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.
Reaction
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
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Substrates Products
Substrates Products on EC 2.4.1.B62 - small GTPase glucosyltransferase
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REACTION DIAGRAM
UDP-alpha-D-glucose + Cdc42Hs
UDP + D-glucosyl-Cdc42Hs
-
-
-
?
UDP-alpha-D-glucose + K-Ras
UDP + D-glucosyl-K-Ras
good substrate
-
-
?
UDP-alpha-D-glucose + murine Rho GTPase
UDP + D-glucosyl-[murine Rho GTPase]
-
-
-
?
UDP-alpha-D-glucose + N-Ras
UDP + D-glucosyl-N-Ras
good substrate
-
-
?
UDP-alpha-D-glucose + RalC
UDP + D-glucosyl-RalC
good substrate
-
-
?
UDP-alpha-D-glucose + Ras GTPase
UDP + D-glucosyl-[Ras GTPase]
murine host substrate
-
-
?
UDP-alpha-D-glucose + RhoB
UDP + D-glucosyl-Rhob
-
-
-
?
UDP-alpha-D-glucose + RhoC
UDP + D-glucosyl-RhoC
-
-
-
?
UDP-alpha-D-glucose + RhoG
UDP + D-glucosyl-RhoG
-
-
-
?
UDP-alpha-D-glucose + TC10
UDP + D-glucosyl-TC10
good substrate
-
-
?
UDP-alpha-D-glucose + TCL signaling G protein
UDP + D-glucosyl-TCL signaling G protein
good substrate
-
-
?
UDP + D-glucosyl-[a small GTPase]
-
-
-
?
UDP-alpha-D-glucose + a small GTPase
UDP + D-glucosyl-[a small GTPase]
-
-
-
?
UDP-alpha-D-glucose + a small GTPase
UDP + D-glucosyl-[a small GTPase]
-
-
-
?
UDP-alpha-D-glucose + a small GTPase
UDP + D-glucosyl-[a small GTPase]
Clostridioides difficile 10463
-
-
-
?
UDP-alpha-D-glucose + a small GTPase
UDP + D-glucosyl-[a small GTPase]
-
-
-
?
UDP-alpha-D-glucose + a small GTPase
UDP + D-glucosyl-[a small GTPase]
-
-
-
-
?
UDP-alpha-D-glucose + a small GTPase
UDP + D-glucosyl-[a small GTPase]
-
-
-
?
UDP-alpha-D-glucose + a small GTPase
UDP + D-glucosyl-[a small GTPase]
-
-
-
?
UDP-alpha-D-glucose + a small GTPase
UDP + D-glucosyl-[a small GTPase]
Paeniclostridium sordellii JGS6382
-
-
-
?
UDP-alpha-D-glucose + Cdc42
UDP + D-glucosyl-Cdc42
-
-
-
?
UDP-alpha-D-glucose + Cdc42
UDP + D-glucosyl-Cdc42
-
-
-
?
UDP-alpha-D-glucose + Cdc42
UDP + D-glucosyl-Cdc42
-
-
-
?
UDP-alpha-D-glucose + H-Ras
UDP + D-glucosyl-H-Ras
good substrate
-
-
?
UDP-alpha-D-glucose + H-Ras
UDP + D-glucosyl-H-Ras
Ras is the exclusive substrate of the Ras subfamily of GTPases. Ras is a better substrate in the GTDP-bound form than in the GTP-bound form
-
-
?
UDP-alpha-D-glucose + H-Ras
UDP + D-glucosyl-H-Ras
Ras is the exclusive substrate of the Ras subfamily of GTPases. Ras is a better substrate in the GTDP-bound form than in the GTP-bound form
-
-
?
UDP-alpha-D-glucose + H-Ras
UDP + D-glucosyl-H-Ras
-
-
-
?
UDP-alpha-D-glucose + H-Ras
UDP + D-glucosyl-H-Ras
good substrate
-
-
?
UDP + D-glucosyl-[human Ras-GTPase]
activity of toxin A in human epithelial colorectal adenocarcinoma Caco-2 cells
-
-
?
UDP-alpha-D-glucose + human Ras-GTPase
UDP + D-glucosyl-[human Ras-GTPase]
Clostridioides difficile 10463
activity of toxin A in human epithelial colorectal adenocarcinoma Caco-2 cells
-
-
?
UDP-alpha-D-glucose + human Ras-GTPase
UDP + D-glucosyl-[human Ras-GTPase]
activity of toxin TcsL in human epithelial colorectal adenocarcinoma Caco-2 cells
-
-
?
