Activities of kinases on wild-type and enzyme mutants, overview -, 736465 2.4.1.18 additional information GGR, construction of chimeric genes, with C-domain of GBE of Deinococcus radiodurans 701786 2.4.1.18 additional information GGR, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus geothermalis -, 701786 2.4.1.18 additional information GRR, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus radiodurans 701786 2.4.1.18 additional information GRR, construction of chimeric genes, with N-domain of GBE of Deinococcus geothermalis -, 701786 2.4.1.18 additional information N-termial truncated enzyme of PvSBE2. Delta46-PvSBE2 has no branching enzyme activity. 676385 2.4.1.18 additional information NT Dg, tuncated at 5' end 701786 2.4.1.18 additional information production of highly branched amylopectin and amylose from rice starch in a multistep procedure using several different enzymes, for braching of amylose, the Bacillus subtilis 168 branching enzyme is used, analysis of the resulting structural changes, overview -, 680324 2.4.1.18 additional information recombinant TK1436 protein (amino acids [aa] 1 to 675) and a deletion derivative devoid of the C-terminal two-copy helix-hairpin-helix (HhH)2 motif (TK1436deltaH, aa 1 to 562) 674295 2.4.1.18 additional information RGG, construction of chimeric genes, with A-domain and C-domain of GBE of Deinococcus geothermalis -, 701786 2.4.1.18 additional information RGG, construction of chimeric genes, with N-domain of GBE of Deinococcus radiodurans 701786 2.4.1.18 additional information RRG, construction of chimeric genes, with C-domain of GBE of Deinococcus geothermalis -, 701786 2.4.1.18 additional information RRG, construction of chimeric genes, with N-domain and A-domain of GBE of Deinococcus radiodurans 701786 2.4.1.18 additional information SBE IIa-, transgenic line with suppressed SBE IIa 704889 2.4.1.18 additional information SBE IIa-/SBE IIb-, transgenic line with suppressed SBE IIb and suppressed SBE IIa 704889 2.4.1.18 additional information SBE IIb-, transgenic line with suppressed SBE IIb 704889 2.4.1.18 additional information starch from tubers of enzyme overexpressing plants posses an increased degree of amylopectin branching, with more short chains of degree of polymerisation (DP) 6-12 and particularly of DP6. Construction of transgenic lines expressing a GRANULE-BOUND STARCH SYNTHASE (GBSS) RNAi, which exhibit post-transcriptional gene silencing of GBSS and reduced amylose content in the starch. Both transgenic modifications do not affect granule morphology but reduce starch peak viscosity. In starch from SBEII-overexpressing lines, the increased ratio of short to long amylopectin branches facilitates gelatinisation, which occurs at a reduced temperature (by up to 3°C) or lower urea concentration. In contrast, silencing of GBSS increases the gelatinisation temperature by 4°C, and starch requires a higher urea concentration for gelatinisation. In lines with a range of SBEII overexpression, the magnitude of the increase in SBEII activity, reduction in onset of gelatinisation temperature and increase in starch swollen pellet volume are highly correlated, consistent with reports that starch swelling is greatly dependent upon the amylopectin branching pattern. Amylose content in starch and thermal properties of tuber starch granules from potato tubers of a range of lines exhibiting silencing of GBSS or overexpressing SBEII, overview 735845 2.4.1.18 additional information suppression of SBE IIa with concominant reduction in SBE IIb 704889 2.4.1.18 Q231K the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme -, 756760 2.4.1.18 Q231R the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme -, 756760 2.4.1.18 R28A R28A-PvSBE2 enzyme shows 10.7% of the specific activity of the wild type enzyme. The large decrease in the specific activities of the mutant is predominatly attributed to the reduced Vmax value. 676385 2.4.1.18 R28K R28K-PvSBE2 enzyme shows 93.5% of the specific activity of the wild type enzyme. 676385 2.4.1.18 R342A mutant with about 15% relative enzyme activity compared to wild-type enzyme 702734 2.4.1.18 R363K site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme mSBEIIa 737078 2.4.1.18 R384A mutation causes almost complete inactivation 636946 2.4.1.18 R384E mutation causes almost complete inactivation 636946 2.4.1.18 R384K residual activity of the mutant enzyme is 5% of the wild-type enzyme 636946 2.4.1.18 R384Q mutation causes almost complete inactivation 636946 2.4.1.18 R384S mutation causes almost complete inactivation 636946 2.4.1.18 R456K site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme mSBEIIa 737078 2.4.1.18 S147A site-directed mutagenesis 736465 2.4.1.18 S204A site-directed mutagenesis -, 736465 2.4.1.18 S286A site-directed mutagenesis -, 736465 2.4.1.18 S286A/S297A/S649A site-directed mutagenesis 736465 2.4.1.18 S297A site-directed mutagenesis -, 736465 2.4.1.18 S297A/S298A site-directed mutagenesis 736465 2.4.1.18 S298A site-directed mutagenesis -, 736465 2.4.1.18 S349F site-directed mutagenesis, creates an additional binding site for glucose, the mutant shows a much lower activity compared to wild-type enzyme mSBEIIa 737078 2.4.1.18 S568A site-directed mutagenesis 736465 2.4.1.18 S598A site-directed mutagenesis 736465 2.4.1.18 S649A site-directed mutagenesis 736465 2.4.1.18 S659A site-directed mutagenesis 736465 2.4.1.18 S699A site-directed mutagenesis 736465 2.4.1.18 S705A site-directed mutagenesis 736465 2.4.1.18 T339D the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme -, 756760 2.4.1.18 T339E the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme -, 756760 2.4.1.18 truncated enzyme form missing the first 107 amino- the purified full-length enzyme is poorly soluble and forms aggregates, which are inactive, at concentrations above 1 mg/ml. In contrast, the truncated form can be concentrated to 6 mg/ml without a visible signs of aggregation or loss of activity on concentration 636953 2.4.1.18 W22A complete loss of activity 744241 2.4.1.18 Y235A mutant with about 15% relative enzyme activity compared to wild-type enzyme 702734 2.4.1.18 Y300A mutant enzyme shows less than 1% of the wild-type activity 636959 2.4.1.18 Y300D mutant enzyme shows less than 1% of the wild-type activity 636959 2.4.1.18 Y300F mutant enzyme shows 25% of the wild-type activity, no effect on Km-value, heat stability is lowered significantly compared to that of the wild-type enzyme, lower relative activity at elevated temperatures compared to wild-type enzyme 636959 2.4.1.18 Y300L mutant enzyme shows less than 1% of the wild-type activity 636959 2.4.1.18 Y300S mutant enzyme shows less than 1% of the wild-type activity 636959 2.4.1.18 Y300W mutant enzyme shows less than 1% of the wild-type activity 636959 2.4.1.18 Y352F site-directed mutagenesis, , the mutant shows a much lower activity compared to wild-type enzyme mSBEIIa 737078