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3.2.1.1: alpha-amylase

This is an abbreviated version!
For detailed information about alpha-amylase, go to the full flat file.

Word Map on EC 3.2.1.1

Reaction

(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose
+
H2O
=
(alpha-D-glucopyranosyl-(1-4))n-m-alpha-D-glucopyranose
 +
(alpha-D-glucopyranosyl-(1-4))m-alpha-D-glucopyranose

Synonyms

1,4-alpha-D-glucan glucanohydrolase, 1,4-alpha-D-glucan glucanohydrolase and endoamylase, 1,4-alpha-D-glucan-glucanohydrolase, ABA, acid-stable amylase, acidic amylase, AGXA, AHA, alkaline alpha-amylase, alkalophilic Bacillus alpha-amylase, alpha amylase, alpha amylase 1, alpha-(1,4)-D-glucan glucanohydrolase, alpha-1,4 glucan-glucanohydrolase, alpha-1,4-glucan-4-glucanohydrolase, alpha-1-4 D-glucan glucanohydrolase, alpha-amylase, alpha-amylase 1, alpha-amylase 2, alpha-amylase 3, alpha-amylase A4, alpha-amylase Aasp, alpha-amylase AI, alpha-amylase AOA, Alpha-amylase carcinoid, alpha-amylase CMA, alpha-amylase gt, alpha-amylase HA, alpha-amylase I, alpha-amylase II, alpha-amylase PA, alpha-amylase PPA, alpha-amylase type A isozyme, alpha-amylase type II, alpha-amylase ZSA, alpha-amylases 1, AMF-3, ami, Amy, Amy B, Amy c6, Amy I, Amy II, Amy-1E, amy-CS2, Amy-E, Amy-FC1, AMY1, AMY121, AMY2, Amy3, amy5, Amy7C, AmyA, AmyB, AmyC, AmyCR, AmyD, AmyD-1, AmyE, AmyH, AmyI-1, AmyI3C6, AmyK, AmyK38, AmyL, Amyl III, amylase AI, amylase AII, amylase I, Amylase THC 250, amylase, alpha-, Amylopsin, amylopullulanase, AmyN26, AmyP, AmyQ, AmyS, AmyUS100, AmyUS100DELTAIG, AmyZ2, AOA, AoA1, AoA2, ApkA, Apu, B4168_3135, Ba-amy, BAA, Bacillus licheniformis alpha-amylase, Bactosol TK, barley alpha-amylase 1, BBG7_0117, BGTG-1, BH072alpha-amylase, BHA, BiLA, BLA, Blamy-I, bllj_0710, BMA.2, BSA-2, Bsamy-I, BSTA, Buclamase, Ca2+-independent alpha-amylase gt, CcAmy, CCAP, Clarase, Clone 103, Clone 168, Clone PHV19, Clones GRAMY56 and 963, cold-active alpha-amylase, cold-adapted alpha-amylase, ComA, crustacean cardioactive peptide, diastase, endo-1,4-alpha-D-glucan glucanohydrolase, endo-1,4-alpha-D-glucan glucohydrolase, endo-1,4-alpha-D-glucanohydrolase, endoamylase, FORILASE NTL alpha-amylase, Fortizyme, Fungamyl 800 L, G 995, G6-amylase, GH13Amy-1, GH13Amy-2, glycogenase, Gt-amy, HaAmy1, HaAmy2, haloalkaline alpha-amylase, HAS, HdAmyI, High pI alpha-amylase, HPA, HSA, HSAmy, HSAmy-ar, htur2110, human salivary alpha-amylase, hyperthermophilic alpha-amylase, Isozyme 1B, Kleistase L 1, KRA, LAMY, liquozyme, LLF-alpha-amylase, Low pI alpha-amylase, MalA, maltogenic amylase, maltohexaose-producing alpha-amylase, maltotriose-producing alpha-amylase, MAmy, Maxamyl, Maxilase, Meiotic expression upregulated protein 30, MJA1, More, N8 alpha-amylase, neutral amylase, Pancreatic alpha-amylase, PFTA, Pivozin, PPA, PPA-I, PPA-II, psychrophilic alpha amylase, Ptyalin, raw-starch-digesting alpha-amylase, RB5AMG_01539, Rbamy5, RBLA, RBSA-1, ROAmy, Ruminococcus bromii intermediary alpha-amylase 5, Saci_1162, salt-tolerant alpha-amylase, ScAmy43, Sfamy, Spitase CP 1, SSO1172, SusG, TAA, TaAmy3, Taka-amylase A, Takatherm, TcAmy, TdAmyA, tergal gland protein-1, TfAmy48, Thermamyl, Thermolase, thermostable alpha-amylase, TO_amyl, Tp-AmyS, TVA II, VAAmy1, VAAmy2, VrAmy, ZSA

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.1 alpha-amylase

Engineering

Engineering on EC 3.2.1.1 - alpha-amylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D231N
the specific activity for the mutant enzyme D233N is decreased by 6.3% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH
D233N
the specific activity for the mutant enzyme D233N is decreased by 84.8% compared to the wild type. D233N exhibits 56% increase in Km and 85.1% decrease in kcat, thermostability at 60°C, optimum temperature and optimum pH for D233N ae reduced to about 10°C and 3-4 units, respectively
D438G
the specific activity for the mutant enzyme D233N is decreased by 3.5% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH
I34H
-
mutation to corresponding residue of Bacillus licheniformis, complete loss of catalytic activity
P407H
-
mutation to corresponding residue of Bacillus licheniformis, leads to increase in thermostability without significant changes in kinetic parameters. Mutant displays a more rigid structure than wild-type
