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2'-AMP + H2O
?
-
10% relative activity compared to NADP+
-
-
?
2'-deoxyadenosine 3',5'-bisphosphate + H2O
2'-deoxyadenosine 5'-phosphate + phosphate
2'-deoxycytidine 3',5'-bisphosphate + H2O
2'-deoxycytidine 5'-phosphate + phosphate
2'-deoxyguanosine 3',5'-bisphosphate + H2O
2'-deoxyguanosine 5'-phosphate + phosphate
-
-
-
?
2'-deoxythymidine 3',5'-bisphosphate + H2O
2'-deoxythymidine 5'-phosphate + phosphate
-
-
-
?
2'-deoxyuridine 3',5'-bisphosphate + H2O
2'-deoxyuridine 5'-phosphate + phosphate
-
-
-
?
3'-AMP + H2O
?
-
84% relative activity compared to NADP+
-
-
?
3'-phosphoadenosine 5'-phosphate + H2
AMP + phosphate
-
-
-
?
3'-phosphoadenosine 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
5'-phosphoadenylyl-(3'->5')-adenosine + H2O
? + phosphate
-
-
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
adenosine 3',5'-bisphosphate + H2O
AMP + phosphate
adenosine 3',5'-bisphosphate sulfate + H2O
adenosine 5'-phosphate sulfate + phosphate
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
cytidine 3',5'-bisphosphate + H2O
cytidine 5'-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
?
D-myo-inositol 2-phosphate + H2O
D-myo-inositol + phosphate
-
9% relative activity compared to NADP+
-
-
?
D-myo-inositol monophosphate + H2O
D-myo-inositol + phosphate
D-myo-inositol-1,4,5-trisphosphate + H2O
?
-
14% relative activity compared to NADP+
-
-
?
D-myo-inositol-1,4-bisphosphate + H2O
?
-
485% relative activity compared to NADP+
-
-
?
guanosine 2',5'-bisphosphate + H2O
guanosine 2'-phosphate + phosphate
-
-
-
?
guanosine 3',5'-bisphosphate + H2O
guanosine 5'-phosphate + phosphate
inositol 1,3,4-trisphosphate + H2O
?
-
-
-
?
inositol 1,3,4-trisphosphate + H2O
inositol 3,4-bisphosphate + phosphate
inositol 1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
inositol-1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
N6-methyl-5'-phosphoadenylyl-(3'->5')-adenosine + H2O
? + phosphate
-
-
-
?
NADP+ + H2O
NAD+ + phosphate
-
100% activity
-
-
?
NADPH + H2O
NADH + phosphate
-
145% relative activity compared to NADP+
-
-
?
p-nitrophenyl phosphate
p-nitrophenol + phosphate
-
21% relative activity compared to NADP+
-
-
?
thymidine 3',5'-bisphosphate + H2O
thymidine 5'-phosphate + phosphate
-
-
-
?
uridine 3',5'-bisphosphate + H2O
uridine 5'-phosphate + phosphate
-
-
-
?
additional information
?
-
2'-deoxyadenosine 3',5'-bisphosphate + H2O
2'-deoxyadenosine 5'-phosphate + phosphate
-
-
-
?
2'-deoxyadenosine 3',5'-bisphosphate + H2O
2'-deoxyadenosine 5'-phosphate + phosphate
-
-
-
?
2'-deoxycytidine 3',5'-bisphosphate + H2O
2'-deoxycytidine 5'-phosphate + phosphate
-
-
-
?
2'-deoxycytidine 3',5'-bisphosphate + H2O
2'-deoxycytidine 5'-phosphate + phosphate
-
-
-
?
3'-phosphoadenosine 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
-
-
?
3'-phosphoadenosine 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
67% enzyme activity in comparison to 3'-phosphoadenosine 5'-phosphate as substrate
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
829% relative activity compared to NADP+
-
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
100% in comparison to 3'-phosphoadenosine 5'-phosphate as substrate
-
?
adenosine 2',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
only 6% enzyme activity in comparison to 3'-phosphoadenosine 5'-phosphate as substrate
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
100% activity
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
607% relative activity compared to NADP+
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
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
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
best substrate
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
best substrate
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
adenosine 5'-phosphate + phosphate
-
-
?
adenosine 3',5'-bisphosphate + H2O
AMP + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
AMP + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
AMP + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
AMP + phosphate
i.e. PAP
-
-
?
adenosine 3',5'-bisphosphate + H2O
AMP + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
AMP + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
AMP + phosphate
i.e. PAP
-
-
?
adenosine 3',5'-bisphosphate + H2O
AMP + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate + H2O
AMP + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate sulfate + H2O
adenosine 5'-phosphate sulfate + phosphate
-
-
-
?
adenosine 3',5'-bisphosphate sulfate + H2O
adenosine 5'-phosphate sulfate + phosphate
-
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
-
-
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
42% activity compared to adenosine 3',5'bisphosphate
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
-
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
-
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
-
-
-
?
adenosine 3'-phosphate 5'-phosphosulfate + H2O
adenosine 5'-phosphosulfate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
?
