2.4.1.25 A406L the mutant shows higher thermostability at 35-40°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.1fold) and disproportionation (1.4fold) than those of the wild type -, 736255 2.4.1.25 A406V site-directed mutagenesis, the mutant shows higher thermostability and gives higher amount of LR-CD products, in comparison to the wild-type enzyme 777118 2.4.1.25 A406V the mutant shows higher thermostability at 50°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.8fold) and disproportionation (2.1fold) than those of the wild type -, 736255 2.4.1.25 A413F site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The A413F mutation affects the enzyme activities: starch tranglycosylation, disproportionation and cyclization -, 777118 2.4.1.25 D214N the specific activity of the D214N mutant is decreased about 10000fold as compared with that of the wild-type enzyme -, 489022 2.4.1.25 D293A site-directed mutagenesis of the active site nucleophile, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme -, 685153 2.4.1.25 D293N site-directed mutagenesis of the active site nucleophile, the D293N mutation reduces the pH stability of the enzyme, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme -, 685153 2.4.1.25 D294S site-directed mutagenesis, the mutant shows highly reduced kcat and reduced activity with malto-oligomers compared to the wild-type enzyme 685153 2.4.1.25 D395A site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme 685153 2.4.1.25 D395N site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme -, 685153 2.4.1.25 E123Q the specific activity of the mutant enzyme toward maltotriose is about 15000fold lower than the specific activity of the wild-type enzyme 726933 2.4.1.25 E129Q the specific activity of the mutant enzyme is almost the same as that of the wild-type enzyme 726933 2.4.1.25 E231Y site-directed mutagenesis, the E231Y mutant exhibits much higher kcat and Km values for starch transglycosylation, compared to that of the wild-type -, 777118 2.4.1.25 E340A site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme -, 685153 2.4.1.25 E340Q site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme -, 685153 2.4.1.25 E758Q the mutant shows highly reduced activity compared to the wild-type enzyme 687557 2.4.1.25 F251G mutation results in significantly lower glucose production but increased maltose production from maltopentose substrates, showing an altered substrate-binding affinity 721013 2.4.1.25 F366L site-directed mutagenesis, the mutant shows reduced kcat compared and reduced activity with malto-oligomers compared to the wild-type enzyme 685153 2.4.1.25 G417F site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type, but with low yield. The G417F mutation hinders the enzyme's cyclization activity 777118 2.4.1.25 H461A the mutation leads to a significant (8.6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate -, 755897 2.4.1.25 H461D the mutation leads to a significant (3.4fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate -, 755897 2.4.1.25 H461R the mutation leads to a significant (6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate -, 755897 2.4.1.25 H461S the mutation leads to a significant (3.4fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate -, 755897 2.4.1.25 H461W the mutation leads to a significant (6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate -, 755897 2.4.1.25 additional information an agtA knockout of Aspergillus niger shows an increased susceptibility towards the cell wall-disrupting compound, phenotypic characterization of CFW hypersensitive DELTAagtA strain and AgtA/AgtB overexpression strains, overview 686463 2.4.1.25 additional information enzymatic modification of rice starch to produce highly branched amylopectin and amylose using alpha-glucanotransferase and maltogenic amylase, overview 680324 2.4.1.25 additional information generation of truncated mutant DELTA167 that exhibits no starch transglycosylation activity, indicating that the N-terminal domain of CgAM is necessary for enzyme activity. Mutants molecular dynamic simulations, overview. The wild-type enzyme exhibits cyclization specific activity at 0.0012 U/mg, while P228Y, E231Y and G417F mutants show the same level of specific activity at range 0.0007 0.0013 U/mg -, 777118 2.4.1.25 additional information in the crumb of fresh white wheat bread, starch is fully gelatinized. Its molecular and three-dimensional structure are major factors limiting the rate of its digestion. In situ modification of starch during bread making with starch-modifying enzymes (maltogenic amylase and amylomaltase) and analysis of the impact thereof on bread characteristics, starch retrogradation and digestibility, overview. Maltogenic