Q67H
-
mutation to corresponding residue of Bacillus licheniformis, leads to increase in thermostability without significant changes in kinetic parameters. Flexibility of mutant is increased compared to wild-type
V289D
-
the mutation results in complete loss of the alpha-amylase activity
V289E
-
the mutation results in complete loss of the alpha-amylase activity
V289F
-
the mutant shows 48.9% activity compared to the wild type enzyme
V289G
-
the mutant shows 14.5% activity compared to the wild type enzyme
V289I
-
the mutant shows 20% more hydrolytic activity than the wild type enzyme
V289L
-
the mutant shows 36.4% activity compared to the wild type enzyme
V289P
-
the mutant shows 2.2% activity compared to the wild type enzyme
V289R
-
the mutation results in complete loss of the alpha-amylase activity
V289S
-
the mutant shows 5% activity compared to the wild type enzyme
V289Y
-
the mutant shows 9.2% activity compared to the wild type enzyme, the mutant has acquired a transglycosylation activity, which results in the change of product profile of the reaction, giving a longer oligosaccharide
I34H
-
mutation to corresponding residue of Bacillus licheniformis, complete loss of catalytic activity
-
P407H
-
mutation to corresponding residue of Bacillus licheniformis, leads to increase in thermostability without significant changes in kinetic parameters. Mutant displays a more rigid structure than wild-type
-
Q67H
-
mutation to corresponding residue of Bacillus licheniformis, leads to increase in thermostability without significant changes in kinetic parameters. Flexibility of mutant is increased compared to wild-type
-
D231N
-
the specific activity for the mutant enzyme D233N is decreased by 6.3% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH
-
D233N
-
the specific activity for the mutant enzyme D233N is decreased by 84.8% compared to the wild type. D233N exhibits 56% increase in Km and 85.1% decrease in kcat, thermostability at 60°C, optimum temperature and optimum pH for D233N ae reduced to about 10°C and 3-4 units, respectively
-
D438G
-
the specific activity for the mutant enzyme D233N is decreased by 3.5% compared to the wild type. There are no significant changes in the Km value, thermostability, optimum temperature, and optimum pH
-
V289F
-
the mutant shows 48.9% activity compared to the wild type enzyme
-
V289G
-
the mutant shows 14.5% activity compared to the wild type enzyme
-
V289I
-
the mutant shows 20% more hydrolytic activity than the wild type enzyme
-
V289L
-
the mutant shows 36.4% activity compared to the wild type enzyme
-
V289Y
-
the mutant shows 9.2% activity compared to the wild type enzyme, the mutant has acquired a transglycosylation activity, which results in the change of product profile of the reaction, giving a longer oligosaccharide
-
A209V
more thermostable than wild type enzyme
H133Y
more thermostable than wild type enzyme
I157S/W193R
-
random mutagenesis, the mutant shows an altered pH profile compared to the wild-type enzyme
L134R
amyl, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. When the pH is 6.5, the kcat/Km is about 1.5times that of the mutants L134R, S320A, and L134R/S320A. In contrast, the kcat/Km of L134R and S320A are about 8.6- and 7.6times higher than that of the wild-type at pH 4.5. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
L134R/S320A
amyd, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. The highest kcat/Km with pH 4.5 approximately 14times that of the wild-type is observed in the double mutant. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
M15T/H133Y/N188S
at pH 83°C, pH 5.0, 5 mM CaCl2, 4fold longer half-life than wild-type enzyme
M15T/H133Y/N188S/A209V
at pH 83°C, pH 5.0, 5 mM CaCl2, 23fold longer half-life than wild-type enzyme
M15T/N188S
at pH 83°C, pH 5.0, 5 mM CaCl2, 1.5fold longer half-life than wild-type enzyme
M15T/N188S/A209V
at pH 83°C, pH 5.0, 5 mM CaCl2, 4.5fold longer half-life than wild-type enzyme
N172R/H156Y/A181T
-
the mutations increase the thermostability of alpha-amylase by 5fold
S320A
