Information on EC 3.1.3.7 - 3'(2'),5'-bisphosphate nucleotidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.1.3.7
-
RECOMMENDED NAME
GeneOntology No.
3'(2'),5'-bisphosphate nucleotidase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
show the reaction diagram
-
-
-
-
adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Sulfur metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
adenosine-3'(2'),5'-bisphosphate 3'(2')-phosphohydrolase
Also acts on 3'-phosphoadenylyl sulfate, and on the corresponding 2'-phosphates.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3'(2'),5'-bisphosphate nucleotidase
-
3'(2'),5'-bisphosphate nucleotidase
gene FIERY1, dual enzymatic activity: inositol polyphosphate-1-phosphatase
3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase
-
-
-
-
3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase
-
-
-
-
3'(2')-phosphoadenosine 5-phosphate phosphatase
-
3'-PAPase
-
-
3'-phosphoadenosine 5'-phosphate 3'-phosphatase
-
-
3'-phosphoadenosine 5'-phosphate phosphatase
-
-
3'-phosphoadenosine-5'-phosphatase
-
3'-phosphoadenosine-5'-phosphatase
-
-
3'-phosphoadenylylsulfate 3'-phosphatase
-
-
-
-
3(2),5-bisphosphate nucleotidase
-
3(2),5-bisphosphate nucleotidase
-
-
3-phosphoadenosine 5-phosphate phosphatase
-
-
3-phosphoadenosine-5-phosphatase
-
3-phosphoadenosine-5-phosphatase
-
-
3-phosphoesterase
-
adenosine-3',5'-bisphosphate 3'-phosphohydrolase
-
-
-
-
bisphosphate 3'-nucleotidase
-
-
bisphosphate 3'-nucleotidase 1
-
BPNT1
-
-
Cv1693
Chromobacterium violaceum DSM 30191
-
-
CysQ
-
exhibits also NADP(H) phosphatase and fructose-1,6-bisphosphatase activities
DPNPase
-
-
-
-
GhHL1
Gossypium hirsutum CRI 12
-
-
gPAPP
-
-
Halotolerance protein tol1
-
-
-
-
nucleotidase, phosphoadenylate 3'-
-
-
-
-
PAP 3'-phosphatase
-
-
PAP-phosphatease
-
phosphoadenylate 3'-nucleotidase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9025-83-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GenBank U40433
-
-
Manually annotated by BRENDA team
formerly known as Arthrospira platensis
UniProt
Manually annotated by BRENDA team
Chromobacterium violaceum DSM 30191
-
UniProt
Manually annotated by BRENDA team
Gossypium hirsutum CRI 12
-
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GenBank AF125042
SwissProt
Manually annotated by BRENDA team
recombinantly expressed in yeast
Uniprot
Manually annotated by BRENDA team
GenBank AF125043
Uniprot
Manually annotated by BRENDA team
GenBank U33283
Uniprot
Manually annotated by BRENDA team
KP767, KP812, KP656, KP801, KP803
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
overexpression of GhHL1 complements yeast hal2 mutant and enhances yeast growth under elevated NaCl or LiCl, showing a role in salt tolerance associated with ionic stress response
physiological function
-
while cytoplasmic bisphosphate nucleotidase Bpnt1 is widely expressed in a majority of tissues, in Bpnt1 knockout mice only the liver, duodenum, and kidneys show high levels of its substrate 3'-phosphoadenosine 5'-phosphate and nucleolar reorganization
physiological function
-
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
physiological function
Gossypium hirsutum CRI 12
-
overexpression of GhHL1 complements yeast hal2 mutant and enhances yeast growth under elevated NaCl or LiCl, showing a role in salt tolerance associated with ionic stress response
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-AMP + H2O
?
show the reaction diagram
-
10% relative activity compared to NADP+
-
-
?
2'-deoxyadenosine 3',5'-bisphosphate + H2O
2'-deoxyadenosine 5'-phosphate + phosphate
show the reaction diagram
Chromobacterium violaceum, Chromobacterium violaceum DSM 30191
-
-
?
