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3.2.1.11: dextranase

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

Word Map on EC 3.2.1.11

Reaction

Dextran
+
H2O
=
dextran fragment 1
+
dextran fragment 2

Synonyms

1,6-alpha-D-glucan-6-glucanohydrolase, 6-alpha-D-glucan 6-glucanohydrolase, alpha-1,6-D-glucan 6-glucanohydrolase, alpha-1,6-D-glucan-6-glucanohydrolase, Alpha-1,6-glucan-6-glucanohydrolase, alpha-D-1,6-glucan-6-glucanohydrolase, alpha-dextranase, alpha-glucanase, AODex, Dex, Dex2, Dex410, Dex49A, DexA, dextran hydrolase, dextranase, dextranase DL 2, dextranase I, dextranase II, Dextranase Plus L, dextransucrase, DL 2, DXSR, endo-dextranase, endodextranase, extracellular dextranase, Fjoh_4430, LSD1, More, rDex, SmDex, Teth39_0264, TLDex, TPDex

ECTree

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

Engineering

Engineering on EC 3.2.1.11 - dextranase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D279C/S289C
T245C/N248C
-
the mutant shows a more than 3°C improvement on its optimal temperature compared to the wild type enzyme
D1252N
-
about 40% of wild-type activtiy
D1254N
36% of wild-type activity
D189A
application of achemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms small sized dextran from alpha-isomaltotetraosyl fluoride in the presence of NaN3
D189N
-
complete loss of activity
D340G
application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms beta-isomaltotetraosyl azide indicating residue D340 as nucleophile catalyst
D340N
-
complete loss of activity
E412Q
D1254N
-
36% of wild-type activity
-
D189A
-
application of achemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms small sized dextran from alpha-isomaltotetraosyl fluoride in the presence of NaN3
-
D340G
-
application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms beta-isomaltotetraosyl azide indicating residue D340 as nucleophile catalyst
-
E412Q
-
application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms alpha-isomaltotetraosyl azide indicating residue E412 as acid/base catalyst
-
A356F
the mutant exhibits improved thermostability compared to the wild type enzyme
G355F
the mutant exhibits improved thermostability compared to the wild type enzyme
S354F
the mutant exhibits improved thermostability compared to the wild type enzyme
S357F
the mutant exhibits improved thermostability compared to the wild type enzyme
S357F/G355F
the mutant exhibits improved thermostability compared to the wild type enzyme
A356F
-
the mutant exhibits improved thermostability compared to the wild type enzyme
-
G355F
-
the mutant exhibits improved thermostability compared to the wild type enzyme
-
S354F
-
the mutant exhibits improved thermostability compared to the wild type enzyme
-
S357F
-
the mutant exhibits improved thermostability compared to the wild type enzyme
-
S357F/G355F
-
the mutant exhibits improved thermostability compared to the wild type enzyme
-
D453E
loss of dextranase activity
W793L
loss of dextranase activity
D453E
-
loss of dextranase activity
-
W793L
-
loss of dextranase activity
-
D380N
-
similar activity as wild-type
D385E
-
no activity
D385N
-
no activity
D385T
-
no activity
D385V
-
no activity
D389N
-
similar activity as wild-type
T558H
the mutation affects the hydrolytic activities of the enzyme. The mutant increases the proportion of isomaltooligosaccharide with degrees of polymerization of 5 in hydrolysates following reactions with 4 mg/ml dextran
T563N
the mutation affects the hydrolytic activities of the enzyme
W279A
the mutation affects the hydrolytic activities of the enzyme
W279A/T563N
the mutations affect the hydrolytic activities of the enzyme
W279F
the mutation affects the hydrolytic activities of the enzyme
W279F/T563N
the mutations affect the hydrolytic activities of the enzyme
T558H
-
the mutation affects the hydrolytic activities of the enzyme. The mutant increases the proportion of isomaltooligosaccharide with degrees of polymerization of 5 in hydrolysates following reactions with 4 mg/ml dextran
-
W279A
-
the mutation affects the hydrolytic activities of the enzyme
-
W279A/T563N
-
the mutations affect the hydrolytic activities of the enzyme
-
W279F
-
the mutation affects the hydrolytic activities of the enzyme
-
W279F/T563N
-
the mutations affect the hydrolytic activities of the enzyme
-
N5A/N537A/N540A
glycosylation-free mutant of Dex49A
D312G
additional information