3.6.1.5: apyrase
This is an abbreviated version!
For detailed information about apyrase, go to the full flat file.
Word Map on EC 3.6.1.5
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3.6.1.5
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platelet
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purinergic
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agonist
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endothelial
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suramin
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ntpdases
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5'-nucleotidase
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thrombin
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utp
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fibrinogen
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thromboxane
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salivary
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blocker
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ecto-nucleotidases
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ecto-5\'-nucleotidase
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purinoceptors
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platelet-rich
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aspirin
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5'-triphosphate
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ecto-enzymes
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ouabain
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ppads
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oligomycin
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adp-induced
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synaptosomes
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serca2
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hirudin
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blood-feeding
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atp-mediated
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carbenoxolone
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tyrode
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hemichannels
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alpha,beta-methylene
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arl
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pannexins
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atp-hydrolyzing
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luciferin-luciferase
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adenosinergic
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agriculture
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e-type
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phlebotomus
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analysis
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pharmacology
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hematophagous
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adp-dependent
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medicine
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preretinal
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gel-filtered
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ap5a
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aggregometry
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bzatp
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drug development
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ectonucleotide
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3.1.3.5
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atpgammas
- 3.6.1.5
- platelet
-
purinergic
- agonist
- endothelial
- suramin
- ntpdases
- 5'-nucleotidase
- thrombin
- utp
- fibrinogen
-
thromboxane
-
salivary
-
blocker
- ecto-nucleotidases
-
ecto-5\'-nucleotidase
-
purinoceptors
-
platelet-rich
- aspirin
- 5'-triphosphate
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ecto-enzymes
- ouabain
-
ppads
- oligomycin
-
adp-induced
-
synaptosomes
- serca2
- hirudin
-
blood-feeding
-
atp-mediated
- carbenoxolone
-
tyrode
-
hemichannels
-
alpha,beta-methylene
- arl
-
pannexins
-
atp-hydrolyzing
- luciferin-luciferase
-
adenosinergic
- agriculture
-
e-type
- phlebotomus
- analysis
- pharmacology
-
hematophagous
-
adp-dependent
- medicine
-
preretinal
-
gel-filtered
- ap5a
-
aggregometry
-
bzatp
- drug development
-
ectonucleotide
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3.1.3.5
- atpgammas
Reaction
Synonyms
