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Information on EC 3.1.3.7 - 3'(2'),5'-bisphosphate nucleotidase and Organism(s) Mus musculus and UniProt Accession Q9Z0S1

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.7 3'(2'),5'-bisphosphate nucleotidase
IUBMB Comments
Also acts on 3'-phosphoadenylyl sulfate, and on the corresponding 2'-phosphates.
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This record set is specific for:
Mus musculus
UNIPROT: Q9Z0S1
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
papase, pap phosphatase, bpnt1, rv2837c, fiery1, met22, 3'(2'),5'-bisphosphate nucleotidase, gpapp, bpnt-1, bpntase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bisphosphate 3'-nucleotidase 1
-
3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase
-
-
-
-
3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase
-
-
-
-
3'-phosphoadenosine 5'-phosphate 3'-phosphatase
-
3'-phosphoadenylylsulfate 3'-phosphatase
-
-
-
-
adenosine-3',5'-bisphosphate 3'-phosphohydrolase
-
-
-
-
DPNPase
-
-
-
-
Halotolerance protein tol1
-
-
-
-
nucleotidase, phosphoadenylate 3'-
-
-
-
-
PAP 3'-phosphatase
-
phosphoadenylate 3'-nucleotidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
adenosine-3'(2'),5'-bisphosphate 3'(2')-phosphohydrolase
Also acts on 3'-phosphoadenylyl sulfate, and on the corresponding 2'-phosphates.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-83-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
-
-
?
inositol 1,3,4-trisphosphate + H2O
inositol 3,4-bisphosphate + phosphate
show the reaction diagram
-
-
?
inositol 1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
show the reaction diagram
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
3'-phosphoadenosine 5'-phosphate 3'-phosphatase plays a role in the formation of skeletal elements derived through endochondral ossification
-
-
?
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
additional information
?
-
3'-phosphoadenosine 5'-phosphate 3'-phosphatase plays a role in the formation of skeletal elements derived through endochondral ossification
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
inositol 1,4-bisphosphate
-
Li+
inhibited by lithium in vitro
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000475 - 0.00052
adenosine 3',5'-bisphosphate
0.1
inositol 1,3,4-trisphosphate
-
0.113
inositol 1,4-bisphosphate
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.174
Li+
in 50 mM Bis-Tris (pH 6.5), 0.05 mM MnCl2, 100 mM KCl
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isoform Bpnt1 is most enriched in the enterocytes of the small intestine and the proximal tubule and thick ascending limb epithelia of the kidneys
Manually annotated by BRENDA team
isoform Bpnt1 is most enriched in the enterocytes of the small intestine and the proximal tubule and thick ascending limb epithelia of the kidneys
Manually annotated by BRENDA team
additional information
isoform Bpnt1 is expressed at relatively similar levels in a majority of tissues including the brain, heart, lungs, spleen, pancreas, stomach, liver, small intestine, colon, kidneys, and testes. Bpnt1 is most enriched in the enterocytes of the small intestine and the proximal tubule and thick ascending limb epithelia of the kidneys
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BPNT1_MOUSE
308
0
33196
Swiss-Prot
Mitochondrion (Reliability: 5)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Sf9 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
mice deficient for bisphosphate 3'-nucleotidase Bpnt1 do not exhibit skeletal defects but instead develop severe liver pathologies, including hypoproteinemia, hepatocellular damage, and in severe cases, frank whole body edema and death. These phenotypes are accompanied by tissue-specific elevations of the substrate 3?-phosphoadenosine 5'-phosphate, up to 50fold in liver, repressed translation, and aberrant nucleolar architecture. The phenotypes of the Bpnt1 knockout are rescued by generating a double mutant mouse deficient for both 3'-phosphoadenosine 5'-phosphate synthesis and hydrolysis, consistent with a mechanism in which 3'-phosphoadenosine 5'-phosphate accumulation is toxic to tissue function independent of sulfation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Spiegelberg, B.D.; Xiong, J.P.; Smith, J.J.; Gu, R.F.; York, J.D.
Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3-nucleotidase inhibited by inositol 1,4-bisphosphate
J. Biol. Chem.
274
13619-13628
1999
Homo sapiens (O95861), Homo sapiens, Mus musculus (Q9Z0S1), Mus musculus
Manually annotated by BRENDA team
Frederick, J.P.; Tafari, A.T.; Wu, S.M.; Megosh, L.C.; Chiou, S.T.; Irving, R.P.; York, J.D.
A role for a lithium-inhibited Golgi nucleotidase in skeletal development and sulfation
Proc. Natl. Acad. Sci. USA
105
11605-11612
2008
Mus musculus (Q80V26)
Manually annotated by BRENDA team
Hudson, B.H.; York, J.D.
Tissue-specific regulation of 3-nucleotide hydrolysis and nucleolar architecture
Adv. Biol. Regul.
54
208-213
2014
Mus musculus (Q9Z0S1)
Manually annotated by BRENDA team
Hudson, B.H.; Frederick, J.P.; Drake, L.Y.; Megosh, L.C.; Irving, R.P.; York, J.D.
Role for cytoplasmic nucleotide hydrolysis in hepatic function and protein synthesis
Proc. Natl. Acad. Sci. USA
110
5040-5045
2013
Mus musculus (Q9Z0S1), Mus musculus
Manually annotated by BRENDA team