3.2.1.41: pullulanase
This is an abbreviated version!
For detailed information about pullulanase, go to the full flat file.
Word Map on EC 3.2.1.41
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3.2.1.41
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starch
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pullulans
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glycogen
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klebsiella
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amylose
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maltotriose
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alpha-amylase
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isoamylase
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lariat
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glucoamylase
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amylolytic
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beta-amylase
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oxytoca
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cyclodextrins
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dextrinase
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amyloglucosidase
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alpha-1,6
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saccharification
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beta-cyclodextrins
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waxy
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maltodextrins
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aureobasidium
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glucanotransferase
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phytoglycogen
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maltotetraose
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aerobacter
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synthesis
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pilins
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thermoanaerobacterium
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branchpoints
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starch-based
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alpha-glucans
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malto-oligosaccharides
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starch-degrading
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maltohexaose
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anoxybacillus
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industry
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food industry
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degradation
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biotechnology
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thermoleovorans
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amylo-1,6-glucosidase
- 3.2.1.41
- starch
- pullulans
- glycogen
- klebsiella
- amylose
- maltotriose
- alpha-amylase
- isoamylase
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lariat
- glucoamylase
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amylolytic
- beta-amylase
- oxytoca
- cyclodextrins
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dextrinase
- amyloglucosidase
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alpha-1,6
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saccharification
- beta-cyclodextrins
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waxy
- maltodextrins
- aureobasidium
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glucanotransferase
- phytoglycogen
- maltotetraose
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aerobacter
- synthesis
- pilins
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thermoanaerobacterium
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branchpoints
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starch-based
- alpha-glucans
- malto-oligosaccharides
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starch-degrading
- maltohexaose
- anoxybacillus
- industry
- food industry
- degradation
- biotechnology
- thermoleovorans
- amylo-1,6-glucosidase
Reaction
Synonyms
1,4-alpha-D-glucan glucanohydrolase, Alpha-dextrin endo-1,6-alpha-glucosidase, amylase-pullulanase, amylopectin 6-glucanohydrolase, amylopullulanase, AmyX, Apu, ApuK885, ApuM957, Ask, BaPul13A, BDPulA324, BmPul, BNPulA324, CAC60157, debranching enzyme, EC 3.2.1.69, glucanohydrolase, amylopectin 6-, limit dextrinase, More, Nostoc punctiforme debranching enzyme, NPDE, PbPulA, Pcal-1616, PelBsp-PulA, PfAPU, Promozyme 200 L, PUL US105, Pul13A, Pul3YH5, PulA, PulASK, PulB, pulGT, Pullulan 6-glucanohydrolase, pullulan-6-glucanohydrolase, pullulanase, pullulanase type 1, pullulanase type I, pullulanase type II, PulWB42, R-enzyme, Saci_1162, TPApu, TTC1198, TTHpu, type II pullulanase, ZUP1
ECTree
3.2.1.41 pullulanaseAdvanced search results
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results (Engineering
Engineering on EC 3.2.1.41 - pullulanase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A90D
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
A90G
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
A90P
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
A90S
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
H5A
Anoxybacillus sp. WB42
