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3.2.1.3: glucan 1,4-alpha-glucosidase

This is an abbreviated version!
For detailed information about glucan 1,4-alpha-glucosidase, go to the full flat file.

Word Map on EC 3.2.1.3

Reaction

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

Synonyms

1,4-alpha-D-glucan glucohydrolase, 1,4-alpha-D-glucan-glucohydrolase, acid maltase, alpha-(1,4)-D-glucan glucohydrolase, alpha-1,4-D-glucan glucohydrolase, alpha-1,4-glucan glucohydrolase, AMG, AmyA, AmyC, AmyD, amyloglucosidase, AnGA, APGA1, AtriGA15A, exo-1,4-alpha-D-glucan glucanohydrolase, exo-1,4-alpha-D-glucanohydrolase, exo-1,4-alpha-glucosidase, exo-amylase, GA, GA A, GA1, GA2, GAI, GAII, GAM, GAM-1, GAM-2, gamma-amylase, GAMP, GHF15 glucoamylase, GLA, Gla1, GlaA, GLL1, Glu-1.1, Glu-A, Glu1, GlucaM, Glucan 1,4-alpha-glucosidase, glucoamylase, glucoamylase 1, glucoamylase 2, glucoamylase C, glucoamylase D, glucoamylase G1, glucoamylase GA15A, glucoamylase P, glucose amylase, GluR, glycoamylase, HjGA, HrGA, lysosomal alpha-glucosidase, maltase glucoamylase, maltase-glucoamylase, maltooligosaccharide-metabolizing enzyme, Meiotic expression upregulated protein 17, MGA, MGAM, More, PDE_05527, PoGA, PoGA15A, PoxGA15A, raw starch-degrading enzyme, raw starch-degrading glucoamylase, RSDE, RSDG, SBD, Sga1, SSG, Sta1, Sta1p, starch-digesting glucoamylase, TagA, tGA, TmGLA, TmGlu1, TtcGA

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.3 glucan 1,4-alpha-glucosidase