amylase treatment increases the relative content of short amylopectin chains. This results in lower starch retrogradation and crumb firmness upon storage, and reduces extent (up to 18%) of in vitro starch digestion for fresh and stored breads. Amylomaltase only modestly shortens amylose chains and has no measurable impact on amylopectin structure. Modification with this enzyme leads to slower bread crumb firming but does not influence starch digestibility 777344 2.4.1.25 additional information mutations in the N-terminal region result in a sharp increase in alpha-1,4-transferase activity and a reduced level of alpha-1,6-glucosidase activity, overview 693147 2.4.1.25 additional information optimization of amylomaltase for the synthesis of alpha-arbutin derivatives as tyrosinase inhibitors. Incubation of AMase with the tapioca starch donor and an alpha- or beta-arbutin acceptor yields at least three glycoside products. AMase has higher disproportionation and cyclization activities but lower hydrolysis activity compared to CGTase 776915 2.4.1.25 additional information the amino acid substitution at Y54 or Y101 for removing their aromatic side chain increases cyclization activity, intra-molecular transglycosylation reaction, but decreases disproportionation, coupling and hydrolytic activities, inter-molecular reactions 687849 2.4.1.25 additional information the deletion mutant DELTAN130 is unable to use glycogen but has high disproportionating activity with maltodextrins 687557 2.4.1.25 additional information the expression level of the recombinant enzyme in Escherichia coli is not very high. Analysis of the mRNA of initial seven codons at the 5'-end of the gene reveals the presence of a hair pin like secondary structure. This secondary structure is removed by site-directed mutagenesis, without altering the amino acids, which results in enhanced expression of the cloned gene -, 777638 2.4.1.25 additional information the glycosyl hydrolase domain alone provides disproportionating activity with a much higher affinity for short maltodextrins than the complete wild-type enzyme, while absence of the carbohydrate binding modules completely abolishes activity with large complex carbohydrates, reflecting the presumed function of DPE2 in vivo 687741 2.4.1.25 additional information the starch-binding domains of Bacillus stearothermophilus ET1 CGTase (E and DE) are introduced into the C-terminus of TAalphaGT to enhance the starch utilizing activity. The chimeric enzymes, TAalphaGT-E and TAalphaGT-DE, show no difference in temperature optimum, transglycosylation activity, and amylolytic degradation pattern compared to TAalphaGT wild-type. However, TAalphaGT-DE exhibits the highest molar specific activity toward amylose. TAalphaGT-DE modifies amylopectin molecules by its disproportionating activities to produce modified amylopectin clusters (MW 100000–1000000) and produces cyclo-amyloses with DP of 19 through 35 from amylose molecules -, 672924 2.4.1.25 N287Y site-directed mutagenesis, the mutant exhibits a higher thermostability, a changed LR-CD profile, and an increased substrate preference for maltoheptaose (G5) compared to wild-type 777118 2.4.1.25 N287Y the mutant shows a significant decrease in all transglucosylation activities including starch transglucosylation, disproportionation, cyclization and coupling compared to the wild type enzyme, while hydrolysis activity is not changed. The mutant shows an increase in thermostability and substrate preference for maltoheptaose in addition to maltotriose -, 755942 2.4.1.25 P228Y site-directed mutagenesis, the mutant produces larger LR-CDs from CD36-CD40 as compared to CD29 by the wild-type. The P228Y mutation significantly lowers the kcat of disproportionation activity compared to wild-type -, 777118 2.4.1.25 Q256G mutation results in increased Km for maltotriose and a sharp decrease of the transglycosylation factor for maltose 721013 2.4.1.25 W229H kcat/KM value of transglycosylation activity significantly decreases to about 15% of wild-type, kcat/Km value of hydrolysis activity changes little 672394 2.4.1.25 W258G mutant shows neither cyclization nor coupling activity, suggesting that residue Trp258 plays an essential role in all catalytic activities including hydrolysis and transglycosylation activities 721013 2.4.1.25 W330A inactive 736249 2.4.1.25 W425A inactive 736249 2.4.1.25 W673A inactive 736249 2.4.1.25 Y172A mutant exhibits lower disproportionation, cyclization, and hydrolysis activities than the wild-type. The kcat/Km of the disproportionation reaction for the Y172A enzyme is 2.8fold lower than that of wild-type. The Y172A enzyme shows a product pattern different from that of wild-type at a long incubation