Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.2.1.135: neopullulanase

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

Word Map on EC 3.2.1.135

Reaction

pullulan
+
H2O
=
panose

Synonyms

Amo105, amylopullalanase, amylopullulanase, ApuA, ApuADELTA, bsNpl, cyclomaltodextrinase, Env Npu193A, More, neopullulanase-alpha-amylase, neopullulanase-like enzyme, Pul, pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose), pullulan hydrolase type I, pullulanase, pullulanase II, pullulanase, neo-, Rbamy5, TetApuM955, TetApuR855, type II pullulanase, type III pullulan hydrolase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.135 neopullulanase

Engineering

Engineering on EC 3.2.1.135 - neopullulanase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A416I
t1/2 of mutant enzyme at 70°C is 17 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
A566L
t1/2 of mutant enzyme at 70°C is 27 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
D328H
-
site-directed mutagenesis, inactive mutant
D328N
-
site-directed mutagenesis, inactive mutant
D424H
-
site-directed mutagenesis, inactive mutant
D424N
-
site-directed mutagenesis, inactive mutant
D46E
t1/2 of mutant enzyme at 70°C is 100 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
E357H
-
site-directed mutagenesis, inactive mutant
E357Q
-
site-directed mutagenesis, inactive mutant
I358V
-
mutation decreases the preference for alpha(1-6)-branched oligosaccharides and pullulan as substrates
I358W
-
mutation reduces the acceptability of alpha(1-6)-branched oligo- and polysaccharides
M375L
-
mutation increases transglycosylation activity in comparison to wild-type enzyme
N413Q
t1/2 of mutant enzyme at 70°C is 32 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
S407T
t1/2 of mutant enzyme at 70°C is 66 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
S422V
-
mutation increases transglycosylation activity in comparison to wild-type enzyme
V239L
t1/2 of mutant enzyme at 70°C is 103 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
V374I
t1/2 of mutant enzyme at 70°C is 14 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
V404L
t1/2 of mutant enzyme at 70°C is 191 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
V533L
t1/2 of mutant enzyme at 70°C is 8 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity
Y377D
-
mutation decreases transglycosylation activity in comparison to wild-type enzyme
Y377F
-
mutation increases transglycosylation activity in comparison to wild-type enzyme
Y377S
-
mutation decreases transglycosylation activity in comparison to wild-type enzyme
I358V
-
mutation decreases the preference for alpha(1-6)-branched oligosaccharides and pullulan as substrates
-
I358W
-
mutation reduces the acceptability of alpha(1-6)-branched oligo- and polysaccharides
-
M375L
-
mutation increases transglycosylation activity in comparison to wild-type enzyme
-
S422V
-
mutation increases transglycosylation activity in comparison to wild-type enzyme
-
Y377F
-
mutation increases transglycosylation activity in comparison to wild-type enzyme
-
I358V
-
site-directed mutagenesis, the mutant shows increased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme
I358W
-
site-directed mutagenesis, the mutant shows decreased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme
I358V
-
site-directed mutagenesis, the mutant shows increased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme
-
I358W
-
site-directed mutagenesis, the mutant shows decreased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme
-
additional information