2'-deoxycytidine 3',5'-bisphosphate + H2O
2'-deoxycytidine 5'-phosphate + phosphate
show the reaction diagram
Chromobacterium violaceum, Chromobacterium violaceum DSM 30191
-
-
?
2'-deoxyguanosine 3',5'-bisphosphate + H2O
2'-deoxyguanosine 5'-phosphate + phosphate
show the reaction diagram
-
-
?
2'-deoxythymidine 3',5'-bisphosphate + H2O
2'-deoxythymidine 5'-phosphate + phosphate
show the reaction diagram
-
-
?
2'-deoxyuridine 3',5'-bisphosphate + H2O
2'-deoxyuridine 5'-phosphate + phosphate
show the reaction diagram
-
-
?
3'-AMP + H2O
?
show the reaction diagram
-
84% relative activity compared to NADP+
-
-
?
3'-phosphoadenosine 5'-phosphate + H2
AMP + phosphate
show the reaction diagram
-
-
-
?
3'-phosphoadenosine 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
show the reaction diagram
-
-
?
3'-phosphoadenosine 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
show the reaction diagram
67% enzyme activity in comparison to 3'-phosphoadenosine 5'-phosphate as substrate
-
?
5'-phosphoadenylyl-(3'->5')-adenosine + H2O
? + phosphate
show the reaction diagram
-
-
?
adenosine 2',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 2',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 2',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 2',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 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
100% in comparison to 3'-phosphoadenosine 5'-phosphate as substrate
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
only 6% enzyme activity in comparison to 3'-phosphoadenosine 5'-phosphate as substrate
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
-
829% relative activity compared to NADP+
-
?
adenosine 3',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',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',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',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',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',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',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',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',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',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
best substrate
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
100% activity
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
the activity of enzyme is required while 3'-phosphoadenosine 5'-phosphate is a potent inhibitor of a variety of enzymes that use 3'-phosphoadenosine 5'-phosphate as cosubstrate
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
-
607% relative activity compared to NADP+
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
Gossypium hirsutum CRI 12
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
best substrate
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
Chromobacterium violaceum DSM 30191
-
-
?
adenosine 3',5'-bisphosphate sulfate + H2O
adenosine 5'-phosphate sulfate + phosphate
show the reaction diagram
Gossypium hirsutum, Gossypium hirsutum CRI 12
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
show the reaction diagram
-
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
show the reaction diagram
-
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
show the reaction diagram
-
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
show the reaction diagram
-
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
show the reaction diagram
-
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
show the reaction diagram
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
show the reaction diagram
42% activity compared to adenosine 3',5'bisphosphate
-
?
CoA + H2O
?
show the reaction diagram
-
-
-
-
?
cytosine 3',5'-bisphosphate + H2O
cytosine 5'-phosphate + phosphate
show the reaction diagram
-
-
?
D-fructose 1,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
?
show the reaction diagram
-
122% relative activity compared to NADP+
-
-
?
D-fructose 1,6-bisphosphate + H2O
?
show the reaction diagram
-
-
-
?
D-myo-inositol 2-phosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
9% relative activity compared to NADP+
-
?
D-myo-inositol monophosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
-
?
D-myo-inositol monophosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
13% relative activity compared to NADP+
-
?
D-myo-inositol monophosphate + H2O
D-myo-inositol + phosphate
show the reaction diagram
-
-
?
D-myo-inositol-1,4,5-trisphosphate + H2O
?
show the reaction diagram
-
14% relative activity compared to NADP+
-
-
?