time. The principal large-ring cyclodextrin products of the Y172A mutant are a cycloamylose mixture with a degree of polymerization of 28 or 29 718654 2.4.1.25 Y172A site-directed mutagenesis, the mutation causes a shift of principal LR-CDs to the larger size products 777118 2.4.1.25 Y23A site-directed mutagenesis, the mutation affects the kinetic parameters of starch transglycosylation and cyclization -, 777118 2.4.1.25 Y418A the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch 755955 2.4.1.25 Y418D the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch 755955 2.4.1.25 Y418F the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 29-33 from pea starch 755955 2.4.1.25 Y418R the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch 755955 2.4.1.25 Y418S the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch 755955 2.4.1.25 Y418W the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch 755955 2.4.1.25 Y54A hydrolytic activity is 39% of the wild-type value, cyclization activity is 192% of the wild-type value 660768 2.4.1.25 Y54A site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54C hydrolytic activity is 48% of the wild-type value, cyclization activity is 122% of the wild-type value 660768 2.4.1.25 Y54C site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54D hydrolytic activity is 38% of the wild-type value, cyclization activity is 177% of the wild-type value 660768 2.4.1.25 Y54D site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54E hydrolytic activity is 48% of the wild-type value, cyclization activity is 157% of the wild-type value 660768 2.4.1.25 Y54E site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54F hydrolytic activity is 96% of the wild-type value, cyclization activity is 91% of the wild-type value 660768 2.4.1.25 Y54F site-directed mutagenesis, the mutant shows increased coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54G hydrolytic activity is 16% of the wild-type value, cyclization activity is 167% of the wild-type value 660768 2.4.1.25 Y54G site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54H hydrolytic activity is 76% of the wild-type value, cyclization activity is 164% of the wild-type value 660768 2.4.1.25 Y54H site-directed mutagenesis, the mutant shows increased coupling and reduced disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54I hydrolytic activity is 33% of the wild-type value, cyclization activity is 157% of the wild-type value 660768 2.4.1.25 Y54I site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54K hydrolytic activity is 99% of the wild-type value, cyclization activity is 176% of the wild-type value 660768 2.4.1.25 Y54K site-directed mutagenesis, the mutant shows unaltered coupling but reduced disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54L hydrolytic activity is 39% of the wild-type value, cyclization activity is 189% of the wild-type value 660768 2.4.1.25 Y54L site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54M hydrolytic activity is 39% of the wild-type value, cyclization activity is 81% of the wild-type value 660768 2.4.1.25 Y54M site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54N hydrolytic activity is 30% of the wild-type value, cyclization activity is 159% of the wild-type value 660768 2.4.1.25 Y54N site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54P hydrolytic activity is 5% of the wild-type value, cyclization activity is 48% of the wild-type value 660768 2.4.1.25 Y54P site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54Q hydrolytic activity is 70% of the wild-type value, cyclization activity is 168% of the wild-type value 660768 2.4.1.25 Y54Q site-directed mutagenesis, the mutant shows unaltered coupling but reduced disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54R hydrolytic activity is 70% of the wild-type value, cyclization activity is 200% of the wild-type value 660768 2.4.1.25 Y54R site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54S hydrolytic activity is 38% of the wild-type value, cyclization activity is 186% of the wild-type value 660768 2.4.1.25 Y54S site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54T hydrolytic activity is 22% of the wild-type value, cyclization activity is 149% of the wild-type value 660768 2.4.1.25 Y54T site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54V hydrolytic activity is 29% of the wild-type value, cyclization activity is 160% of the wild-type value 660768 2.4.1.25 Y54V site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849 2.4.1.25 Y54W hydrolytic activity is 20% of the wild-type value, cyclization activity is 95% of the wild-type value 660768 2.4.1.25 Y54W site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme 687849