UDP-alpha-D-glucose + human Ras-GTPase
UDP + D-glucosyl-[human Ras-GTPase]
activity of toxin TcsL in human epithelial colorectal adenocarcinoma Caco-2 cells
-
-
?
UDP + D-glucosyl-[Rac GTPase]
murine host substrate
-
-
?
UDP-alpha-D-glucose + Rac GTPase
UDP + D-glucosyl-[Rac GTPase]
Paeniclostridium sordellii JGS6382
murine host substrate
-
-
?
UDP-alpha-D-glucose + Rac1
UDP + D-glucosyl-Rac1
very good substrate
-
-
?
UDP-alpha-D-glucose + Rac1
UDP + D-glucosyl-Rac1
Rac is the exclusive substrate of the Rho subfamily of GTPases. Rac is a better substrate in the GTDP-bound form than in the GTP-bound form
-
-
?
UDP-alpha-D-glucose + Rac1
UDP + D-glucosyl-Rac1
Rac is the exclusive substrate of the Rho subfamily of GTPases. Rac is a better substrate in the GTDP-bound form than in the GTP-bound form
-
-
?
UDP-alpha-D-glucose + Rac1
UDP + D-glucosyl-Rac1
very good substrate
-
-
?
UDP + D-glucosyl-[Rac1 GTPase]
murine host substrate
-
-
?
UDP-alpha-D-glucose + Rac1 GTPase
UDP + D-glucosyl-[Rac1 GTPase]
Paeniclostridium sordellii JGS6382
murine host substrate
-
-
?
UDP + D-glucosyl-[Ral GTPase]
murine host substrate
-
-
?
UDP-alpha-D-glucose + Ral GTPase
UDP + D-glucosyl-[Ral GTPase]
Paeniclostridium sordellii JGS6382
murine host substrate
-
-
?
UDP + D-glucosyl-[Rap GTPase]
murine host substrate
-
-
?
UDP-alpha-D-glucose + Rap GTPase
UDP + D-glucosyl-[Rap GTPase]
Paeniclostridium sordellii JGS6382
murine host substrate
-
-
?
UDP + D-glucosyl-Rap2A
modification occurs in vitro and in cells
-
-
?
UDP-alpha-D-glucose + Rap2A
UDP + D-glucosyl-Rap2A
modification occurs in vitro and in cells
-
-
?
UDP-alpha-D-glucose + Rap2A
UDP + D-glucosyl-Rap2A
good substrate
-
-
?
UDP-alpha-D-glucose + Rap2A
UDP + D-glucosyl-Rap2A
good substrate
-
-
?
UDP-alpha-D-glucose + RhoA
UDP + D-glucosyl-RhoA
-
-
-
?
UDP-alpha-D-glucose + RhoA
UDP + D-glucosyl-RhoA
-
-
toxin B catalyses the incorporation of up to one mole of glucose per mole of RhoA at the amino acid threonine at position 37. UDP-glucose selectively serves as cosubstrate for the monoglucosylation reaction
-
?
UDP-alpha-D-glucose + RhoA
UDP + D-glucosyl-RhoA
-
-
-
?
UDP-alpha-D-glucose + RhoA
UDP + D-glucosyl-RhoA
no substrate for wild-type. Mutation S385/A387Q reverses the donor specificity of alpha-toxin from UDP-N-acetylglucosamine to UDP-glucose
-
-
?
UDP-alpha-D-glucose + RhoA
UDP + D-glucosyl-RhoA
no substrate for wild-type. Mutation S385/A387Q reverses the donor specificity of alpha-toxin from UDP-N-acetylglucosamine to UDP-glucose
-
-
?
UDP-alpha-D-glucose + RhoA
UDP + D-glucosyl-RhoA
-
-
-
?
UDP-alpha-D-glucose + RhoA
UDP + D-glucosyl-RhoA
-
-
-
?
UDP + N-acetyl-alpha-D-glucosamine-H-Ras
no substrate for wild-type, but substrate for mutant I383S/Q385A
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + H-Ras
UDP + N-acetyl-alpha-D-glucosamine-H-Ras
no substrate for wild-type, but substrate for mutant I383S/Q385A
-
-
?
UDP + N-acetyl-D-glucosamine-RhoA
wild-type shows negligible activity, mutant I383S/Q385A has catalytic activity on UDP-N-acetyl-D-glucosamine
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + RhoA
UDP + N-acetyl-D-glucosamine-RhoA
wild-type shows negligible activity, mutant I383S/Q385A has catalytic activity on UDP-N-acetyl-D-glucosamine
-
-
?