amy2, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. When the pH is 6.5, the kcat/Km is about 1.5times that of the mutants L134R, S320A, and L134R/S320A. In contrast, the kcat/Km of L134R and S320A are about 8.6- and 7.6times higher than that of the wild-type at pH 4.5. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
L134R
-
amyl, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. When the pH is 6.5, the kcat/Km is about 1.5times that of the mutants L134R, S320A, and L134R/S320A. In contrast, the kcat/Km of L134R and S320A are about 8.6- and 7.6times higher than that of the wild-type at pH 4.5. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
-
L134R/S320A
-
amyd, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. The highest kcat/Km with pH 4.5 approximately 14times that of the wild-type is observed in the double mutant. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
-
S320A
-
amy2, from recombinant Bacillus subtilis, when the pH is reduced from 6.5 to 4.5, compared with wild-type, Km increases but turnover number decreases, the mutants show an inverse trend, which results in catalytic efficiency (kcat/Km) increased. When the pH is 6.5, the kcat/Km is about 1.5times that of the mutants L134R, S320A, and L134R/S320A. In contrast, the kcat/Km of L134R and S320A are about 8.6- and 7.6times higher than that of the wild-type at pH 4.5. No significant difference on the kcat/Km of the mutants L134R, S320A, and L134R/S320A is shown when the pH is 5.5 and 6.5, respectively
-
I157S/W193R
-
random mutagenesis, the mutant shows an altered pH profile compared to the wild-type enzyme
-
E151A
-
mutant of N- and C-terminally truncated alpha-amylase, specific activity for E151A is decreased by more than 30%
E219
-
mutant of N- and C-terminally truncated alpha-amylase, decreased half-life at 70°C
E295A
-
mutant of N- and C-terminally truncated alpha-amylase, mutation results in a complete loss of enzyme activity
E295D
-
mutant of N- and C-terminally truncated alpha-amylase, mutation results in a complete loss of enzyme activity
H137L
-
no activity
H191L
-
similar activity as wild-type
H239L
-
similar activity as wild-type
H269L
-
no activity
H305L
-
similar activity as wild-type
H323L
-
approx. 50% of wild-type activity
H361L
-
no activity
H436L
-
approx. 40% of wild-type activity, reduced thermostability
H475L
-
similar activity as wild-type
M231L
-
construction of a thermostable variant BACDELTANC/DELTARS derived from the truncated alpha-amylase BACDELTANC, introduction of mutation M231L for enhancing the resistance towards chemical oxidation, and site-directed mutagenesis of the 483th codon in the gene to stop codon, resulting in the mutants BACDELTANC/DELTARS/M231L/DELTAC31. Mutants BACDELTANC/DELTARS/M231L and BACDELTANC/DELTARS/M231L/DELTAC31 are very similar to BACDELTANC in terms of specific activity, kinetic parameters, pH-activity profile, and the hydrolysis of raw starch, but the engineered enzymes show an increased half-life at 70°C
E151A
-
mutant of N- and C-terminally truncated alpha-amylase, specific activity for E151A is decreased by more than 30%
-
E219
-
mutant of N- and C-terminally truncated alpha-amylase, decreased half-life at 70°C
-
E295A
-
mutant of N- and C-terminally truncated alpha-amylase, mutation results in a complete loss of enzyme activity
-
E295D
-
mutant of N- and C-terminally truncated alpha-amylase, mutation results in a complete loss of enzyme activity
-
H137L
-
no activity
-
H191L
-
similar activity as wild-type
-
H239L
-
similar activity as wild-type
-
H305L
-
similar activity as wild-type
-
H323L
-
approx. 50% of wild-type activity
-
M231L
-
construction of a thermostable variant BACDELTANC/DELTARS derived from the truncated alpha-amylase BACDELTANC, introduction of mutation M231L for enhancing the resistance towards chemical oxidation, and site-directed mutagenesis of the 483th codon in the gene to stop codon, resulting in the mutants BACDELTANC/DELTARS/M231L/DELTAC31. Mutants BACDELTANC/DELTARS/M231L and BACDELTANC/DELTARS/M231L/DELTAC31 are very similar to BACDELTANC in terms of specific activity, kinetic parameters, pH-activity profile, and the hydrolysis of raw starch, but the engineered enzymes show an increased half-life at 70°C
-
H100I
