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2.4.1.19: cyclomaltodextrin glucanotransferase

This is an abbreviated version!
For detailed information about cyclomaltodextrin glucanotransferase, go to the full flat file.

Word Map on EC 2.4.1.19

Reaction

alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose
=
alpha-cyclodextrin
 +
alpha-D-glucose

Synonyms

1,4-alpha-D-glucopyranosyl transferase, Akrilex C cyclodextrin glycosyltransferase, alpha-1,4-glucan 4-glycosyltransferase, cyclizing, alpha-cgt, alpha-CGTase, alpha-cyclodextrin glucanotransferase, alpha-cyclodextrin glucosyltransferase, alpha-cyclodextrin glycosyltransferase, Bacillus macerans amylase, beta-CGTase, beta-cyclodextrin glucanotransferase, beta-cyclodextrin glucosyltransferase, beta-cyclodextrin glycosyltransferase, beta-cyclodextrinase, BMA, C-CGTase, CD glucanotransferase, CGT, CGT13, CGTase, cgtS, CGTse ET1, CGT_TK, cyclodextrin beta-glucanotransferase, cyclodextrin glucanotransferase, cyclodextrin glucosyltransferase, cyclodextrin glycosyl transferase, cyclodextrin glycosyltransferase, cyclodextrin-glycosyltransferase, cyclodextrinase, cyclomaltodextrin glucanyltransferase, cyclomaltodextrin glucotransferase, cyclomaltodextrin glycanotransferase, cyclomaltodextrin glycosyltransferase, gamma-CGTase, gamma-cyclodextrin glycosyltransferase, konchizaimu, M-CGTase, More, neutral-cyclodextrin glycosyltransferase, PFCGT, Toruzyme

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.19 cyclomaltodextrin glucanotransferase