?
-
enzyme glucosylates and inactivates small GTPases of the Rho or Ras families, culminating in cytotoxicity
-
-
?
additional information
?
-
in the absence of target proteins toxin A acts as hydrolase cleaving UDP-D-glucose to UDP and D-glucose
-
-
?
additional information
?
-
UDP-alpha-D-glucose selectively serves as cosubstrate for toxin A-catalyzed modification. The acceptor amino acid of glucosylation is Thr37. Mutation of Thr37 to Ala completely abolishes glucosylation. No substrates: H-Ras, Rab5, and Arf1
-
-
?
additional information
?
-
Clostridioides difficile toxin B is not active on human Ras-GTPase in human epithelial colorectal adenocarcinoma Caco-2 cells
-
-
-
additional information
?
-
Clostridioides difficile toxin B is not active on human Ras-GTPase in human epithelial colorectal adenocarcinoma Caco-2 cells
-
-
-
additional information
?
-
-
Clostridioides difficile toxin B is not active on human Ras-GTPase in human epithelial colorectal adenocarcinoma Caco-2 cells
-
-
-
additional information
?
-
Clostridioides difficile 10463
Clostridioides difficile toxin B is not active on human Ras-GTPase in human epithelial colorectal adenocarcinoma Caco-2 cells
-
-
-
additional information
?
-
Clostridioides difficile 10463
Clostridioides difficile toxin B is not active on human Ras-GTPase in human epithelial colorectal adenocarcinoma Caco-2 cells
-
-
-
additional information
?
-
a circular electron transfer reaction is suggested tha does not directly involve any residues from the toxin. The transfer starts with the split of the glycosidic bond leading to the most stable transient state. The split increases the pK of the phosphoryl oxygen atom, facilitating deprotonation of the accepor, and provides space for the nucleophilic attack
-
-
?
additional information
?
-
a circular electron transfer reaction is suggested tha does not directly involve any residues from the toxin. The transfer starts with the split of the glycosidic bond leading to the most stable transient state. The split increases the pK of the phosphoryl oxygen atom, facilitating deprotonation of the accepor, and provides space for the nucleophilic attack
-
-
?
additional information
?
-
lethal toxin from Clostridium sordellii is a glucosyltransferase, which uses UDP-glucose as cosubstrate to modify low molecular mass GTPases. Lethal toxin selectively modifies Rac and Ras. In Rac, acceptor amino acid is residue threonine 35. No substrates: Rho, Cdc42, Rab, Arf
-
-
?
additional information
?
-
full-length hemorrhagic toxin TcsH exclusively glucosylates Rho-GTPases. The recombinant transferase domain glucosylates preferably Rho-GTPases but also Ras-GTPases to some extent. Vero cells treated with full length TcsH also show glucosylation of Ras, albeit to a lower extent than of Rho-GTPases
-
-
?
additional information
?
-
full-length hemorrhagic toxin TcsH exclusively glucosylates Rho-GTPases. The recombinant transferase domain glucosylates preferably Rho-GTPases but also Ras-GTPases to some extent. Vero cells treated with full length TcsH also show glucosylation of Ras, albeit to a lower extent than of Rho-GTPases
-
-
?
additional information
?
-
-
full-length hemorrhagic toxin TcsH exclusively glucosylates Rho-GTPases. The recombinant transferase domain glucosylates preferably Rho-GTPases but also Ras-GTPases to some extent. Vero cells treated with full length TcsH also show glucosylation of Ras, albeit to a lower extent than of Rho-GTPases
-
-
?
additional information
?
-
lethal toxin from Clostridium sordellii is a glucosyltransferase, which uses UDP-glucose as cosubstrate to modify low molecular mass GTPases. Lethal toxin selectively modifies Rac and Ras. In Rac, acceptor amino acid is residue threonine 35. No substrates: Rho, Cdc42, Rab, Arf
-
-
?
additional information
?
-
full-length hemorrhagic toxin TcsH exclusively glucosylates Rho-GTPases. The recombinant transferase domain glucosylates preferably Rho-GTPases but also Ras-GTPases to some extent. Vero cells treated with full length TcsH also show glucosylation of Ras, albeit to a lower extent than of Rho-GTPases
-
-
?
additional information
?
-
full-length hemorrhagic toxin TcsH exclusively glucosylates Rho-GTPases. The recombinant transferase domain glucosylates preferably Rho-GTPases but also Ras-GTPases to some extent. Vero cells treated with full length TcsH also show glucosylation of Ras, albeit to a lower extent than of Rho-GTPases
-
-
?