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Information on EC 2.4.1.B62 - small GTPase glucosyltransferase and Organism(s) Clostridium novyi and UniProt Accession Q46149

for references in articles please use BRENDA:EC2.4.1.B62
preliminary BRENDA-supplied EC number
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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.B62 small GTPase glucosyltransferase
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This record set is specific for:
Clostridium novyi
UNIPROT: Q46149 not found.
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The taxonomic range for the selected organisms is: Clostridium novyi
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
a small GTPase
=
+
D-glucosyl-[a small GTPase]
Synonyms
hemorrhagic toxin, clostridium sordellii lethal toxin, haemorrhagic toxin, lethal-toxin, glucosyltransferase tcdb, more
SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:small GTPase glucosyltransferase
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + RhoA
UDP + D-glucosyl-RhoA
show the reaction diagram
no substrate for wild-type. Mutation S385/A387Q reverses the donor specificity of alpha-toxin from UDP-N-acetylglucosamine to UDP-glucose
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-
?
additional information
?
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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
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + RhoA
UDP + D-glucosyl-RhoA
show the reaction diagram
no substrate for wild-type. Mutation S385/A387Q reverses the donor specificity of alpha-toxin from UDP-N-acetylglucosamine to UDP-glucose
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
UDP-alpha-D-glucose
mutant S385/A387Q, pH 7.5, 37┬░C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.39
UDP-alpha-D-glucose
mutant S385/A387Q, pH 7.5, 37┬░C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
91.7
UDP-alpha-D-glucose
mutant S385/A387Q, pH 7.5, 37┬░C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TCDA_CLONO
2178
0
250136
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
63992
x * 63992, catalytic fragment, residues 1-551
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 63992, catalytic fragment, residues 1-551
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic fragment, residues 1-551 to 2.85 A resolution. Geometry suggests that the reaction runs as a circular electron transfer in a six-membered ring, which involves the deprotonation of the nucleophile by the beta-phosphoryl group of the donor substrate UDP-glucose
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S385/A387Q
mutation reverses the donor specificity of alpha-toxin from UDP-N-acetylglucosamine to UDP-glucose
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of catalytic fragment, residues 1-551
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jank, T.; Reinert, D.; Giesemann, T.; Schulz, G.; Aktories, K.
Change of the donor substrate specificity of Clostridium difficile toxin B by site-directed mutagenesis
J. Biol. Chem.
280
37833-37838
2005
Clostridioides difficile (P18177), Clostridioides difficile, Clostridioides difficile VPI 10463 (P18177), Clostridium novyi (Q46149), Clostridium novyi, Clostridium novyi 19402 (Q46149), Paeniclostridium sordellii (Q46342), Paeniclostridium sordellii, Paeniclostridium sordellii 6018 (Q46342)
Manually annotated by BRENDA team
Ziegler, M.O.; Jank, T.; Aktories, K.; Schulz, G.E.
Conformational changes and reaction of clostridial glycosylating toxins
J. Mol. Biol.
377
1346-1356
2007
Clostridium novyi (Q46149), Paeniclostridium sordellii (Q46342)
Manually annotated by BRENDA team
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