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Information on EC 3.1.4.B4 - UDP-alpha-D-glucose glucohydrolase and Organism(s) Clostridioides difficile and UniProt Accession P16154

for references in articles please use BRENDA:EC3.1.4.B4
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.4 Phosphoric-diester hydrolases
                3.1.4.B4 UDP-alpha-D-glucose glucohydrolase
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Select one or more organisms in this record: ?
This record set is specific for:
Clostridioides difficile
UNIPROT: P16154
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Word Map
  • 3.1.4.B4
  • typhimurium
  • hydrolases
  • periplasmic
  • localisation
  • glucosylation
The taxonomic range for the selected organisms is: Clostridioides difficile
The enzyme appears in selected viruses and cellular organisms
Synonyms
udp-glucose hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-glucose hydrolase
-
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 + H2O
UDP + D-glucose
show the reaction diagram
toxin A transfers glucose to small GTPases. In the absence of target proteins, toxin A acts as hydrolase cleaving UDP-D-glucose to UDP and D-glucose
-
-
?
UDP-alpha-D-glucose + H2O
UDP + D-glucose
show the reaction diagram
additional information
?
-
no substrates: UDP-galactose, UDP-N-acetylglucosamine
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MgCl2
-
about 30% as effective as Mn2+ for both toxin A and toxin B
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
2 mM, complete loss of activity
sodium cholate
-
0.1%, complete loss of activity
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0894 - 0.1755
UDP-alpha-D-glucose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
inactive below
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
toxin A
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TCDA_CLODI
2710
0
308056
Swiss-Prot
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ciesla, W.P.; Bobak, D.A.
Clostridium difficile toxins A and B are cation-dependent UDP-glucose hydrolases with differing catalytic activities
J. Biol. Chem.
273
16021-16026
1998
Clostridioides difficile
Manually annotated by BRENDA team
Just, I.; Wilm, M.; Selzer, J.; Rex, G.; von Eichel-Streiber, C.; Mann, M.; Aktories, K.
The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins
J. Biol. Chem.
270
13932-13936
1995
Clostridioides difficile (P16154)
Manually annotated by BRENDA team
Genth, H.; Schelle, I.; Just, I.
Metal ion activation of Clostridium sordellii lethal toxin and Clostridium difficile toxin B
Toxins
8
109
2016
Clostridioides difficile (P18177), Paeniclostridium sordellii (V5T923)
Manually annotated by BRENDA team