Engineering

Engineering on EC 3.2.1.3 - glucan 1,4-alpha-glucosidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A246C
A276C/S347C
101% of wild-type kcat
A276C/S347C/S298C
107% of wild-type kcat
C320A
-
barely improved thermostability or altered activity
D71N
-
increase in thermosability at 65 and 75°C
DELTA439-441
-
increase in thermosability at 65 and 75°C
E389M
104% of wild-type kcat
E400C
G127A/P128A
-
site-directed mutagenesis, the mutation decreases the enzyme thermostability compared to the wild-type protein
G137A
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
G139A
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
G183K
-
slight increase in activity as compared with the wild-type enzyme towards maltose. The mutation broadens the optimal pH range for activity towards acidic as well as alkaline conditions. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
G396A
90% of wild-type kcat
G396A/G407A
92% of wild-type kcat
G407A
96% of wild-type kcat
G447S
-
increase in thermosability at 65 and 75°C
H391M
89% of wild-type kcat
I136L
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
P128A
-
site-directed mutagenesis, the mutant destabilizes the enzyme
P128A/G139A/I136L
-
site-directed mutagenesis, mutations G139A and I136L, located in the center of alpha-helix, completely compensate for the destabilization caused by substitution P128A
P307A/T310V/Y312M/N313G
-
up to 15fold decreased turnover-number for alpha-1,4-linked substrates. Up to 9fold increase in Km-value for alpha-1,6-linked substrates
Q409P
-
increase in thermosability at 65 and 75°C
S119Y
-
slight increase in activity as compared with the wild-type enzyme towards maltose. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
S184H
-
slight increase in activity as compared with the wild-type enzyme towards maltose. The mutation broadens the optimal pH range for activity towards acidic as well as alkaline conditions. Selectivity of the mutant for alpha-1,4-linked disaccharides over alpha-1,6-linked disaccharides is enhanced 2.3fold to 3.5fold
S298C/L354C
104% of wild-type kcat
S386L
103% of wild-type kcat
S411A
-
54-74% of the catalytic efficiency of the wild type enzyme. Increased pH-optimum by 0.8 units for both maltose and maltoheptaose hydrolysis while maintaining a high level of activity and catalytic efficiency. In hydrolysis of 28% DE 10 maltodextrin, the mutant enzyme has a pH optimum of 7 compared with 5.6 for wild-type enzyme, and has higher initial rates of glucose production than wild-type enzyme at all pH values tested above pH 6.6
S411C
-
54-74% of the catalytic efficiency of the wild type enzyme
S411D
-
6-12% of the catalytic efficiency of the wild type enzyme
S411G
-
catalytic efficiency like that of wild type enzyme for isomaltose, maltose and maltoheptaose hydrolysis at pH 4.4
S411H
-
6-12% of the catalytic efficiency of the wild type enzyme
S418L
103% of wild-type kcat
S54P/T314A/H415Y
-
the mutant enzyme is more thermostable compared to the wild-type enzyme at 70°C. The mutation does not affect the protein secretion nor the production of the enzyme
T390L
101% of wild-type kcat
T416L
101% of wild-type kcat
V181T/N182Y/G183A
-
2fold increased Km-value for alpha-1,4-linked substrates: For alpha-1,6-linked substrates a 2fold increase in Km and a 3fold decrease in turnover-number
V181T/N182Y/G183A/P307A/T310V/Y312M/A313G
-
remarkably low Km-value for isomaltotriose through isomaltoheptaose and elevated turnover-number on isomaltose, resulting in an approximately 2fold improved catalytic effeciency
S54P/T314A/H415Y
-
the mutant enzyme is more thermostable compared to the wild-type enzyme at 70°C. The mutation does not affect the protein secretion nor the production of the enzyme
-
A246C
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
-
G137A
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
-
G139A
-
site-directed mutagenesis, the mutant has a strong additive thermostabilizing effect
-
P128A
-
site-directed mutagenesis, the mutant destabilizes the enzyme
-
D20C/A27C/S30P/G137A
-
site-directed mutagenesis, the mutant, designated THS8, is highly thermotolerant with increased stability at 80°C compared to the wild-type enzyme
E180Q
H391Y
-
random mutagenesis, the mutant shows increased thermotolerance compared to the wild-type enzyme
R54L
-
active site mutant. For inhibitor acarbose, a rapid binding event is apparently intersected by a slower secondary binding event. Mutant shows a dramatically higher Kd value for acarbose
T290A
-
random mutagenesis, the mutant shows increased thermotolerance compared to the wild-type enzyme
T62A
-
random mutagenesis, the mutant shows increased thermotolerance compared to the wild-type enzyme
W120F
-
mutant of G1, 3% of wild-type kcat for maltose, 2% of kcat for maltotriose
W317F
-
mutant of G1, 90% of wild-type kcat for maltose, 97% of kcat for maltotriose
W52F
-
mutant of G2, almost no activity with maltose and maltotriose
Y175F
-
mutation in subsite +3. Mutant displays only minor differences to wild-type in affinities to inhibitors acarbose and an acarbose conjugate
I339G
about 10% of wild-type specific activity
T47A
about 50% of wild-type specific activity
T47A/W48A
about 25% of wild-type specific activity
W48A
about 55% of wild-type specific activity
I339G
-
about 10% of wild-type specific activity
-
T47A
-
about 50% of wild-type specific activity
-
T47A/W48A
-
about 25% of wild-type specific activity
-
W48A
-
about 55% of wild-type specific activity
-
W47A
-
site-directed mutagenesis, the mutant shows altered kinetics and starch binding compared to the wild-type enzyme
Y32A
-
site-directed mutagenesis, the mutant shows altered kinetics and starch binding compared to the wild-type enzyme
Y32A/Y47A
-
site-directed mutagenesis, the mutant shows altered kinetics and starch binding compared to the wild-type enzyme
H447A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
H447A/D450A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
R15A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
T462A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
H447A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
H447A/D450A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
R15A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
T462A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
H447A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
H447A/D450A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
R15A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
T462A
-
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
-
W622C
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 87% reduced activity compared to the wild-type enzyme
W622D
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95% reduced activity compared to the wild-type enzyme
W622G
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95.7% reduced activity compared to the wild-type enzyme
W622H
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 48% reduced activity compared to the wild-type enzyme
W622S
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 83% reduced activity compared to the wild-type enzyme
W622C
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 87% reduced activity compared to the wild-type enzyme
-
W622D
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95% reduced activity compared to the wild-type enzyme
-
W622G
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 95.7% reduced activity compared to the wild-type enzyme
-
W622H
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 48% reduced activity compared to the wild-type enzyme
-
W622S
-
site-directed mutagenesis, the mutant enzyme shows slightly altered pH optimum and 83% reduced activity compared to the wild-type enzyme
-
additional information