mutant enzyme shows the same thermostability as wild-type enzyme. No activity with pullulan
H5A/R6A/T7A
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
L173D
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
M88D
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme. No activity with pullulan
Q87A
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
Q87A/L173D
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
Q87G
Anoxybacillus sp. WB42
mutant enzyme shows slight decrease in thermostability as compared to wild-type enzyme. No activity with pullulan
R6A
Anoxybacillus sp. WB42
mutant enzyme shows the same thermostability as wild-type enzyme. No activity with pullulan
R93A
Anoxybacillus sp. WB42
mutant enzyme shows slight decrease in thermostability as compared to wild-type enzyme, slight decrease in kcat/Km for pullulan
R93E
Anoxybacillus sp. WB42
mutant enzyme shows slight decrease in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
R93K
Anoxybacillus sp. WB42
mutant enzyme shows slight increase in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
R93T
Anoxybacillus sp. WB42
mutant enzyme shows slight increase in thermostability as compared to wild-type enzyme, slight decrease in kcat/Km for pullulan
T7A
Anoxybacillus sp. WB42
mutant enzyme shows the same thermostability as wild-type enzyme. No activity with pullulan
L627R
Ax203843.1
the pH optimum of the mutant enzyme shifts from 5.0 to 4.0, and its relative activity at pH 4.0 is 117% that of the wide-type enzyme. The L627R mutant exhibits increased tolerance against acid-mediated denaturation, and its maximum D-glucose content (97.4%) is obtained after 40 h incubation, which is shorter by 10 h compared with the time required by the wild-type enzyme to produce a comparable amount of the monosaccharide. The L627R mutant may be suitable for industrial application because its shortened reaction time translates to reduced energy consumption
D332H/D398Y
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mutant enzyme shows remarkable improvement of thermal stability in higher temperature range (above 55 °C). The best temperature of the relative activity moves to 60°C. The activity performance in the middle temperature range (40 to 55°C) is worse than that of the wild type pullulanase
D332H/D398Y/V390N
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the activity performance of mutations D332H/D398Y/V390N is better than that of mutations D332H/D398Y/V390S in all temperature range from 40°C to 65°C
D332H/D398Y/V390S
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the activity performance of the mutant enzyme is better than the wild pullulanase-BDPulA in all temperature range from 40°C to 65°C. In the temperature range lower than 55°C the activity is worse than mutation V390S alone, and in the temperature range higher than 55°C the activity of the mutant enzyme is worse than the mutation D332H/D398Y, but better than the wild type enzyme and V390S-mutated BDPulA
D787C
D787F
higher enzymatic activity than that of wild-type enzyme
D787N
higher enzymatic activity than that of wild-type enzyme
N680D
mutation shows positive effects for the hydrolysis reaction of pullulanase
N680D/T477N
mutation improves thermal stability, pH-sensitivity, and catalysis activity of pullulanase
T477N
mutation shows positive effects for the hydrolysis reaction of pullulanase
N680D
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mutation shows positive effects for the hydrolysis reaction of pullulanase
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N680D/T477N
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mutation improves thermal stability, pH-sensitivity, and catalysis activity of pullulanase
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T477N
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mutation shows positive effects for the hydrolysis reaction of pullulanase
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D394N
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kcat/KM is 24.2fold lower than wild-type value, specific activity on starch decreases 11.7times
E291Q
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kcat/KM is 123fold lower than wild-type value, specific activity on starch decreases 91times
E396Q
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activity of the mutant enzyme on pullulan is to low to allow reliable determination of catalytic efficiency, specific activity on starch decreases 37.2times
additional information
D787C
higher enzymatic activity than that of wild-type enzyme
D787C
the enzymatic activity and specific activity of D787C are 1.5fold higher than those of the wild-type. The enzyme shows a 1.8fold increase in kcat and a 1.7-fold increase in kcat/Km. It maintains higher activity compared with that of wild-type enzyme at temperatures over 60°C. Higher acid resistance than wild-type enzyme, maintaining 90% residual activity at pH 4.0
additional information
truncated form of enzyme, lacking first 252 amino acids, physicochemical properties almost identical to wild type enzyme
additional information
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truncated form of enzyme, lacking first 252 amino acids, physicochemical properties almost identical to wild type enzyme
additional information
EPZ37738