5' ectonucleotidase, 5'-nucleotidase, adenosine diphosphatase, adenosine pyrophosphatase, adenylpyrophophatase, ADPase, APT102, Apy, Apy 1, Apy 2, APY-1, APY1, APY10, APY2, APY2-type apyrase, APY4, APY5, APY6, APY7, APY8, APY9, Apyrase, apyrase 2, APYRASE2, At1g14230, At1g14240, At1g14250, At2g02970, At3g04080, At5g18280, AtAPY1, AtAPY2, AtAPY3, AtAPY4, AtAPY5, AtAPY6, ATP diphosphohydrolase, ATP diphosphohyrolase, ATP-diphosphatase, ATP-diphosphohydrolase, ATP-diphosphohydrolase 2, ATPase, ATPase 2, ATPDase, ATPDase1, ATPDase2, BjAPY2, Ca2+-activated nucleoside diphosphatase, CApy, CD39, CD39 antigen, CD39-like ATP diphosphohydrolase, CD39L1, Def11, E-NTPDase, E-NTPDase 3, ecto-5'-nucleotidase, ecto-apyrase, ecto-ATP diphosphohydrolase, ecto-ATP-diphosphohydrolase, ecto-ATPase, ecto-ATPDase, ecto-NTPDase, Ecto-NTPDase1, ecto-nucleoside triphosphate diphosphohydrolase, ecto-nucleoside triphosphate diphosphohydrolase 1, ecto-nucleoside triphosphate diphosphohydrolase 2, ecto-nucleoside triphosphate diphosphohydrolase1, ecto-nucleoside triphosphate diphosphohydrolase2, ecto-nucleoside triphosphate diphosphohydrolase3, ecto-nucleoside triphosphate diphosphohydrolase8, ecto-nucleoside triphosphate-diphosphohydrolase, ecto-nucleoside-triphosphate-diphosphohydrolase, ectoapyrase, ectonucleoside triphosphate diphosphohydrolase, ectonucleoside triphosphate diphosphohydrolase 3, ectonucleotidase, ENTPD1, ENTPD2, ENTPD3, Entpd8, ENTPDase1, esctonucleoside triphosphate diphosphohydrolase 1, esctonucleoside triphosphate diphosphohydrolase 2, esctonucleoside triphosphate diphosphohydrolase 8, Golgi nucleoside diphosphatase, GS50, GS52, HB6, hCD39, LALP1, LBRM_15_0030, LicNTPDase-2, LINJ_15_0030, LmjF15.0030, LmNTPDase 1, Lpg1905, lumenal NDPase, Lymphoid cell activation antigen, More, MP67, MpAPY2, NTPase, NTPD1, NTPDase, NTPDase 1, NTPDase 2, NTPDase 3, NTPDase 5, NTPDase 6, NTPDase 8, NTPDase1, NTPDase1/CD39, NTPDase2, NTPDase2/CD39L1, NTPDase3, NTPDase8, nucleoside triphosphatase, nucleoside triphosphate diphosphohydrolase, nucleoside triphosphate diphosphohydrolase 1, nucleoside triphosphate diphosphohydrolase 2, nucleoside triphosphate diphosphohydrolase 8, nucleoside triphosphate diphosphohydrolase-1, NDPDase 1, nucleoside triphosphate diphosphohydrolase-2, nucleoside triphosphate diphosphohydrolase-3, nucleoside triphosphate diphosphohydrolase-8, nucleoside triphosphate disphophohydrolase, nucleoside triphosphate-diphosphohydrolase, nucleotide triphosphate diphosphohydrolase, PeAPY2, potato-specific apyrase, PsAPY1, psNTP9, r-NTPDase 1, r-NTPDase 2, r-NTPDase 3, r-NTPDase 8, Ruviapyrase, SCAN-1, snake venom apyrase, SolCD39/NTPDase1, soluble apyrase, soluble calcium-activated nucleotidase 1, soluble CD39, TaAPY1, TaAPY2, TaAPY3-1, TaAPY3-2, TaAPY3-3, TaAPY3-4, TaAPY5, TaAPY6, TaAPY7, XAPY
ECTree
3.6.1.5 apyraseAdvanced search results
results (
results (Engineering
Engineering on EC 3.6.1.5 - apyrase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D209A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
E182A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
Q216A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
S214A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
C10S
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112% of wild-type ATPase activity, 105% of wild-type ADPase activity, residue responsible for dimer formation
C10S/C501S
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148% of wild-type ATPase activity, 133% of wild-type ADPase activity
C10S/C501S/C509S
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79% of wild-type ATPase activity, 77% of wild-type ADPase activity
C10S/C509S
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103% of wild-type ATPase activity, 99% of wild-type ADPase activity
C501S
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130% of wild-type ATPase activity, 130% of wild-type ADPase activity, site of modification by p-chloromercuriphenylsulfonic acid
C501S/C509S
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138% of wild-type ATPase activity, 134% of wild-type ADPase activity
N168A
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site-directed mutagenesis, the mutant shows reduced activity due to decreased affinity for the nucleotide substrates, with a relatively increased Km 1.3fold for ATP hydrolysis and 3fold for ADP hydrolysis for the mutant enzyme, the mutant partially restores the ability of an enzyme-deficient Legionella pneumophila lpg1905 mutant strain to replicate in THP-1 macrophages
A75S
the Km value for ADP of the isoform APY2 mutant is decreased compared to the wild type enzyme, while the Km value for ATP is substantially increased. The mutant shows higher specific acitivity for ADP than ATP
S63A
the ratio of the velocity of ATP/ADP hydrolysis is higher for the isoform MP67 mutant (approximately 1) compared to the wild type enzyme
E493G
the mutant of isoform NTPDase1 shows conversion of ATP/ADP specificity compared to the wild type enzyme
R492G
the mutant of isoform NTPDase1 shows conversion of ATP/ADP specificity compared to the wild type enzyme
R492G/E493G
the mutant of isoform NTPDase1 shows conversion of ATP/ADP specificity compared to the wild type enzyme
additional information
additional information
AtAPY4 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
additional information
AtAPY4 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
additional information
AtAPY4 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