D-myo-inositol-1,4-bisphosphate + H2O
?
show the reaction diagram
-
485% relative activity compared to NADP+
-
-
?
guanosine 2',5'-bisphosphate + H2O
guanosine 2'-phosphate + phosphate
show the reaction diagram
-
-
-
?
guanosine 3',5'-bisphosphate + H2O
guanosine 5'-phosphate + phosphate
show the reaction diagram
-
-
-
?
guanosine 3',5'-bisphosphate + H2O
guanosine 5'-phosphate + phosphate
show the reaction diagram
Chromobacterium violaceum, Chromobacterium violaceum DSM 30191
-
-
?
inositol 1,3,4-trisphosphate + H2O
inositol 3,4-bisphosphate + phosphate
show the reaction diagram
-
-
?
inositol 1,3,4-trisphosphate + H2O
inositol 3,4-bisphosphate + phosphate
show the reaction diagram
-
-
-
?
inositol 1,3,4-trisphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
inositol 1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
show the reaction diagram
-
-
?
inositol 1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
show the reaction diagram
-
-
-
?
inositol 1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
show the reaction diagram
-
-
-
?
inositol 1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
show the reaction diagram
-
-
?
inositol-1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
show the reaction diagram
-
-
?
N6-methyl-5'-phosphoadenylyl-(3'->5')-adenosine + H2O
? + phosphate
show the reaction diagram
-
-
?
NADP+ + H2O
NAD+ + phosphate
show the reaction diagram
-
100% activity
-
?
NADPH + H2O
NADH + phosphate
show the reaction diagram
-
145% relative activity compared to NADP+
-
?
p-nitrophenyl phosphate
p-nitrophenol + phosphate
show the reaction diagram
-
21% relative activity compared to NADP+
-
?
thymidine 3',5'-bisphosphate + H2O
thymidine 5'-phosphate + phosphate
show the reaction diagram
-
-
?
uridine 3',5'-bisphosphate + H2O
uridine 5'-phosphate + phosphate
show the reaction diagram
-
-
?
inositol-1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
show the reaction diagram
5.6% activity compared to adenosine 3',5'bisphosphate
-
?
additional information
?
-
not: 3-AMP, ATP, NADP, O-phospho-L-serine, phosphoglycolic acid, L-histidinol phosphate
-
-
?
additional information
?
-
adenosine 3',5'-bisphosphate is not the primary substrate, the enzyme may be important for response to salt stress
-
-
-
additional information
?
-
the enzyme mediates lithium toxicity effects
-
-
-
additional information
?
-
-
glycerol phosphate, D-glucose-1-phosphate, D-glucose-6-phosphate, D-fructose-1-phosphate, D-fructose 1,6-bisphosphate, D-fructose-6-phosphate, ADP, 5'-AMP, ATP, NAD+, NMN+, bis-p-nitrophenol phosphate are no substrates
-
-
-
additional information
?
-
3'-phosphoadenosine 5'-phosphate 3'-phosphatase plays a role in the formation of skeletal elements derived through endochondral ossification
-
-
-
additional information
?
-
GhHL1 protein efficiently hydrolyzes 3'(2'),5'-bisphosphate nucleotide and 3'(2'),5'-bisphosphate nucleotide sulfate, at 128% of 3'(2'),5'-bisphosphate nucleotide levels, but has low or no activity with other tested compounds including 3'-AMP, 5'-AMP, or ADP. Purified recombinant GhHL1 protein dephosphorylates both 3',5'-bisphosphate nucleotide and inositol 1,4-bisphosphate, demonstrating dual 3',5'-bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase activities, substrate specificity, overview
-
-
-
additional information
?
-
enzyme is promiscuous and is able to hydrolyze several 3',5'-bisphosphonucleotides such as pGp, pCp, pUp, and pIp, and 2'-deoxynucleotides with comparable catalytic efficiency. In addition, it is capable of hydrolyzing short oligonucleotides such as (pdA)5, albeit at rates much lower than that of adenosine 3',5'-bisphosphate
-
-
-
additional information
?
