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Information on EC 3.1.3.7 - 3'(2'),5'-bisphosphate nucleotidase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32179

for references in articles please use BRENDA:EC3.1.3.7
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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:
Saccharomyces cerevisiae
UNIPROT: P32179
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
papase, pap phosphatase, bpnt1, fiery1, rv2837c, met22, 3'(2'),5'-bisphosphate nucleotidase, gpapp, bpnt-1, bpntase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3',5'-bisphosphate nucleotidase
-
3’-phosphoadenosine-5’-phosphatase
-
Yeast 3',5'-bisphosphate nucleotidase
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3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase
-
-
-
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3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase
-
-
-
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3'-phosphoadenylylsulfate 3'-phosphatase
-
-
-
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adenosine-3',5'-bisphosphate 3'-phosphohydrolase
-
-
-
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DPNPase
-
-
-
-
Halotolerance protein tol1
-
-
-
-
nucleotidase, phosphoadenylate 3'-
-
-
-
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phosphoadenylate 3'-nucleotidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
show the reaction diagram
mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
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
3'-phosphoadenosine 5'-phosphate + H2
AMP + phosphate
show the reaction diagram
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
-
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
dependend on
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
competitive to Mg2+. Inhibition by Ca2+can be prevented by addition of Mg2+
Li+
mechanism of lithium inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00025
3'-phosphoadenosine 5'-phosphate
pH 8.0, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11
3'-phosphoadenosine 5'-phosphate
pH 8.0, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035
Ca2+
Saccharomyces cerevisiae
pH 8.0, temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray structure in complex with magnesium and with calcium ions
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
aqueous two-phase micellar system (ATPMS), as an alternative liquid-liquid extraction technique, is exploited for the precise separation or large-scale concentration of biomolecules. An affinity-based ATPMS composed of mixed micelles is constructed by introducing a copper-chelated Triton X-114 (TX-Cu(II)) into an aqueous solution of hydrophobically modified ethylene oxide polymer (HMEO). The phase diagram of the HM-EO/TX-Cu(II) system is measured, and the partitioning behavior of model proteins (YND, BSA, lysozyme) is studied by using this system. The addition of HM-EO can result in formation of the micellar network in the micelle-rich phase, making the phase separation easier and stabler. In addition, the extractive performance of ATPMS is enhanced due to the existence of the mixed micelles composed by HM-EO and Cu(II)-chelated TX. The recombinant His6-tagged enzyme YND from Escherichia coli strain BL21(DE3) is selectively extracted into the micelle-rich phase, while the histidine-poor proteins (BSA and lysozyme) remain in the micelle-poor phase. Enzyme YND can be recovered from the cell lysate with a recovery yield of 49.23% and purification factor of 2.63, method, overview. And purification of the His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
overexpression of the HAL2 gene in Saccharomyces cerevisiae
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
the enzyme as a potential target of lithium therapy
synthesis
construction of a protein expression vector using 3',5'-bisphosphate nucleotidase HAL2 in the presence of Ca2+ as an affinity tag. The tag can be used for procaryotic protein expression and purification by maintaining Ca2+ for efficient affinity binding and chelating Ca2+ for elution
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Murguia, J.R.; Belles, J.M.; Serrano, R.
A salt-sensitive 3 (2 ),5-bisphosphate nucleotidase involved in sulfate activation
Science
267
232-234
1995
Saccharomyces cerevisiae, Solanum lycopersicum
Manually annotated by BRENDA team
Patel, S.; Martinez-Ripoll, M.; Blundell, T.L.; Albert, A.
Structural enzymology of Li(+)-sensitive/Mg(2+)-dependent phosphatases
J. Mol. Biol.
320
1087-1094
2002
Saccharomyces cerevisiae (P32179)
Manually annotated by BRENDA team
Yang, Y.; Ma, J.; Yang, Y.; Zhang, X.; Wang, Y.; Yang, L.; Sun, M.
Yeast 3,5-bisphosphate nucleotidase: an affinity tag for protein purification
Protein Expr. Purif.
97
81-87
2014
Saccharomyces cerevisiae (P32179), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Liu, Y.; Sun, M.-H.; Shao, S.-K.; Deng, G.
An affinity-based aqueous two-phase mixed micellar system and its purification of yeast 3',5'-bisphosphate nucleotidase
J. Chromatogr. B
1060
215-220
2017
Saccharomyces cerevisiae (P32179), Saccharomyces cerevisiae
Manually annotated by BRENDA team