-
122% relative activity compared to NADP+
-
-
?
D-fructose 1,6-bisphosphate + H2O
?
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
?
-
-
-
?
D-myo-inositol monophosphate + H2O
D-myo-inositol + phosphate
-
13% relative activity compared to NADP+
-
-
?
D-myo-inositol monophosphate + H2O
D-myo-inositol + phosphate
-
-
-
?
D-myo-inositol monophosphate + H2O
D-myo-inositol + phosphate
-
-
-
?
guanosine 3',5'-bisphosphate + H2O
guanosine 5'-phosphate + phosphate
-
-
-
?
guanosine 3',5'-bisphosphate + H2O
guanosine 5'-phosphate + phosphate
-
-
-
?
guanosine 3',5'-bisphosphate + H2O
guanosine 5'-phosphate + phosphate
-
-
-
?
inositol 1,3,4-trisphosphate + H2O
inositol 3,4-bisphosphate + phosphate
-
-
-
-
?
inositol 1,3,4-trisphosphate + H2O
inositol 3,4-bisphosphate + phosphate
-
-
?
inositol 1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
-
-
-
-
?
inositol 1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
-
-
?
inositol 1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
-
-
-
?
inositol 1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
-
-
?
inositol-1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
5.6% activity compared to adenosine 3',5'bisphosphate
-
-
?
inositol-1,4-bisphosphate + H2O
inositol 4-phosphate + phosphate
-
-
?
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
?
-
-
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
?
-
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
?
-
-
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
?
-
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
?
-
-
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
?
-
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
?
-
-
the enzyme mediates lithium toxicity effects
-
-
?
additional information
?
-
3'-phosphoadenosine 5'-phosphate 3'-phosphatase plays a role in the formation of skeletal elements derived through endochondral ossification
-
-
?
additional information
?
-
enzyme has c-di-AMP specific phosphodiesterase activity. It hydrolyzes c-di-AMP to 5'-AMP in two steps. First, it linearizes c-di-AMP into pApA , reaction of EC 3.1.4.59, which is further hydrolyzed to 5'-AMP, reaction of EC 3.1.4.60
-
-
?
additional information
?
-
-
enzyme has c-di-AMP specific phosphodiesterase activity. It hydrolyzes c-di-AMP to 5'-AMP in two steps. First, it linearizes c-di-AMP into pApA , reaction of EC 3.1.4.59, which is further hydrolyzed to 5'-AMP, reaction of EC 3.1.4.60
-
-
?
additional information
?
-
Mtb CysQ can dephosphorylate myo-inositol 1-phosphate (IMP), fructose 1,6-bisphosphate (FBP), and 3'-phosphoadenosine 5'-monophosphate (PAP), but the catalytic efficiency is 1700 and 15000fold greater for PAP over FBP and IMP, respectively. AMP and phosphate enzyme binding structures, overview. The specificity of a 5'-phosphate or bis-phosphate sugars for CysQ can likely come from a conserved positively charged residue, Lys190 in CysQ, that ion pairs with the nonhydrolyzed phosphate
-
-
?
additional information
?
-
-
Mtb CysQ can dephosphorylate myo-inositol 1-phosphate (IMP), fructose 1,6-bisphosphate (FBP), and 3'-phosphoadenosine 5'-monophosphate (PAP), but the catalytic efficiency is 1700 and 15000fold greater for PAP over FBP and IMP, respectively. AMP and phosphate enzyme binding structures, overview. The specificity of a 5'-phosphate or bis-phosphate sugars for CysQ can likely come from a conserved positively charged residue, Lys190 in CysQ, that ion pairs with the nonhydrolyzed phosphate
-
-
?
additional information
?
-
enzyme has c-di-AMP specific phosphodiesterase activity. It hydrolyzes c-di-AMP to 5'-AMP in two steps. First, it linearizes c-di-AMP into pApA , reaction of EC 3.1.4.59, which is further hydrolyzed to 5'-AMP, reaction of EC 3.1.4.60
-
-
?
additional information
?
-
Mtb CysQ can dephosphorylate myo-inositol 1-phosphate (IMP), fructose 1,6-bisphosphate (FBP), and 3'-phosphoadenosine 5'-monophosphate (PAP), but the catalytic efficiency is 1700 and 15000fold greater for PAP over FBP and IMP, respectively. AMP and phosphate enzyme binding structures, overview. The specificity of a 5'-phosphate or bis-phosphate sugars for CysQ can likely come from a conserved positively charged residue, Lys190 in CysQ, that ion pairs with the nonhydrolyzed phosphate
-
-
?
additional information
?