additional information
AtAPY4 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
additional information
AtAPY4 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
additional information
AtAPY4 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
additional information
AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. Construction of atapy6 mutants. dKO mutants lacking both isozymes AtAPY6 and AtAPY7 produce relatively normal plants but with low male fertility from collapsed pollen which further results in reduced seed set. Synergistic effects observed in atapy6atapy7 double mutant
additional information
AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. Construction of atapy6 mutants. dKO mutants lacking both isozymes AtAPY6 and AtAPY7 produce relatively normal plants but with low male fertility from collapsed pollen which further results in reduced seed set. Synergistic effects observed in atapy6atapy7 double mutant
additional information
AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. Construction of atapy6 mutants. dKO mutants lacking both isozymes AtAPY6 and AtAPY7 produce relatively normal plants but with low male fertility from collapsed pollen which further results in reduced seed set. Synergistic effects observed in atapy6atapy7 double mutant
additional information
AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. Construction of atapy6 mutants. dKO mutants lacking both isozymes AtAPY6 and AtAPY7 produce relatively normal plants but with low male fertility from collapsed pollen which further results in reduced seed set. Synergistic effects observed in atapy6atapy7 double mutant
additional information
AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. Construction of atapy6 mutants. dKO mutants lacking both isozymes AtAPY6 and AtAPY7 produce relatively normal plants but with low male fertility from collapsed pollen which further results in reduced seed set. Synergistic effects observed in atapy6atapy7 double mutant
additional information
AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. Construction of atapy6 mutants. dKO mutants lacking both isozymes AtAPY6 and AtAPY7 produce relatively normal plants but with low male fertility from collapsed pollen which further results in reduced seed set. Synergistic effects observed in atapy6atapy7 double mutant
additional information
generation of apy1 single knockout (APY1 KO) seedlings by RNAi. Treatment of R2-4A seedlings with estradiol induces 70% suppression of APY1 expression in the null background of APY2 and results in shortened roots with swollen root tips
additional information
generation of apy1 single knockout (APY1 KO) seedlings by RNAi. Treatment of R2-4A seedlings with estradiol induces 70% suppression of APY1 expression in the null background of APY2 and results in shortened roots with swollen root tips
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant reveals that AtAPY3 exhibits relatively weak complementation compared with other members of this clade. The AtAPY3 construct is the least able to recover cell wall mannose, reflecting the reduced growth phenotype
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant reveals that AtAPY3 exhibits relatively weak complementation compared with other members of this clade. The AtAPY3 construct is the least able to recover cell wall mannose, reflecting the reduced growth phenotype
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant reveals that AtAPY3 exhibits relatively weak complementation compared with other members of this clade. The AtAPY3 construct is the least able to recover cell wall mannose, reflecting the reduced growth phenotype
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant reveals that AtAPY3 exhibits relatively weak complementation compared with other members of this clade. The AtAPY3 construct is the least able to recover cell wall mannose, reflecting the reduced growth phenotype
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant reveals that AtAPY3 exhibits relatively weak complementation compared with other members of this clade. The AtAPY3 construct is the least able to recover cell wall mannose, reflecting the reduced growth phenotype
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant reveals that AtAPY3 exhibits relatively weak complementation compared with other members of this clade. The AtAPY3 construct is the least able to recover cell wall mannose, reflecting the reduced growth phenotype
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. AtAPY5 is able to complement the growth defect phenotype of the mutant. The proportion of mannose in cell wall extracts significantly increases in all the complemented strains with the AtAPY5 construct resulting in near wild-type levels
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. AtAPY5 is able to complement the growth defect phenotype of the mutant. The proportion of mannose in cell wall extracts significantly increases in all the complemented strains with the AtAPY5 construct resulting in near wild-type levels