-
Gossypium hirsutum CRI 12
GhHL1 protein efficiently hydrolyzes 3'(2'),5'-bisphosphate nucleotide and 3'(2'),5'-bisphosphate nucleotide sulfate, at 128% of 3'(2'),5'-bisphosphate nucleotide levels, but has low or no activity with other tested compounds including 3'-AMP, 5'-AMP, or ADP. Purified recombinant GhHL1 protein dephosphorylates both 3',5'-bisphosphate nucleotide and inositol 1,4-bisphosphate, demonstrating dual 3',5'-bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase activities, substrate specificity, overview
-
-
-
additional information
?
-
Chromobacterium violaceum DSM 30191
enzyme is promiscuous and is able to hydrolyze several 3',5'-bisphosphonucleotides such as pGp, pCp, pUp, and pIp, and 2'-deoxynucleotides with comparable catalytic efficiency. In addition, it is capable of hydrolyzing short oligonucleotides such as (pdA)5, albeit at rates much lower than that of adenosine 3',5'-bisphosphate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
show the reaction diagram
O95861
the activity of enzyme is required while 3'-phosphoadenosine 5'-phosphate is a potent inhibitor of a variety of enzymes that use 3'-phosphoadenosine 5'-phosphate as cosubstrate
-
?
additional information
?
-
P0C5A3
adenosine 3',5'-bisphosphate is not the primary substrate, the enzyme may be important for response to salt stress
-
-
-
additional information
?
-
Q9NX62
the enzyme mediates lithium toxicity effects
-
-
-
additional information
?
-
Q80V26
3'-phosphoadenosine 5'-phosphate 3'-phosphatase plays a role in the formation of skeletal elements derived through endochondral ossification
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
activates slightly
Mg2+
required, optimal concentration of 1 mM
Mg2+
required
Mg2+
the activity increases over increasing concentrations of Mg2+ to reach its optimal values in the presence of 2 to 2.5 mM Mg2+
Mg2+
-
in the presence of 10 mM MgCl2, CysQ shows maximum activities of 3'-PAPase and NADP(H)ase at pH 6.4 and pH 8.0, respectively
Mg2+
required for activity, optimal activity observed between pH 8.5 and pH 9.5, using 0.5 mM Mg2+
Mg2+
dependent on, optimal at 2 mM
Mg2+
-
activates
Mg2+
activates; dependend on
Mg2+
-
strict requirement
Mg2+
-
dependend on
Mn2+
enzyme has a trinuclear metal center in the active site with three Mn2+ ions
additional information
GhHL1 is Mg2+-dependent and cation-sensitive
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 5'-phosphosulfate
-
slight
adenosine-3',5'-bisphosphate
-
inhibition at high concentration
Ca2+
-
competitive to Mg2+. Inhibition by Ca2+can be prevented by addition of Mg2+
Ca2+
-
in presence of Mg2+
dithiothreitol
-
slight
inositol 1,4-bisphosphate
-
inositol 1,4-bisphosphate
-
Li+
-
mechanism of lithium inhibition
Li+
inhibited by lithium in vitro
Mg2+
-
activity is decreased to approximately 70% in the presence of 10 mM MgCl2
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0102
2'-deoxyadenosine 3',5'-bisphosphate
pH 7.5, 3C
-
0.026
2'-deoxycytidine 3',5'-bisphosphate
pH 7.5, 3C
-
0.0052
2'-deoxyguanosine 3',5'-bisphosphate
pH 7.5, 3C
-
0.022
2'-deoxythymidine 3',5'-bisphosphate
pH 7.5, 3C
-
0.029
2'-deoxyuridine 3',5'-bisphosphate
pH 7.5, 3C
-
0.00025
3'-phosphoadenosine 5'-phosphate
-
pH 8.0, temperature not specified in the publication
41.5
5'-ADP
in 50 mM Tris (pH 8.0), 2 mM MgCl2, at 30C
0.0016
5'-phosphoadenylyl-(3'->5')-adenosine
pH 7.5, 3C
-
0.007
adenosine 2',5'-bisphosphate
-
-
0.14