increase in half-inactivation temperature, kcat value similar to wild-type
H100M/D144R
increase in half-inactivation temperature, 70% decrease in kcat value
L134R/S320A
-
the mutagenised protein is more acid resistant than the native protein. The optimum pH and stable range of pH with the mutagenised protein is 4.5 and 4.0 to 6.5, respectively, compared with pH 6.5 and 5.5 to 7.0 as the favorite pH and pH stability range of the native protein
N197C
decrease in half-inactivation temperature, kcat value similar to wild-type
T147P
increase in half-inactivation temperature, 25% decrease in kcat value
H100I
-
increase in half-inactivation temperature, kcat value similar to wild-type
-
H100M/D144R
-
increase in half-inactivation temperature, 70% decrease in kcat value
-
N197C
-
decrease in half-inactivation temperature, kcat value similar to wild-type
-
T147P
-
increase in half-inactivation temperature, 25% decrease in kcat value
-
L134R/S320A
-
the mutagenised protein is more acid resistant than the native protein. The optimum pH and stable range of pH with the mutagenised protein is 4.5 and 4.0 to 6.5, respectively, compared with pH 6.5 and 5.5 to 7.0 as the favorite pH and pH stability range of the native protein
-
D498N
site-directed mutagenesis, a catalytically inactive mutant, crystal structure determination and analysis
M197A
site-directed mutagenesis. Studies of its catalytic properties show no effect on the thermostability, pH activity/stability, calcium demand and chelator resistance. Specific activity is decreased from 1000 to 845 U/mg. The profile of starch hydrolysis is affected. As a result hereof AmyUS100DELTAIG/M197A produces in majority maltose and maltotriose as major products compared to maltohexaose and maltopentaose produced by the wild-type and the AmyUS100DELTAIG variant. The mutant retains 85% of its original activity. 70% of the mutantM197A activity is retained after 60 min of treatment at 60°C in the presence of 1.8 M H2O2, whereas AmyUS100DELTAIG is totally inactivated. These results confirm the importance of Met197 in the oxidative sensibility, situated in the cavity of the active site
DELTAAmyB
-
lacking the N-domain, with no significant difference between the rates of soluble starch degradation, indicating that the N-domain does not play a direct role in catalysis with this substrate. For insoluble starch AmyB shows increase binding compared with DELTAAmyB, suggesting that the N-domain enhances the ability of AmyB to bind this substrate. The temperature stability of AmyB and DELTAAmyB, lacking the N-domain are strongly influenced by NaCl concentration, shown by an increasing melting temperature with increased NaCl concentrations up to 4-4.5 M
D197A
-
no activity
D197N
-
no activity
D300A
-
0.0005% of wild-type starch hydrolyzing activity
D300N
-
0.0005% of wild-type starch hydrolyzing activity
E233A
-
0.005% of wild-type starch hydrolyzing activity
E233A/D300A
-
0.001% of wild-type starch hydrolyzing activity
E233Q
-
0.0005% of wild-type starch hydrolyzing activity
N298S
variant of the enzyme has an approximate 200fold reduction in affinity for chloride ion
W134A/W203A/Y276A/W284A/W316A/W388A
P04745
HSAmy-ar, multiple mutant, 10fold reduction of activity compared with wild-type enzyme and also sigificant reductaion of starch binding activity
W203A
P04745
2fold reduction of activity compared to the wild-type enzyme, similar starch-binding activity like the wild-type enzyme
W284A
P04745
similar specific activity and similar starch-binding activity like the wild-type enzyme
W316A/W388A
P04745
similar specific activity and similar starch-binding activity like the wild-type enzyme
W58L
-
reduced inhibitory efficiency of the mutants W58L and Y151M with 92 and 97% remaining enzyme activity at 0.00235 mM pentagalloyl glucose inhibitor concentration, respectively, pH 6.0, 37°C
Y151M
-
reduced inhibitory efficiency of the mutants W58L and Y151M with 92 and 97% remaining enzyme activity at 0.00235 mM pentagalloyl glucose inhibitor concentration, respectively, pH 6.0, 37°C
Y276/W284A
P04745
similar specific activity and similar starch-binding activity like the wild-type enzyme
Y276A
P04745
similar specific activity and similar starch-binding activity like the wild-type enzyme