-
adenosine 3',5'-bisphosphate is not the primary substrate, the enzyme may be important for response to salt stress
-
-
?
additional information
?
-
-
adenosine 3',5'-bisphosphate is not the primary substrate, the enzyme may be important for response to salt stress
-
-
?
additional information
?
-
isoform additonally hydrolyses cyclic di-AMP, reaction of EC 3.1.4.59. No substrate: ATP
-
-
?
additional information
?
-
isoform additonally hydrolyses cyclic di-AMP, reaction of EC 3.1.4.59. No substrate: ATP
-
-
?
additional information
?
-
not: 3-AMP, ATP, NADP, O-phospho-L-serine, phosphoglycolic acid, L-histidinol phosphate
-
?
additional information
?
-
not: 3-AMP, ATP, NADP, O-phospho-L-serine, phosphoglycolic acid, L-histidinol phosphate
-
?
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0.0102
2'-deoxyadenosine 3',5'-bisphosphate
pH 7.5, 3°C
0.026
2'-deoxycytidine 3',5'-bisphosphate
pH 7.5, 3°C
0.0052
2'-deoxyguanosine 3',5'-bisphosphate
pH 7.5, 3°C
0.022
2'-deoxythymidine 3',5'-bisphosphate
pH 7.5, 3°C
0.029
2'-deoxyuridine 3',5'-bisphosphate
pH 7.5, 3°C
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 30°C
0.0016
5'-phosphoadenylyl-(3'->5')-adenosine
pH 7.5, 3°C
0.007 - 0.14
adenosine 2',5'-bisphosphate
0.000475 - 1.03
adenosine 3',5'-bisphosphate
0.1 - 0.61
adenosine 3'-phosphate 5'-phosphosulfate
0.566 - 1.17
D-fructose 1,6-bisphosphate
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, 3°C
0.25
guanosine-3',5'-bisphosphate
-
-
0.1
inositol 1,3,4-trisphosphate
-
0.077 - 0.113
inositol 1,4-bisphosphate
0.0004
inositol-1,4-bisphosphate
pH 7.5, 30°C
0.0054
N6-methyl-5'-phosphoadenylyl-(3'->5')-adenosine
pH 7.5, 3°C
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, 3°C
0.0088
uridine 3',5'-bisphosphate
pH 7.5, 3°C
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, 30°C
0.0015
adenosine 3',5'-bisphosphate
pH 7.5, 3°C
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 30°C
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 30°C
0.033
adenosine 3',5'-bisphosphate
pH 8.1, 30°C
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 30°C
0.126
adenosine 3',5'-bisphosphate
pH 8.1, 30°C
0.24
adenosine 3',5'-bisphosphate
-
-
0.24
adenosine 3',5'-bisphosphate
-
in 10 mM HEPES pH 7.0
1.03
adenosine 3',5'-bisphosphate
in 50 mM Tris (pH 8.0), 2 mM MgCl2, at 30°C
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 30°C
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
0.077
inositol 1,4-bisphosphate
-
pH 7.8, 30°C
0.09
inositol 1,4-bisphosphate
-
-
0.113
inositol 1,4-bisphosphate
-
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evolution
BPNT-1 is conserved in all eukaryotes, and belongs to a family of lithium-sensitive phosphatases that includes inositol monophosphatase and inositol polyphosphate-1-phosphatase
evolution
CysQ is part of the larger FIG superfamily of phosphatases that dephosphorylates a monosaccharide-containing substrate. The FIG superfamily is comprised of family members: fructose-1,6-bisphosphatase (FBPase), inositol-monophosphatases (IMPase)/polyphosphatases (IPPase), and the glpX-encoded variant of FBPase (Class II). Many members of this superfamily display promiscuous phosphatase activity toward various monosaccharide-containing substrates but are usually more efficient in one type, which identifies their subfamily class. Mtb CysQ can dephosphorylate myo-inositol 1-phosphate (IMP), fructose 1,6-bisphosphate (FBP), and 3'-phosphoadenosine 5'-monophosphate (PAP), but the catalytic efficiency is 1700 and 15000fold greater for PAP over FBP and IMP, respectively. The FIG superfamily enzymes have demonstrated a dependence on divalent metal ions and are most active with magnesium. The superfamily also displays sensitivity to monovalent metals, and members are most strongly inhibited by lithium (Li+)
evolution
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CysQ is part of the larger FIG superfamily of phosphatases that dephosphorylates a monosaccharide-containing substrate. The FIG superfamily is comprised of family members: fructose-1,6-bisphosphatase (FBPase), inositol-monophosphatases (IMPase)/polyphosphatases (IPPase), and the glpX-encoded variant of FBPase (Class II). Many members of this superfamily display promiscuous phosphatase activity toward various monosaccharide-containing substrates but are usually more efficient in one type, which identifies their subfamily class. Mtb CysQ can dephosphorylate myo-inositol 1-phosphate (IMP), fructose 1,6-bisphosphate (FBP), and 3'-phosphoadenosine 5'-monophosphate (PAP), but the catalytic efficiency is 1700 and 15000fold greater for PAP over FBP and IMP, respectively. The FIG superfamily enzymes have demonstrated a dependence on divalent metal ions and are most active with magnesium. The superfamily also displays sensitivity to monovalent metals, and members are most strongly inhibited by lithium (Li+)