Engineering

Engineering on EC 2.4.1.19 - cyclomaltodextrin glucanotransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F183L
-
strain 1011, decreases affinity of acarbose
F259L
-
strain 1011, decreases affinity of acarbose
F283L
F283Y
-
mutation decreases the enzymatic activity in the basic pH range
H233Y
the mutant primarily produces maltoheptaose using beta-cyclodextrin via a hydrolysis reaction. The mutant enzyme also shows hydrolyzing activity against gamma-cyclodextrin but is unable to catalyze the hydrolysis of alpha-cyclodextrin
N132R
introduction of an ionic interaction at the first Ca2+ site, disruption of catalytic activity
N28R
introduction of an additional ionic interaction at the second Ca2+ site, mutant displays increased cyclization activity
S182E
mutation adjacent to the first Ca2+ site and the active site cleft. Mutant shows enhanced thermostability, and decreased catalytic activity
S182G
mutation adjacent to the first Ca2+ site and the active site cleft. Increase in half-life at 60°C to 94 min
Y195F
-
strain 1011
Y195I
-
the mutant produces less alpha-cyclodextrin, slightly more beta-cyclodextrin, and 3-4times more gamma-cyclodextrin than the wild type enzyme
Y195L
Y93F
-
the substitution causes no alpha-cyclodextrin formation, but produces 6% more beta-cyclodextrin, 16% less gamma-cyclodextrin, and decreases its kcat and kcat/Km values
F183L
-
strain 1011, decreases affinity of acarbose
-
F259L
-
strain 1011, decreases affinity of acarbose
-
F283L
-
starch degrading activity is similar to that of wild-type enzyme between the acidic and neutral pH ranges but decreases to 10% at pH 10.0. The pH-value of half-maximal activity at basic pH side is shifted to 8.6 from 10.0 of the wild-type. 23%-67% decrease in KM-value for 3-ketobutylidene-beta-2-chloro-4-nitrophenylmalto-pentaoside in the disproportionation reaction. The turnover-number for the disproportionating reaction at various pH conditions decreases to 1.6% to 4.4% compared with those of wild-type enzyme
-
F283Y
-
mutation decreases the enzymatic activity in the basic pH range
-
Y195F
-
strain 1011
-
Y195L
F183L
-
strain 1011, decreases affinity of acarbose
-
F259L
-
strain 1011, decreases affinity of acarbose
-
Y195F
-
strain 1011
-
Y195L
Y195I
-
the mutant produces less alpha-cyclodextrin, slightly more beta-cyclodextrin, and 3-4times more gamma-cyclodextrin than the wild type enzyme
-
Y93F
-
the substitution causes no alpha-cyclodextrin formation, but produces 6% more beta-cyclodextrin, 16% less gamma-cyclodextrin, and decreases its kcat and kcat/Km values
-
F183L
-
strain 1011, decreases affinity of acarbose
-
F259L
-
strain 1011, decreases affinity of acarbose
-
Y195F
-
strain 1011
-
Y195L
N132R
-
introduction of an ionic interaction at the first Ca2+ site, disruption of catalytic activity
-
N28R
-
introduction of an additional ionic interaction at the second Ca2+ site, mutant displays increased cyclization activity
-
S182E
-
mutation adjacent to the first Ca2+ site and the active site cleft. Mutant shows enhanced thermostability, and decreased catalytic activity
-
S182G
-
mutation adjacent to the first Ca2+ site and the active site cleft. Increase in half-life at 60°C to 94 min
-
H233Y
-
the mutant primarily produces maltoheptaose using beta-cyclodextrin via a hydrolysis reaction. The mutant enzyme also shows hydrolyzing activity against gamma-cyclodextrin but is unable to catalyze the hydrolysis of alpha-cyclodextrin
-
D358R
the mutant forms mainly cyclodextrins with 8-12 glucose units during a reaction time of 24 h from soluble starch
Y183R
the mutant has completely lost its ability to synthesize beta-cyclodextrin from soluble starch, and gamma-cyclodextrin and the larger cyclodextrins are the only cyclic oligosaccharides produced
Y183R/D358R
the mutant almost completely loses its cyclization activity (1.3% activity compared to the wild type enzyme)
Y183W
the mutant mainly produces gamma-cyclodextrin from soluble starch
Y183W/D358R
the mutant shows very low beta-cyclodextrin cyclization activity and an increased formation of the larger cyclodextrins
D355R
the mutant shows 164% of wild type activity, and the mutation does not have significant negative effect on stability when compared to the wild type
R254F
the mutant shows 196% of wild type activity, and the mutation does not have significant negative effect on stability when compared to the wild type
Y127F
the mutant shows 210% of wild type activity, and the mutation does not have significant negative effect on stability when compared to the wild type
P176G
P176I
-
the mutant is increased by 9.4 % on cyclodextrin production, indicating replacement of hydrophobic amino acids significantly improve in cyclization activity
P176K
-
the substrate affinity of the mutant is increased by 14% and the catalytic efficiency is increased by 14% compared to the wild type
P176L
-
the mutant is increased by 7.9 % on cyclodextrin production, indicating replacement of hydrophobic amino acids significantly improve in cyclization activity
DELTA154–160
-
mutation increases cyclization activity around 1.5times without any significant reduction of coupling and hydrolyzing activities, conversion yield into cyclodextrins is 39% higher than that of wild-type enzyme without any recognizable change in cyclodextrin ratio. pH-Stability decreases drastically in acidic pH region. Decrease in thermal stability
Y96M
-