adenosine 2',5'-bisphosphate
-
in 10 mM HEPES pH 7.0
0.000475
adenosine 3',5'-bisphosphate
native enzyme
0.00052
adenosine 3',5'-bisphosphate
recombinant enzyme
0.001
adenosine 3',5'-bisphosphate
pH 7.5, 30C
0.0015
adenosine 3',5'-bisphosphate
pH 7.5, 3C
0.0081
adenosine 3',5'-bisphosphate
in 50 mM Tris buffer, pH 8.5, 0.5 mM Mg2+
0.01
adenosine 3',5'-bisphosphate
-
-
0.01704
adenosine 3',5'-bisphosphate
-
wild type enzyme, in 50 mM Tris-MES, pH 7.5, 0.5 mM magnesium acetate for 30 min at 30C
0.02646
adenosine 3',5'-bisphosphate
-
mutant enzyme E301K, in 50 mM Tris-MES, pH 7.5, 0.5 mM magnesium acetate for 30 min at 30C
0.033
adenosine 3',5'-bisphosphate
pH 8.1, 30C
0.07299
adenosine 3',5'-bisphosphate
-
mutant enzyme V131A, in 50 mM Tris-MES, pH 7.5, 0.5 mM magnesium acetate for 30 min at 30C
0.126
adenosine 3',5'-bisphosphate
pH 8.1, 30C
0.24
adenosine 3',5'-bisphosphate
-
in 10 mM HEPES pH 7.0
0.24
adenosine 3',5'-bisphosphate
-
-
1.03
adenosine 3',5'-bisphosphate
in 50 mM Tris (pH 8.0), 2 mM MgCl2, at 30C
0.1
adenosine 3'-phosphate 5'-phosphosulfate
-
0.25
adenosine 3'-phosphate 5'-phosphosulfate
-
-
0.61
adenosine 3'-phosphate 5'-phosphosulfate
in 50 mM Tris (pH 8.0), 2 mM MgCl2, at 30C
0.014
cytosine 3',5'-bisphosphate
pH 7.5, 3C
-
0.566
D-fructose 1,6-bisphosphate
in 50 mM Tris buffer, pH 8.5, 0.5 mM Mg2+
1.17
D-fructose 1,6-bisphosphate
-
in 10 mM HEPES pH 7.0
7.11
D-myo-inositol monophosphate
in 50 mM Tris buffer, pH 8.5, 0.5 mM Mg2+
0.2
Guanosine 2',5'-bisphosphate
-
-
0.0173
guanosine 3',5'-bisphosphate
pH 7.5, 3C
0.25
guanosine-3',5'-bisphosphate
-
-
0.1
inositol 1,3,4-trisphosphate
-
0.077
inositol 1,4-bisphosphate
-
pH 7.8, 30C
0.09
inositol 1,4-bisphosphate
-
-
0.113
inositol 1,4-bisphosphate
-
0.0004
inositol-1,4-bisphosphate
pH 7.5, 30C
0.0054
N6-methyl-5'-phosphoadenylyl-(3'->5')-adenosine
pH 7.5, 3C
-
2.7
NADP+
-
in 10 mM HEPES pH 7.0
2.13
NADPH
-
in 10 mM HEPES pH 7.0
0.0093
thymidine 3',5'-bisphosphate
pH 7.5, 3C
0.0088
uridine 3',5'-bisphosphate
pH 7.5, 3C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.1
2'-deoxyadenosine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
-
9.4
2'-deoxycytidine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
-
4.2
2'-deoxyguanosine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
-
4.3
2'-deoxythymidine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
-
5.2
2'-deoxyuridine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
-
11
3'-phosphoadenosine 5'-phosphate
Saccharomyces cerevisiae
-
pH 8.0, temperature not specified in the publication
0.05
5'-phosphoadenylyl-(3'->5')-adenosine
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
-
13.2
adenosine 2',5'-bisphosphate
Escherichia coli
-
in 10 mM HEPES pH 7.0
0.069
adenosine 3',5'-bisphosphate
Debaryomyces hansenii
-
mutant enzyme E301K, in 50 mM Tris-MES, pH 7.5, 0.5 mM magnesium acetate for 30 min at 30C
1.465
adenosine 3',5'-bisphosphate
Debaryomyces hansenii
-
mutant enzyme V131A, in 50 mM Tris-MES, pH 7.5, 0.5 mM magnesium acetate for 30 min at 30C
1.921
adenosine 3',5'-bisphosphate
Debaryomyces hansenii
-
wild type enzyme, in 50 mM Tris-MES, pH 7.5, 0.5 mM magnesium acetate for 30 min at 30C
2.94
adenosine 3',5'-bisphosphate
Debaryomyces hansenii
-
wild type enzyme, in 50 mM Tris-MES, pH 7.5, 0.5 mM magnesium acetate for 30 min at 30C
5.4
adenosine 3',5'-bisphosphate
Mycobacterium tuberculosis
P9WKJ1
in 50 mM Tris buffer, pH 8.5, 0.5 mM Mg2+
6.08
adenosine 3',5'-bisphosphate
