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Information on EC 3.6.1.45 - UDP-sugar diphosphatase and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.45 UDP-sugar diphosphatase
IUBMB Comments
A divalent cation is required for activity. UDP-sugar is the best substrate, although other nucleoside-sugar diphosphates are used as substrates with similar Km values but much lower maximum velocities. Thus, this enzyme has a specificity distinct from that of ADP-sugar diphosphatase (EC 3.6.1.21). Some but not all enzymes of this class also appear to have 5'-nucleotidase (see EC 3.1.3.5) activity.
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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
toxin b, udp-sugar hydrolase, udp-glucose pyrophosphatase, ugppase, udp-sugar diphosphatase, udp-sugar pyrophosphatase, ushb protein, udpg pyrophosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolase, uridine diphosphoglucose (Escherichia coli precursor reduced)
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-
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hydrolase, uridine diphosphoglucose (Escherichia coli reduced)
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-
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hydrolase, uridine diphosphoglucose (Salmonella typhimurium clone pAGS5 gene ushB isoenzyme reduced)
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-
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hydrolase, uridine diphosphoglucose (Salmonella typhimurium gene ushA0 isoenzyme precursor reduced)
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-
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hydrolase, uridine diphosphoglucose (Salmonella typhimurium gene ushA0 isoenzyme reduced)
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-
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nucleosidediphosphate-sugar diphosphatase
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-
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nucleosidediphosphate-sugar pyrophosphatase
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-
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Nudix hydrolase-like nucleotide hydrolase
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UDP-glucose pyrophosphatase
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UDP-sugar diphosphatase
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-
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UDP-sugar hydrolase
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-
-
-
UDP-sugar pyrophosphatase
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-
-
-
UDPG pyrophosphatase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of diphosphate bonds
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-
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-
SYSTEMATIC NAME
IUBMB Comments
UDP-sugar sugarphosphohydrolase
A divalent cation is required for activity. UDP-sugar is the best substrate, although other nucleoside-sugar diphosphates are used as substrates with similar Km values but much lower maximum velocities. Thus, this enzyme has a specificity distinct from that of ADP-sugar diphosphatase (EC 3.6.1.21). Some but not all enzymes of this class also appear to have 5'-nucleotidase (see EC 3.1.3.5) activity.
CAS REGISTRY NUMBER
COMMENTARY hide
103716-25-2
-
103716-25-2
hydrolase, uridine diphosphoglucose (Escherichia coli precursor reduced)
103716-26-3
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103716-26-3
hydrolase, uridine diphosphoglucose (Escherichia coli reduced)
106528-92-1
hydrolase, uridine diphosphoglucose (Salmonella typhimurium gene ushA0 isoenzyme precursor reduced)
106528-93-2
hydrolase, uridine diphosphoglucose (Salmonella typhimurium gene ushA0 isoenzyme reduced)
127497-57-8
hydrolase, uridine diphosphoglucose (Salmonella typhimurium clone pAGS5 gene ushB isoenzyme reduced)
57127-20-5
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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
ADP-glucose + H2O
AMP + alpha-D-glucose 1-phosphate
show the reaction diagram
15% of the activity with UDP-glucose
-
-
?
ADP-ribose + H2O
AMP + alpha-D-ribose 1-phosphate
show the reaction diagram
best substrate, 130% of the activity with UDP-glucose
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-
?
CDP-glucose + H2O
CMP + alpha-D-glucose 1-phosphate
show the reaction diagram
3% of the activity with UDP-glucose
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-
?
GDP-glucose + H2O
GMP + alpha-D-glucose 1-phosphate
show the reaction diagram
10% of the activity with UDP-glucose
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-
?
UDP-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
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-glucose + H2O
UMP + alpha-D-glucose 1-phosphate
show the reaction diagram
hydrolysis of the precursor molecule of numerous glycosylation reactions in animals, to produce glucose 1-phosphate and UMP
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene UGPP
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NUD22_HUMAN
303
0
32580
Swiss-Prot
other Location (Reliability: 2)
NUD14_HUMAN
222
0
24118
Swiss-Prot
Mitochondrion (Reliability: 5)
B3KXY7_HUMAN
149
0
16369
TrEMBL
Mitochondrion (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from kineys by anion exchange chromatography, hydroxyapatite and again anion exchange chromatography, gel filtration, another different step of anion exchange and finally cation exchange chromatography followed by native PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene UGPP, overexpression in Escherichia coli strain AD494(DE3), subcloning in strain JM109
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yagi, T.; Baroja-Fernandez, E.; Yamamoto, R.; Munnoz, F.-J.; Akazawa, A.; Hong, K.S.; Pozueta-Romero, J.
Cloning, expression and characterization of a mammalian Nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose
Biochem. J.
370
409-415
2003
Sus scrofa, Homo sapiens (O95848), Homo sapiens
Manually annotated by BRENDA team