mutation increases cyclization activity around 1.5times without any significant reduction of coupling and hydrolyzing activities, conversion yield into cyclodextrins is 28.6% higher than that of wild-type enzyme without any recognizable change in cyclodextrin ratio. Decrease in thermal stability
A223H
-
mutant snzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 2fold increases at pH 7.5. pH activity profiles of the mutant shows higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase
A223K
-
mutant enzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 3fold increases at pH 7.5. pH activity profiles of the mutant show higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase
A223R
-
mutant enzyme shows a 4fold increase in gamma-cycodextrin-forming activity at pH 7.5 and 1.5fold increase in activity at pH 10.0. Mutant enzyme shows higher activity in pH range pH 6-10.5
A223H
-
mutant snzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 2fold increases at pH 7.5. pH activity profiles of the mutant shows higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase
-
A223K
-
mutant enzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 3fold increases at pH 7.5. pH activity profiles of the mutant show higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase
-
A223R
-
mutant enzyme shows a 4fold increase in gamma-cycodextrin-forming activity at pH 7.5 and 1.5fold increase in activity at pH 10.0. Mutant enzyme shows higher activity in pH range pH 6-10.5
-
F191Y
-
Phe at position 191 replaced by Tyr
F255I
-
cyclodextrins undetectable
I631T
the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability
I641T
the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability
K647E
the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability
F191Y
-
Phe at position 191 replaced by Tyr
-
I631T
-
the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability
-
I641T
-
the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability
-
K647E
-
the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability
-
F191Y
-
Phe at position 191 replaced by Tyr
-
A230V
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
A315D
-
the mutation significantly changes the contribution of Ca2+ to the enzyme's thermostability
D577A
D577E
-
the mutant displays an 11.2% increase in the beta-cyclization activity compared to the wild type enzyme
D577G
D577H
-
the mutant displays a slight decrease in the beta-cyclization activity compared to the wild type enzyme
D577I
D577K
D577L
D577R
D577V
F283L
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
H140Q
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
K192R
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 11.6 min for the mutant enzyme
K232E
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
K427S/V615L
reduction of cyclodextrin-forming activity
L600E
the mutant shows wild type cyclization activities. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
L600I
the mutant shows decreased cyclization activities compared to the wild type enzyme. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
L600R
the mutant shows increased cyclization activities compared to the wild type enzyme. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
L600Y
the mutant shows wild type cyclization activities. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
N188D
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 35 min for the mutant enzyme
N188D/K192R
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 56 min for the mutant enzyme
Q179G
-
mutation to residue G which is conserved in all the corresponding enzymes except in that from Bacillus circulans Df 9R. Activity and kinetic parameters remain unchanged
Q179L
-
mutation results in a different ratio of cyclodextrin products with a ratio for alpha- to beta- to gamma-cyclodextrin 1:1.7:0.7, a lower catalytic efficiency, and a decreased ability to convert starch into cyclodextrins
T185S
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 14.8 min for the mutant enzyme
T186Y
-
decrease in half-life at 60°C from 9.7 min for the wild-type enzyme to 8 min for the mutant enzyme
Y89D
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 14.3% and 17.6%, respectively
Y89D/D577R
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 14% and 35.1%, respectively
Y89G
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 10.6% and 14.6%, respectively
Y89G/D577R
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 25% and 29.3%, respectively
Y89N
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 8.9% and 13%, respectively
Y89N/D577R
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 19.4% and 25.2%, respectively
A230V
-
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
-
F283L
-
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
-
H140Q
-
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
-
K232E
-
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
-
K427S/V615L
-
reduction of cyclodextrin-forming activity
-
Q179G
-
mutation to residue G which is conserved in all the corresponding enzymes except in that from Bacillus circulans Df 9R. Activity and kinetic parameters remain unchanged
-
Q179L
-
mutation results in a different ratio of cyclodextrin products with a ratio for alpha- to beta- to gamma-cyclodextrin 1:1.7:0.7, a lower catalytic efficiency, and a decreased ability to convert starch into cyclodextrins
-
D577A
D577E
-