H395A
located in the C-domain, the sugar tong, may be involved in the allosteric activation of the enzyme
S378P
kcat/KM for amylose is 1.2fold lower than wild-type value. kcat/KM for 2-chloro-4-nitrophenyl beta-D-maltoheptaoside is nearly identical to wild-type value
S378T
kcat/KM for amylose is 1.4fold lower than wild-type value. kcat/KM for 2-chloro-4-nitrophenyl beta-D-maltoheptaoside is nearly identical to wild-type value
T212P
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
T212W
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
T212Y
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
Y105A
Y105A/T212W
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
Y105A/T212Y
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
Y105A/Y380A
loss of 18-36% activity relative to wild-type
Y105A/Y380M
loss of 18-36% activity relative to wild-type
Y105F
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
Y105W
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
Y380A
Y380A/H395A
located in the C-domain, the sugar tong, may be involved in the allosteric activation of the enzyme
Y380F
kcat/KM for amylose is fold lowerthan wild-type value. kcat/KM for is 2.6fold lower than wild-type value. kcat/KM for 2-chloro-4-nitrophenyl beta-D-maltoheptaoside is 1.1fold higher than wild-type value
Y380M
N240Q
-
mutant of isoenzyme Amy1A
A53S
in comparison to the wild type, calcium ion has more effect on the catalytic efficiency, kcat/Km, and half-life (at 60°C) of A53S mutant, although the overall activity (kcat/Km) has not improved, about 80% of activity is maintained in the case of A53S mutant
H58I
calcium-independent mutant possessing high thermostability, in the absence of CaCl2, the H58I mutant is much more stable than the wild type and there is a 7fold increase in the residual activity of H58I mutant after 30 min of incubation as compared to the wild type
A53S
-
in comparison to the wild type, calcium ion has more effect on the catalytic efficiency, kcat/Km, and half-life (at 60°C) of A53S mutant, although the overall activity (kcat/Km) has not improved, about 80% of activity is maintained in the case of A53S mutant
-
H58I
-
calcium-independent mutant possessing high thermostability, in the absence of CaCl2, the H58I mutant is much more stable than the wild type and there is a 7fold increase in the residual activity of H58I mutant after 30 min of incubation as compared to the wild type
-
K300R
-
47% of wild-type kcat
K300R/N150D/V196F/Q164I/T232V
-
44% of wild-type kcat, increase in temperature stability
N150D
-
98% of wild-type kcat
Q164I
-
73% of wild-type kcat
T232V
-
105% of wild-type kcat
V196F
-
108% of wild-type kcat
H286A
site-directed mutagenesis, altered activity compared to wild-type
H286C
site-directed mutagenesis, altered activity compared to wild-type
H286D
site-directed mutagenesis, the mutant shows a decreased optimum pH compared to wild-type, altered activity compared to wild-type
H286E
site-directed mutagenesis, the mutant shows a 6.43fold increase in half-life at pH 4.5 and an decreased pH optimum compared to wild-type, altered activity compared to wild-type
H286F
site-directed mutagenesis, altered activity compared to wild-type
H286G
site-directed mutagenesis, altered activity compared to wild-type
H286I
site-directed mutagenesis, mutant H286I shows a 1.5fold increase in half-life at 55°C compared to wild-type, and the mutant shows an increased optimum temperature and a decreased pH optimum compared to wild-type, altered activity compared to wild-type
H286K
site-directed mutagenesis, altered activity compared to wild-type
H286L
site-directed mutagenesis, the mutant shows an increased optimum temperature and a decreased pH optimum compared to wild-type, the ability to form maltose from soluble starch is significantly improved, altered activity compared to wild-type
H286M
site-directed mutagenesis, the mutant shows an inproved ability to form maltose from soluble starch compared to wild-type, altered activity compared to wild-type
H286N
site-directed mutagenesis, altered activity compared to wild-type
H286P
site-directed mutagenesis, the mutant shows an increased optimum temperature compared to wild-type, altered activity compared to wild-type