amino acids 362-370 of Ask are replaced with the corresponding sequence of type I pullulanase Pul-LM14-2 from Anoxybacillus sp. LM14-2. Unlike wild-type, the mutant enzyme forms reducing sugars on digesting starch
additional information
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amino acids 362-370 of Ask are replaced with the corresponding sequence of type I pullulanase Pul-LM14-2 from Anoxybacillus sp. LM14-2. Unlike wild-type, the mutant enzyme forms reducing sugars on digesting starch
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additional information
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construction of an amyX knockout strain and a glycogen overproducing glg strain with or without knockdown of amyX. The amyX glg strain accumulates significantly larger amounts of glycogen than the glg mutant, molecular masses of theglycogens, overview. Glycogen samples from the amyX glg strain exhibits average molecular masses two and three times larger, respectively, than that of glycogen from the glg mutant
additional information
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construction of an amyX knockout strain and a glycogen overproducing glg strain with or without knockdown of amyX. The amyX glg strain accumulates significantly larger amounts of glycogen than the glg mutant, molecular masses of theglycogens, overview. Glycogen samples from the amyX glg strain exhibits average molecular masses two and three times larger, respectively, than that of glycogen from the glg mutant
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additional information
different N-terminally domain truncated (730T) or spliced (730T-U1 and 730T-U2) mutants are constructed. Truncating the N-terminal 85 amino acids decreases the Km value and does not change its optimum pH. Wild-type enzyme can exhibit almost entirely soluble expression, but inclusion bodies are formed after truncating 85 amino acids from its N-terminus. This indicates that the N-terminal 85 amino acids of PulGT are responsible for ensuring secretory protein folding and maintaining its stability
additional information
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different N-terminally domain truncated (730T) or spliced (730T-U1 and 730T-U2) mutants are constructed. Truncating the N-terminal 85 amino acids decreases the Km value and does not change its optimum pH. Wild-type enzyme can exhibit almost entirely soluble expression, but inclusion bodies are formed after truncating 85 amino acids from its N-terminus. This indicates that the N-terminal 85 amino acids of PulGT are responsible for ensuring secretory protein folding and maintaining its stability
additional information
Geobacillus thermocatenulatus DSMZ730
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different N-terminally domain truncated (730T) or spliced (730T-U1 and 730T-U2) mutants are constructed. Truncating the N-terminal 85 amino acids decreases the Km value and does not change its optimum pH. Wild-type enzyme can exhibit almost entirely soluble expression, but inclusion bodies are formed after truncating 85 amino acids from its N-terminus. This indicates that the N-terminal 85 amino acids of PulGT are responsible for ensuring secretory protein folding and maintaining its stability
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additional information
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investigation of the function of pullulanase in starch biosynthesis using the mutant lines e10-/- and i16-/- containing the Tos17 insertion at exon 10 and intron 16 of the OsPUL gene, respectively, and EM1003, a product of N-methyl-N-nitrosourea mutagenesis, which mutated from C to T at 1266 bp before the start codon. Reduction of pullulanase activity has no effects on the other enzymes involved in starch biosynthesis. Short chains with a degree of polymerizytion below 14 are increased in the mutants compared with wild-type. The alpha-glucan composition and the structure of the starch components of the mutants is essentially the same, although the average chain length of the B2,3 chains of amylopectin in the mutants is about 3 residues longer than that of wild-type. Pullulanase fucntion may partially overlap with that of isoamylase 1
additional information
construction of GUS expressing transgenic rice lines by Agrobacterium tumefaciens transfection, overview
additional information
construction of GUS expressing transgenic rice lines by Agrobacterium tumefaciens transfection, overview
additional information
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construction of GUS expressing transgenic rice lines by Agrobacterium tumefaciens transfection, overview
additional information
the active hydrogen bond network is applied for engineering of pullulanase and improvement of thermal stability and pH-sensitivity of the enzyme
additional information
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the active hydrogen bond network is applied for engineering of pullulanase and improvement of thermal stability and pH-sensitivity of the enzyme
additional information
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the active hydrogen bond network is applied for engineering of pullulanase and improvement of thermal stability and pH-sensitivity of the enzyme
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additional information
parallel N- and C-terminal truncations facilitate purification. Catalytic properties of truncation construct Pul13A-N1/C1 are not impaired