Debaryomyces hansenii
-
mutant enzyme V131A, in 50 mM Tris-MES, pH 7.5, 0.5 mM magnesium acetate for 30 min at 30C
11.4
adenosine 3',5'-bisphosphate
Escherichia coli
-
in 10 mM HEPES pH 7.0
22
adenosine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
8.6
cytosine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
-
0.24
D-fructose 1,6-bisphosphate
Mycobacterium tuberculosis
P9WKJ1
in 50 mM Tris buffer, pH 8.5, 0.5 mM Mg2+
1.1
D-fructose 1,6-bisphosphate
Escherichia coli
-
in 10 mM HEPES pH 7.0
0.31
D-myo-inositol monophosphate
Mycobacterium tuberculosis
P9WKJ1
in 50 mM Tris buffer, pH 8.5, 0.5 mM Mg2+
12.3
guanosine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
11.6
N6-methyl-5'-phosphoadenylyl-(3'->5')-adenosine
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
-
0.7
NADP+
Escherichia coli
-
in 10 mM HEPES pH 7.0
1.45
NADPH
Escherichia coli
-
in 10 mM HEPES pH 7.0
3.3
thymidine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
5.4
uridine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
700
2'-deoxyadenosine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
197727
360
2'-deoxycytidine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
197729
790
2'-deoxyguanosine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
197730
190
2'-deoxythymidine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
197733
180
2'-deoxyuridine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
197732
32
5'-phosphoadenylyl-(3'->5')-adenosine
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
197734
1400
adenosine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
68
620
cytosine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
197728
710
guanosine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
93572
2100
N6-methyl-5'-phosphoadenylyl-(3'->5')-adenosine
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
197735
360
thymidine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
103683
610
uridine 3',5'-bisphosphate
Chromobacterium violaceum
Q7NXD4
pH 7.5, 3C
197731
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
Ca2+
pH 8.1, 30C
0.35
Ca2+
pH 8.1, 30C
140
K+
pH 8.1, 30C
0.174
Li+
in 50 mM Bis-Tris (pH 6.5), 0.05 mM MnCl2, 100 mM KCl
0.3
Li+
pH 7.5, 30C, substrate: adenosine 3,5-bisphosphate
0.6
Li+
pH 7.5, 30C, substrate: inositol-1,4-bisphosphate
1.6
Li+
pH 8.1, 30C
20
Li+
pH 8.1, 30C
160
Na+
pH 8.1, 30C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.035
Ca2+
Saccharomyces cerevisiae
-
pH 8.0, temperature not specified in the publication
2.4
Li+
Debaryomyces hansenii
-
wild type enzyme, in 50 mM Tris-MES, pH 7.5, 0.5 mM magnesium acetate for 30 min at 30C
3.6
Li+
Arthrospira platensis
Q3LS17
in 50 mM Tris (pH 8.0), 2 mM MgCl2, at 30C
0.05
LiCl
Escherichia coli
-
using adenosine 3',5'-bisphosphate as a substrate
0.15
LiCl
Escherichia coli
-
using adenosine 2',5'-bisphosphate as a substrate
180
Na+
Debaryomyces hansenii
-
wild type enzyme, in 50 mM Tris-MES, pH 7.5, 0.5 mM magnesium acetate for 30 min at 30C
600
Na+
Arthrospira platensis
Q3LS17
in 50 mM Tris (pH 8.0), 2 mM MgCl2, at 30C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
activity range, highest activity in the pH range from pH 7.0 to pH 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 75
highest activity at 30-65C, low activity at below 10C, and 28.9% of maximal activity at 75C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
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
GeneOntology No.