the mutant displays an 11.2% increase in the beta-cyclization activity compared to the wild type enzyme
-
D577G
D577H
-
the mutant displays a slight decrease in the beta-cyclization activity compared to the wild type enzyme
-
D577I
D577K
-
the mutant displays a 1.5% increase in the beta-cyclization activity compared to the wild type enzyme
-
D577L
D577R
D577V
L600E
-
the mutant shows wild type cyclization activities. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
-
L600I
-
the mutant shows decreased cyclization activities compared to the wild type enzyme. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
-
L600R
-
the mutant shows increased cyclization activities compared to the wild type enzyme. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
-
L600Y
-
the mutant shows wild type cyclization activities. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
-
Y89D
-
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 14.3% and 17.6%, respectively
-
Y89D/D577R
-
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 14% and 35.1%, respectively
-
Y89G/D577R
-
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 25% and 29.3%, respectively
-
Y89N
-
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 8.9% and 13%, respectively
-
A137V
-
the mutation produces a perturbation in the catalytic site of the enzyme which correlates with a 10fold reduction in its catalytic efficiency. Moreover, this mutant shows increased production of maltooligosaccharides with a high degree of polymerization, mostly maltopentaose to maltoheptaose
A144V
-
the mutant shows slightly reduced activity compared to the wild type enzyme
L280A
-
the mutant displays an about 30% reduction in its catalytic efficiency as compared to the wild type enzyme
M329I
-
the mutant shows slightly reduced activity compared to the wild type enzyme
A137V
-
the mutation produces a perturbation in the catalytic site of the enzyme which correlates with a 10fold reduction in its catalytic efficiency. Moreover, this mutant shows increased production of maltooligosaccharides with a high degree of polymerization, mostly maltopentaose to maltoheptaose
-
A144V
-
the mutant shows slightly reduced activity compared to the wild type enzyme
-
L280A
-
the mutant displays an about 30% reduction in its catalytic efficiency as compared to the wild type enzyme
-
M329I
-
the mutant shows slightly reduced activity compared to the wild type enzyme
-
A156V
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme
A156V/A166Y
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme
A156V/L174P
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme
A156V/L174P/A166Y
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme
A166Y
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme
A166Y/L174P
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme
D372K
-
site-directed mutagenesis, the mutant shows a great shift in substrate specificity towards the production of alpha-cyclodextrin
D372K/Y89R
-
site-directed mutagenesis, the mutant enzyme shows a 1.5fold increase in the production of alpha-cyclodextrin, with a concomitant 43% decrease in the production of beta-cyclodextrin compared to the wild-type CGTase
K47F
improved synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid with maltodextrin as glucosyl donor, 30% increase in yield. Mutation leads to relatively lower cyclization activities and higher disproportionation activities. The enhancement of maltodextrin specificity may be due to the short residue chain and the removal of hydrogen bonding interactions between the side chain of residue 47 and the sugar at -3 subsite
K47H
-
site-directed mutagenesis, the mutant shows a shift in product specificity, slight enhancement of beta-cyclodextrin production and slight reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47R
-
site-directed mutagenesis, the mutant shows a shift in product specificity, slight enhancement of beta-cyclodextrin production and slight reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47S
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47T
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47V
improved synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid with maltodextrin as glucosyl donor, 48% increase in yield. Mutation leads to relatively lower cyclization activities and higher disproportionation activities. The enhancement of maltodextrin specificity may be due to the short residue chain and the removal of hydrogen bonding interactions between the side chain of residue 47 and the sugar at -3 subsite
K47W
improved synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid with maltodextrin as glucosyl donor, 24% increase in yield. Mutation leads to relatively lower cyclization activities and higher disproportionation activities. The enhancement of maltodextrin specificity may be due to the short residue chain and the removal of hydrogen bonding interactions between the side chain of residue 47 and the sugar at -3 subsite
L174P
the mutant shows increased sophoricoside glycosylation activity compared to the wild type enzyme
Q265K
Q265K/Y195S
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 226% hydrolysis (starch-degrading) activities compared to the wild type enzyme
R146A/D147P
-
the double mutant exhibits a ratio of alpha-cyclodextrin to total cyclodextrin production of 75.1%, approximately one-fifth greater than that of the wild-type enzyme (63.2%), without loss of thermostability