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malfunction
cysQ knockout results in reduced levels of the sulfated glycolipid sulfolipid-1 and attenuation of cell growth
malfunction
in glioma tissues, glycerophosphatidylcholine [PC(36:1)] is not detected and 3'-phosphoadenylate (pAp) content is significantly increased. The gene expressions of 3'-nucleotidases inositol monophosphatase (IMPAD-1) and 3'(2'),5'-bisphosphate nucleotidase 1 (BPNT-1)) are dramatically downregulated. Dramatic downregulation of IMPAD-1 and BPNT-1 are the primary cause for pAp dramatic accumulation
malfunction
loss of BPNT-1 in Caenorhabditis elegans results in the selective dysfunction two neurons, the bilaterally symmetric pair of ASJ chemosensory neurons. As a result, BPNT-1 mutants are defective in behaviors dependent on the ASJ neurons, such as dauer exit and pathogen avoidance. Acute treatment with lithium also causes dysfunction of the ASJ neurons. This effect is reversible, and mediated specifically through inhibition of BPNT-1. The selective effect of lithium on the nervous system is due in part to the limited expression of the cytosolic sulfotransferase SSU-1 in the ASJ neuron pair. Lithium, through inhibition of BPNT-1 in the nervous system, can cause selective toxicity to specific neurons, resulting in corresponding effects on behavior of Caenorhabditis elegans, molecular mechanism by which loss of BPNT-1 leads to dysfunction of the ASJ neuron, bpnt-1 phenotypes, overview. The specific expression of the cytosolic sulfotransferase SSU-1 in the ASJ neuron pair may contribute to the selective neuronal dysfunction caused by loss of BPNT-1
malfunction
-
cysQ knockout results in reduced levels of the sulfated glycolipid sulfolipid-1 and attenuation of cell growth
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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
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
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
a Pde2 mutant strain displays a growth defect in the early growth phase. Mutation leads to an increase in cellular c-di-AMP and 5'-O-phosphonoadenylyl-(3'->5')-adenosine levels and increased resistance to oxacillin
physiological function
because excess 3'-phosphoadenosine 5'-phosphate (PAP) alters the equilibrium of the sulfur pathway and inhibits sulfotransferases, PAP concentrations can affect the levels of sulfur-containing metabolites. PAP is removed by the phosphatase activity of CysQ, a 3',5'-bisphosphate nucleotidase, yielding AMP and phosphate, CysQ, a divalent cation metal-dependent phosphatase, is a major regulator of the sulfur activation pathway
physiological function
bisphosphate 3'-nucleotidase (BPNT-1) is a lithium-sensitive phosphatase that catalyzes the breakdown of cytosolic 3'-phosphoadenosine-5'-phosphate (PAP), a byproduct of sulfation reactions utilizing the universal sulfate group donor 3'-phosphoadenosine-5'-phosphosulfate (PAPS). The daf-7 gene encodes a TGF-beta ligand that regulates diverse behaviors Caenorhabditis elegans and is transcriptionally activated in the ASJ chemosensory neuron pair upon exposure to the pathogenic bacteria Pseudomonas aeruginosa. BPNT-1 is required for the expression of daf-7 specifically in the ASJ neurons
physiological function
Gene expression of enzymes associated with 3'-phosphoadenylate (pAp) metabolism, pAp is a toxic by-product
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
-
a Pde2 mutant strain displays a growth defect in the early growth phase. Mutation leads to an increase in cellular c-di-AMP and 5'-O-phosphonoadenylyl-(3'->5')-adenosine levels and increased resistance to oxacillin
-
physiological function
-
because excess 3'-phosphoadenosine 5'-phosphate (PAP) alters the equilibrium of the sulfur pathway and inhibits sulfotransferases, PAP concentrations can affect the levels of sulfur-containing metabolites. PAP is removed by the phosphatase activity of CysQ, a 3',5'-bisphosphate nucleotidase, yielding AMP and phosphate, CysQ, a divalent cation metal-dependent phosphatase, is a major regulator of the sulfur activation pathway
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