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2.4.1.B62: small GTPase glucosyltransferase

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

Word Map on EC 2.4.1.B62

Reaction

UDP-alpha-D-glucose
+
a small GTPase
=
UDP
+
D-glucosyl-[a small GTPase]

Synonyms

Clostridium sordellii lethal toxin, cytotoxin B, cytotoxin L, glucosyltransferase TcdA, glucosyltransferase TcdB, haemorrhagic toxin, hemorrhagic toxin, letal toxin, lethal toxin, lethal-toxin, TcdA, TcdB, TcsH, TcsL, toxA, ToxB, toxin, toxin A, toxin B

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.B62 small GTPase glucosyltransferase

Engineering

Engineering on EC 2.4.1.B62 - small GTPase glucosyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C698A
mutant is able to glucosylate Rac protein but does not display cytotoxicity. Mutant does not show autocatalytical activity
D587N
mutant is able to glucosylate Rac protein but does not display cytotoxicity. Mutant does not show autocatalytical activity
H653A
mutant is able to glucosylate Rac protein but does not display cytotoxicity. Mutant does not show autocatalytical activity
I383S
mutation in toxin B, 67% of wild-type catalytic efficiency with substrate UDP-alpha-D-glucose
I383S/Q385A
mutation in toxin B, 23% of wild-type catalytic efficiency with substrate UDP-alpha-D-glucose. Mutation largely increases the acceptance of UDP-Nacetylglucosamine as a sugar donor for modification of RhoA
Q385A
mutation in toxin B, 58% of wild-type catalytic efficiency with substrate UDP-alpha-D-glucose
I383S
-
mutation in toxin B, 67% of wild-type catalytic efficiency with substrate UDP-alpha-D-glucose
-
I383S/Q385A
-
mutation in toxin B, 23% of wild-type catalytic efficiency with substrate UDP-alpha-D-glucose. Mutation largely increases the acceptance of UDP-Nacetylglucosamine as a sugar donor for modification of RhoA
-
Q385A
-
mutation in toxin B, 58% of wild-type catalytic efficiency with substrate UDP-alpha-D-glucose
-
S385/A387Q
C698A
site-directed mutagenesis of the autoprocessing domain, mutant TcsL C698A is able to quickly glucosylate Rac1, similar to wild-type TcsL, but is attenuated in its ability to glucosylate Ras GTPases. The introduction of the autoprocessing mutation does not impact the glucosylation of Rac1 or H-Ras in an in vitro assay
F17K
mutation strongly decreases binding to brain phosphatidylserine
F17N/R18A
site-directed mutagenesis in the GTD membrane localization domain, on the surface of the membrane localization domain (MLD), the mutant shows a defect in membrane association in a liposome binding assay
F17N/R18A/C698A
site-directed mutagenesis in the GTD membrane localization domain, on the surface of the membrane localization domain (MLD), the mutant shows a defect in membrane association in a liposome binding assay. The triple mutant is also inhibited in both Rac1 and Ras glucosylation
I383S/Q385A
mutation allow modification of Ras in the presence of UDP-N-acetyl-glucosamine and reduces the acceptance of UDP-glucose as a donor for glycosylation
K11I
mutation moderately decreases binding to brain phosphatidylserine
K16I
mutation moderately decreases binding to brain phosphatidylserine
Q10A
mutation does not significantly decrease binding to brain phosphatidylserine
Q20A
mutation moderately decreases binding to brain phosphatidylserine
R18P
mutation strongly decreases binding to brain phosphatidylserine
R68A
mutation strongly decreases binding to brain phosphatidylserine
S38A
mutation does not significantly decrease binding to brain phosphatidylserine
V15S
mutation strongly decreases binding to brain phosphatidylserine
Y14A
mutation strongly decreases binding to brain phosphatidylserine
Y78A
mutation does not significantly decrease binding to brain phosphatidylserine
I383S/Q385A
-
mutation allow modification of Ras in the presence of UDP-N-acetyl-glucosamine and reduces the acceptance of UDP-glucose as a donor for glycosylation
-
C698A
-
site-directed mutagenesis of the autoprocessing domain, mutant TcsL C698A is able to quickly glucosylate Rac1, similar to wild-type TcsL, but is attenuated in its ability to glucosylate Ras GTPases. The introduction of the autoprocessing mutation does not impact the glucosylation of Rac1 or H-Ras in an in vitro assay
-
F17N/R18A
-
site-directed mutagenesis in the GTD membrane localization domain, on the surface of the membrane localization domain (MLD), the mutant shows a defect in membrane association in a liposome binding assay
-
F17N/R18A/C698A
-
site-directed mutagenesis in the GTD membrane localization domain, on the surface of the membrane localization domain (MLD), the mutant shows a defect in membrane association in a liposome binding assay. The triple mutant is also inhibited in both Rac1 and Ras glucosylation
-
additional information