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. AtAPY5 is able to complement the growth defect phenotype of the mutant. The proportion of mannose in cell wall extracts significantly increases in all the complemented strains with the AtAPY5 construct resulting in near wild-type levels
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. AtAPY5 is able to complement the growth defect phenotype of the mutant. The proportion of mannose in cell wall extracts significantly increases in all the complemented strains with the AtAPY5 construct resulting in near wild-type levels
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. AtAPY5 is able to complement the growth defect phenotype of the mutant. The proportion of mannose in cell wall extracts significantly increases in all the complemented strains with the AtAPY5 construct resulting in near wild-type levels
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. AtAPY5 is able to complement the growth defect phenotype of the mutant. The proportion of mannose in cell wall extracts significantly increases in all the complemented strains with the AtAPY5 construct resulting in near wild-type levels
additional information
when clade I Arabidopsis apyrases are expressed in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, both AtAPY1 and AtAPY2 are able to complement the growth phenotype compared to the yeast mutant harbouring the empty vector
additional information
when clade I Arabidopsis apyrases are expressed in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, both AtAPY1 and AtAPY2 are able to complement the growth phenotype compared to the yeast mutant harbouring the empty vector
additional information
when clade I Arabidopsis apyrases are expressed in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, both AtAPY1 and AtAPY2 are able to complement the growth phenotype compared to the yeast mutant harbouring the empty vector
additional information
when clade I Arabidopsis apyrases are expressed in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, both AtAPY1 and AtAPY2 are able to complement the growth phenotype compared to the yeast mutant harbouring the empty vector
additional information
when clade I Arabidopsis apyrases are expressed in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, both AtAPY1 and AtAPY2 are able to complement the growth phenotype compared to the yeast mutant harbouring the empty vector
additional information
when clade I Arabidopsis apyrases are expressed in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, both AtAPY1 and AtAPY2 are able to complement the growth phenotype compared to the yeast mutant harbouring the empty vector
additional information
construction of a hu-ck ACR1,5 chimera in which the extracellular domain of human NTPDase2 is anchored to the membrane by the two transmembrane domains of the chicken NTPDase8. The hu-ck ACR1,5 chimera is the first chimeric NTPDase reported that shows a resistance to membrane perturbation and substrate inactivation. The strength of interaction of the respective transmembrane domain pairs of the human NTPDase2 and chicken NTPDase8 determine their different responses to membrane perturbation and substrate. The chimeric mutants all show highly reduced ATPase activities, overview. Catalysis at the active site in the extracellular domain of the hu-ck ACR1,5 chimera is no longer negatively affected by membrane perturbation in the lipid bilayer by detergent and temperature
additional information
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construction of a hu-ck ACR1,5 chimera in which the extracellular domain of human NTPDase2 is anchored to the membrane by the two transmembrane domains of the chicken NTPDase8. The hu-ck ACR1,5 chimera is the first chimeric NTPDase reported that shows a resistance to membrane perturbation and substrate inactivation. The strength of interaction of the respective transmembrane domain pairs of the human NTPDase2 and chicken NTPDase8 determine their different responses to membrane perturbation and substrate. The chimeric mutants all show highly reduced ATPase activities, overview. Catalysis at the active site in the extracellular domain of the hu-ck ACR1,5 chimera is no longer negatively affected by membrane perturbation in the lipid bilayer by detergent and temperature
additional information
generation of a soluble truncated mutant NTPDase8 by removal of amino acids 1-28 (containing TMD1) and 464-493 (containing TMD2), the mutant shows 85% reduced activity compared to the full-length membrane-bound enzyme. Generation of chimeric mutant Ck-hu TMD1, encoding a protein in which the N-terminus (aa 1-28) of the chicken NTPDase8 is substituted with the corresponding region (aa 1-29) of the human NTPDase2, which includes its TMD1, and of chimeric mutant Ck-hu TMD2, encoding a protein in which the C-terminus (aa 465-493) of the chicken NTPDase8 is substituted with the corresponding region (aa 461-495) of the human NTPDase2, which includes its TMD2
additional information