R146P/D147A
-
the double mutant exhibits a ratio of alpha-cyclodextrin to total cyclodextrin production of 76.1%, approximately one-fifth greater than that of the wild-type enzyme (63.2%), without loss of thermostability
Y167H
Y195I
-
the mutation drastically alters the cyclodextrin specificity of the enzyme by switching toward the synthesis of both beta- and gamma-cyclodextrins
Y195S
Y195S/Q265K
-
compared with the wild type enzyme, the mutant has no cyclization activity and 498% hydrolysis and disproportionation activity
Y195S/Y260R
-
compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
Y260R
Y260R/Q265K
-
compared with the wild type enzyme, the mutant has 8% cyclization activity and 213% hydrolysis activity
Y260R/Q265K/Y195S
-
the mutant shows 12% cyclization (alpha-cyclodextrin-forming) and 557% hydrolysis (starch-degrading) activities compared to the wild type enzyme
Y260R/Y195S
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 492% hydrolysis (starch-degrading) activities compared to the wild type enzyme
Y89D
-
site-directed mutagenesis, the mutant shows a shift in substrate specificity towards the production of alpha-cyclodextrin
Y89K
-
site-directed mutagenesis, the mutant shows a shift in substrate specificity towards the production of alpha-cyclodextrin
Y89N
-
site-directed mutagenesis, the mutant shows a shift in substrate specificity towards the production of alpha-cyclodextrin
Y89R
-
site-directed mutagenesis, the mutant shows a great shift in substrate specificity towards the production of alpha-cyclodextrin
Y167H
Y195I
-
the mutation drastically alters the cyclodextrin specificity of the enzyme by switching toward the synthesis of both beta- and gamma-cyclodextrins
-
K47H
-
site-directed mutagenesis, the mutant shows a shift in product specificity, slight enhancement of beta-cyclodextrin production and slight reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
K47L
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
K47R
-
site-directed mutagenesis, the mutant shows a shift in product specificity, slight enhancement of beta-cyclodextrin production and slight reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
K47S
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
K47T
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
-
Q265K
-
the mutant shows 15% cyclization (alpha-cyclodextrin-forming) and 236% hydrolysis (starch-degrading) activities compared to the wild type enzyme
-
Y195S
Y260R
A315D
the mutation decreases starch conversion activity. The mutant exhibits the highest thermostability at 60-70°C for 30 min compared to the wild type enzyme
A315H
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
A315R
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
A315S
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
H233D
the mutation decreases starch conversion activity
S145D
the mutation decreases starch conversion activity
S145G
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
S145P
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
Y100A
the mutation decreases starch conversion activity
Y100D
the mutation decreases starch conversion activity
Y100I
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
Y100T
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
Y167H
the mutation increases starch conversion activity, particularly the beta-cyclodextrin-forming activity
Y195A
the mutation strongly decreases starch conversion activity
Y195E
the mutation decreases starch conversion activity
Y195T
the mutation decreases starch conversion activity
Y195V
the mutation decreases starch conversion activity
Y89S
the mutation decreases starch conversion activity
synthesis
-
immobilization of enzyme on mesoporous silica microspheres produces high yields of immobilization, up to 83%, and activity recoveries, up to 73%. The soluble enzyme and its immobilized form show similar values for the optimal pH activity, while optimal reaction temperatures are 100°C and 80°C, respectively. The immobilized enzyme shows similar values for Km and thermal stabilities as the soluble form, while its Vmax is lower. The immobilized enzyme was tested in repeated batches in order to simulate recovery and reuse, keeping about 60% of the initial catalytic activity after 15 cycles
S77P
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, molecular modelling of the location and effect of S77P mutation on the Tabium CGTase active-site conformation
W239L
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, the mutation destroys a hydrogen-bonding interaction between the side chains of Asp209 and Trp239, compromising the stability of the mutant
W239R
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, the mutation destroys a hydrogen-bonding interaction between the side chains of Asp209 and Trp239, compromising the stability of the mutant
S77P
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, molecular modelling of the location and effect of S77P mutation on the Tabium CGTase active-site conformation
-
W239L
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, the mutation destroys a hydrogen-bonding interaction between the side chains of Asp209 and Trp239, compromising the stability of the mutant
-
W239R
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, the mutation destroys a hydrogen-bonding interaction between the side chains of Asp209 and Trp239, compromising the stability of the mutant
-
additional information