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2.4.1.248: cycloisomaltooligosaccharide glucanotransferase

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

Word Map on EC 2.4.1.248

Reaction

cyclizes part of a (1->6)-alpha-D-glucan chain by formation of a (1->6)-alpha-D-glucosidic bond =

Synonyms

cit, CITase, CITase-598K, CITase-T3040, isocyclomaltooligosaccharide glucanotransferase

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.248 cycloisomaltooligosaccharide glucanotransferase

Engineering

Engineering on EC 2.4.1.248 - cycloisomaltooligosaccharide glucanotransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A452N
-
3fold increase in reaction velocity, 9fold increase in Km value. Activation by Ca2+ and inactivation by Cu2+ are reduced
F268V/D469Y/A513V/Y515S
mutant produces three times as much megalo-cycloisomaltooligosaccharides (10-12 glucose units) and 1.5 times as much total cycloisomaltooligosaccharides (7-12 glucose units) as compared with the wild-type. The modified product size specificity is attributable to the construction of novel substrate-binding sites in the B-2 substrate-binding site and reactivity is improved by mutation on subsite -3 on the catalytic domain
V744L
-
2fold increase in reaction velocity, 3fold increase in Km value. Activation by Ca2+ and inactivation by Cu2+ are reduced
A452N
-
3fold increase in reaction velocity, 9fold increase in Km value. Activation by Ca2+ and inactivation by Cu2+ are reduced
-
F268V/D469Y/A513V/Y515S
-
mutant produces three times as much megalo-cycloisomaltooligosaccharides (10-12 glucose units) and 1.5 times as much total cycloisomaltooligosaccharides (7-12 glucose units) as compared with the wild-type. The modified product size specificity is attributable to the construction of novel substrate-binding sites in the B-2 substrate-binding site and reactivity is improved by mutation on subsite -3 on the catalytic domain
-
V744L
-
2fold increase in reaction velocity, 3fold increase in Km value. Activation by Ca2+ and inactivation by Cu2+ are reduced
-
D144A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D144N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D264A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D269A
site-directed mutagenesis, the mutant is inactive
D269N
site-directed mutagenesis, the mutant is almost inactive
D662A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E341A
site-directed mutagenesis, the mutant is inactive
E341Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information