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generation of a soluble truncated mutant NTPDase8 by removal of amino acids 1-28 (containing TMD1) and 464-493 (containing TMD2), the mutant shows 85% reduced activity compared to the full-length membrane-bound enzyme. Generation of chimeric mutant Ck-hu TMD1, encoding a protein in which the N-terminus (aa 1-28) of the chicken NTPDase8 is substituted with the corresponding region (aa 1-29) of the human NTPDase2, which includes its TMD1, and of chimeric mutant Ck-hu TMD2, encoding a protein in which the C-terminus (aa 465-493) of the chicken NTPDase8 is substituted with the corresponding region (aa 461-495) of the human NTPDase2, which includes its TMD2
additional information
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RNA interference to silence GS52 expression in Glycine max roots using Agrobacterium rhizogenes-mediated root transformation. Transcript levels of GS52 are significantly reduced in GS52 silenced roots, and these roots exhibit reduced numbers of mature nodules. Development of the nodule primordium and subsequent nodule maturation is significantly suppressed in GS52 silenced roots. Application of exogenous adenosine diphosphate to silenced GS52 roots restores nodule development, phenotype, overview
additional information
construction of a hu-ck ACR1,5 chimera in which the extracellular domain is anchored to the membrane by the two transmembrane domains of the chicken NTPDase8. The hu-ck ACR1,5 chimera is the first chimeric NTPDase reported that shows a resistance to membrane perturbation and substrate inactivation. The strengths of interaction of the respective transmembrane domain pairs of the human NTPDase2 and chicken NTPDase8 determine their different responses to membrane perturbation and substrate. The chimeric mutants all show highly reduced ATPase activities, overview. Catalysis at the active site in the extracellular domain of the hu-ck ACR1,5 chimera is no longer negatively affected by membrane perturbation in the lipid bilayer by detergent and temperature
additional information
-
construction of a hu-ck ACR1,5 chimera in which the extracellular domain is anchored to the membrane by the two transmembrane domains of the chicken NTPDase8. The hu-ck ACR1,5 chimera is the first chimeric NTPDase reported that shows a resistance to membrane perturbation and substrate inactivation. The strengths of interaction of the respective transmembrane domain pairs of the human NTPDase2 and chicken NTPDase8 determine their different responses to membrane perturbation and substrate. The chimeric mutants all show highly reduced ATPase activities, overview. Catalysis at the active site in the extracellular domain of the hu-ck ACR1,5 chimera is no longer negatively affected by membrane perturbation in the lipid bilayer by detergent and temperature
additional information
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inactivation of apy-1 function by RNAi increased GFP expression fourfold with respect to control, which reflects an hsp-4 upregulation, indicating that loss of apy-1 may effectively cause endoplasmic reticulum stress
additional information
construction of hCD39 transgene expressing CD39Tg mice from C57BL/6 wild-type expressing human CD39, hCD39 transgene expression in CD39Tg mice reduces ischemia-induced acute renal injury, but exacerbates chronic renal injury. In comparison with wild-type littermates, hCD39 transgenic mice are protected from acute renal injury at 24 hours, but have increased renal fibrosis at 4 weeks post-ischemia-reperfusion injury (IRI), hCD39 transgene expression is localized to the vascular endothelium at baseline and does not affect total renal nucleotide and nucleoside levels during ischemia. But hCD39 transgene is more widespread at 4 weeks post-IRI and is associated with higher renal adenosine levels at 4 weeks post-IRI compared with wild-type littermates
additional information
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construction of hCD39 transgene expressing CD39Tg mice from C57BL/6 wild-type expressing human CD39, hCD39 transgene expression in CD39Tg mice reduces ischemia-induced acute renal injury, but exacerbates chronic renal injury. In comparison with wild-type littermates, hCD39 transgenic mice are protected from acute renal injury at 24 hours, but have increased renal fibrosis at 4 weeks post-ischemia-reperfusion injury (IRI), hCD39 transgene expression is localized to the vascular endothelium at baseline and does not affect total renal nucleotide and nucleoside levels during ischemia. But hCD39 transgene is more widespread at 4 weeks post-IRI and is associated with higher renal adenosine levels at 4 weeks post-IRI compared with wild-type littermates
additional information
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following intratracheal inoculation of A/J mice, none of the Lpg1905 mutants is able to restore virulence to an lpg1905 mutant during lung infection
additional information
