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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

Reaction

(Glcalpha(1-4)Glcalpha(1-4)Glcalpha(1-6))n
+
H2O
=
alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose
 +
(Glcalpha(1-4)Glcalpha(1-4)Glcalpha(1-6))n-1

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 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.41 pullulanase

Temperature Stability

Temperature Stability on EC 3.2.1.41 - pullulanase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105
-
2 h, about 80% loss of activity
30 - 60
EPZ37738
20 min, stable
42
stable
45
thermal denaturing half-lives: 253 min
50 - 70
-
irreversible inactivation of free pullulanase, 92.51% and 82.52% of maximal activity at 55°C and 60°C, respectively, rapid decrease at 70°C
52
melting temperature
65
1 h, residual activity is more than 90%
65.8
T50, mutant enzyme Q87G
66.4
T50, mutant enzyme R93A, mutant enzyme R93E, mutant enzyme A90G
66.6
T50, wild-type enzyme, mutant enzyme H5A, mutant enzyme R6A
66.8
T50, mutant enzyme R93K, mutant enzyme R93T, mutant enzyme R93T
67
T50, mutant enzyme A90P, mutant enzyme A90D
68.2
T50, mutant enzyme H5A/R6A/T7A
68.4
T50, mutant enzyme M88D
69
T50, mutant enzyme Q87A, T50, mutant enzyme L173D, mutant enzyme Q87A/L173D
69.4
T50, mutant enzyme A90S
80 - 110
the pullulanase shows 96%, 91%, 70%, and 50% of the maximum activity at 80, 90, 100 and 110°C, respectively. The residual total activities of the amylopullulanase-MalE fusion protein and the hydrolytic domain of the amylopullulanase are both 89% after incubation at 100°C for 1 h
90 - 95
40 h, stable
95
-
after 30 min, pH 5.5, no loss of activity
98
-
8 h, about 60% loss of activity
additional information