LITERATURE
SOURCE
-
bound to. Stress markedly influences the accumulation of the membrane-bound enzyme form in the cell. The N-terminal hydrophobic region is necessary for the synthesis of the membrane-bound isoform
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
-
652120
28000
-
SDS-PAGE
677696
30000
SDS-PAGE
696267
33000
SDS-PAGE
651264
38000
-
gel filtration
81107
40000
-
-
651657
40000
-
652120
41800
SDS-PAGE
677661
44000
-
membrane-bound enzyme form
668452
44000
calculation from sequence of cDNA
81105
375000
-
calculation from sequence of cDNA
81104
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 37000, recombinant enzyme, SDS-PAGE
?
x * 47000, SDS-PAGE
?
Gossypium hirsutum CRI 12
-
x * 37000, recombinant enzyme, SDS-PAGE
-
monomer
-
1 * 38000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 1.9 resolution, with AMP and orthophosphate bound in the active site. The enzyme has a trinuclear metal center in the active site with three Mn2+ ions. It belongs to the Cluster of Orthologous Groups cog0613 from the polymerase and histidinol phosphatase family of enzymes
X-ray structure in complex with magnesium and with calcium ions
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
the 3'-PAPase activity is decreased to approximately 50% at pH 8.0
677696
10
remained 60% of maximal activity when the pH of the reaction sample is increased to pH 10
677661
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel affinity chromatography
partial, copurification with other enzymes
-
Ni-NTA column chromatography
-
TALON metal affinity resin column chromatography
-
recombinant enzyme
adenosine 3',5'-bisphosphate-agarose resin column chromatography
recombinant protein
-
recombinant enzyme
-
recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Arabidopsis for genetic complementation
expressed in Escherichia coli
expression of the Sal1 gene in Escherichia coli
-
expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli K-12 AG1
-
GhHL1 gene, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21, overexpression of GhHL1 complements yeast hal2 mutant and enhances yeast growth under elevated NaCl or LiCl
cloning of HsPIP and expression in Escherichia coli
expression in Sf9 cells
expression in Sf9 cells
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
overexpression of the HAL2 gene in Saccharomyces cerevisiae
-
expressed in Escherichia coli
-
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after 1h of dark treatment
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D201N
-
8.2% relative activity compared to the wild type enzyme
D363N
-
6.2% relative activity compared to the wild type enzyme
E133Q
-
4.8% relative activity compared to the wild type enzyme
E301K
-
strongly reduced activity compared to the wild type enzyme
T206A
-
5.6% relative activity compared to the wild type enzyme
V131A
-
strongly reduced activity compared to the wild type enzyme
D141A
less than 5% of the wild-type activity
D141N
less than 5% of the wild-type activity
D144N
less than 5% of the wild-type activity
D292A
less than 5% of the wild-type activity
D292N
less than 5% of the wild-type activity
W291L
less than 5% of the wild-type activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
GhHL1 is a functional and good candidate gene that might be used to improve salt tolerance in plants
biotechnology
Gossypium hirsutum CRI 12
-
GhHL1 is a functional and good candidate gene that might be used to improve salt tolerance in plants
-
medicine
enzyme as a potential target of lithium therapy
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
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
medicine
-
enzyme as a potential target of lithium therapy