purified recombinant LicNTPDase-2 is covalently immobilized onto a fused silica capillary tube to create an immobilized capillary enzyme reactor (ICER) based on LicNTPDase-2(LicNTPDase-2-ICER), development of a label-free online screening method, evaluation of the activity and stability of the enzyme by the multidimensional LicNTPDase-2-ICER method, overview
additional information
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purified recombinant LicNTPDase-2 is covalently immobilized onto a fused silica capillary tube to create an immobilized capillary enzyme reactor (ICER) based on LicNTPDase-2(LicNTPDase-2-ICER), development of a label-free online screening method, evaluation of the activity and stability of the enzyme by the multidimensional LicNTPDase-2-ICER method, overview
additional information
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Cd39-/- mice phenotype with increased levels of macrophages and neutrophils, cerebral ischemia effects, overview. 50% increase in the number of alphaMbeta2-integrin high-expressing monocytes in Cd39-/- mice compared with wild-type controls. Although an acute rescue from CD39 deficiency can be obtained through administration of an apyrase or solCD39 analog, a permanent rescue can be obtained via bone marrow reconstitution with CD39-bearing cells
additional information
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under cold stress, PeAPY2-overexpressing transgenic plants maintain plasma membrane integrity and show reduced cold-elicited electrolyte leakage compared with wild-type plants. These responses probably result from efficient plasma membrane repair via vesicular trafficking. Transgenic plants show accelerated endocytosis and exocytosis during cold stress and recovery. Low doses of extracellular ATP accelerate vesicular trafficking, but high extracellular ATP inhibit trafficking and reduce cell viability. The transcript abundance of seven intrinsic Arabidopsis apyrase genes, AtAPY1, AtAPY2, AtAPY3, AtAPY4, AtAPY5, AtAPY6, and AtAPY7, is not altered by the overexpression of exogenous PeAPY2
additional information
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construction of chimeric proteins from enzyme and ectoATPase. ectoATPase prefers ATP as substrate over ADP and releases mainly ADP. Chimeras contain N-terminal sequences of enzyme of increasing length fused to ectoATPase and vice versa. Protein structure rather than conserved regions may be of major relevance for determining differences in the catalytic properties
additional information
replacement of the extracellular domain of Rattus norvegicus NTPDase1, i.e. amino acid sequence 190TQEQSWLNFISDSQKQA206, with the shorter hydrophilic loop found in Homo sapiens NTPDase6, 240KTPGGS245. This NTPDase1 ECD DELTAMIL mutant variant is a soluble NTPDase1 that lacks a putative membrane interaction loop identified between the two lobes of the catalytic domain
additional information
efficient PiggyBac-mediated transposition of the recombinant soluble enzymes, method overview. Transfected cells secrete an enzymatically active wild-type soluble NTPDase1/CD39
additional information
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mutational analysis of residues involved in catalysis, overview
additional information
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silencing of the apyrase with RNAi constructs under the control of the constitutive 35S promoter leads to a strong decrease in apyrase activity to below 10% of the wild-type level. This decreased activity leads to phenotypic changes in the transgenic lines, including a general retardation in growth, an increase in tuber number per plant, and differences in tuber morphology. Silencing of apyrase under the control of a tuber-specific promoter B33 leads to similar changes in tuber morphology, but not to direct effects of apyrase inhibition on tuber metabolism, phenotypes, overview
additional information
development of a two-dimensional array ATP/ADP sensitive image sensor with a uniform distribution of chemically immobilized apyrase, immobilization via the two different methods 3-APTES and CEST, analysis method evaluation and optimization, overview. The surface of the ATP image sensor with 3-APTES method is polluted with the precipitation and shows heterogeneity. The ATP image sensor with CEST method shows a clear surface as well as that before the immobilization of apyrase. Potential disributions, and durability analysis
additional information
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immobilization of the enzyme in a two-step process: in the first step, carboxyl group on polyethylene terephthalate (PET) surface is activated by the crosslinker 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride, and in the second step, the enzyme is covalently attached to the activated carboxyl group, method development and evaluation. Kinetic study of NTPDase immobilization and its effect of hemocompatibility on PET, overview. Surface morphology and chemical composition of the unmodified and modified PET films are examined using scanning electron microscope with energy dispersive X-ray spectroscopy analysis