H286Q
site-directed mutagenesis, altered activity compared to wild-type
H286R
site-directed mutagenesis, altered activity compared to wild-type
H286S
site-directed mutagenesis, the mutant shows an increased optimum temperature compared to wild-type, altered activity compared to wild-type
H286T
site-directed mutagenesis, the mutant shows an increased optimum temperature compared to wild-type, altered activity compared to wild-type
H286V
site-directed mutagenesis, altered activity compared to wild-type
H286W
site-directed mutagenesis, altered activity compared to wild-type
H286Y
site-directed mutagenesis, altered activity compared to wild-type
D325N
-
site-directed mutagenesis, inactive mutant
Y374A
-
site-directed mutagenesis, the mutant shows reduced activity, and altered substrate specificity and kinetics compared to the wild-type enzyme
D325N
-
site-directed mutagenesis, inactive mutant
-
Y374A
-
site-directed mutagenesis, the mutant shows reduced activity, and altered substrate specificity and kinetics compared to the wild-type enzyme
-
F179V
yield a similar product profile to that of the wild-type enzyme
H222D
show different product spectrum than wild-type, in addition small amounts of maltotriose are produced. When methanol and butanol are used as nucleophil instead of H2O, the mutant produces more methylglucoside and butylglucoside than wild-type, respectively
H222E
show different product spectrum than wild-type, in addition small amounts of maltotriose are produced. When methanol is used as nucleophil instead of H2O, more methylglucoside is produced than with wild-type enzyme. Butanol produces almost equal amount in both wild-type and H222E mutant
H222Q
show different product spectrum than wild-type, in addition small amounts of maltotriose are produced. When methanol and butanol are used as nucleophil instead of H2O, the mutant produces more methylglucoside and butylglucoside than wild-type, respectively
V259W
in addition to alpha-D-glucose and maltose the product profile is broadened with small amounts of maltotriose
W177V
yield a similar product profile to that of the wild-type enzyme
Y178V
yield a similar product profile to that of the wild-type enzyme
K205L
-
site-directed mutagenesis, the mutant shows a increased temperature optimum and an improved thermal stability compared to the wild-type enzyme
K209A
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209C
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209D
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209E
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209F
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209G
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209H
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site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209I
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site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209L
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209M
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209N
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209P
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209Q
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209R
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209S
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209T
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209V
-
site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209W
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site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
K209Y
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site-directed mutagenesis, the mutant shows a decreased temperature optimum and a lower thermal stability compared to the wild-type enzyme
Y187E
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site-directed mutagenesis, the mutant shows a increased temperature optimum and an improved thermal stability compared to the wild-type enzyme
Y187E/K205L
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site-directed mutagenesis, the mutant shows a increased temperature optimum and an improved thermal stability compared to the wild-type enzyme
additional information