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Information on EC 3.6.1.5 - apyrase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9XI62
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3.6.1.5 apyraseIUBMB Comments
Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyse NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates. They differ from ATPases, which specifically hydrolyse ATP, by hydrolysing both ATP and ADP. The eukaryotic enzymes requires Ca2+, but Mg2+ can substitute. Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family.
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- 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
-
ecto-enzymes
- ouabain
-
ppads
- oligomycin
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adp-induced
-
synaptosomes
- serca2
- hirudin
-
blood-feeding
-
atp-mediated
- carbenoxolone
-
tyrode
-
hemichannels
-
alpha,beta-methylene
- arl
-
pannexins
-
atp-hydrolyzing
- luciferin-luciferase
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adenosinergic
- agriculture
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e-type
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- analysis
- pharmacology
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hematophagous
-
adp-dependent
- medicine
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preretinal
-
gel-filtered
- ap5a
-
aggregometry
-
bzatp
- drug development
-
ectonucleotide
-
3.1.3.5
- atpgammas
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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Synonyms
apyrase, ecto-atpase, adpase, ntpdase3, atp diphosphohydrolase, entpd1, atpase 2, ecto-apyrase, ectonucleoside triphosphate diphosphohydrolase, atpdase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine diphosphatase
-
-
-
-
ADPase
-
-
-
-
APY1
APY2
ATP-diphosphatase
-
-
-
-
ATP-diphosphohydrolase
ATPDase
-
-
-
-
CD39 antigen
-
-
-
-
Golgi nucleoside diphosphatase
-
-
-
-
HB6
-
-
-
-
Lymphoid cell activation antigen
-
-
-
-
NTPDase
NTPDase1
-
-
-
-
NTPDase3
-
-
-
-
additional information
ATP-diphosphohydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
nucleoside triphosphate phosphohydrolase (nucleoside monophosphoate-forming)
Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyse NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates. They differ from ATPases, which specifically hydrolyse ATP, by hydrolysing both ATP and ADP. The eukaryotic enzymes requires Ca2+, but Mg2+ can substitute. Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family.
CAS REGISTRY NUMBER
COMMENTARY
9000-95-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + H2O
AMP + phosphate
-
-
-
?
CTP + H2O
CDP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
very low activity with UDP
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
CDP + H2O
CMP + phosphate
best substrate
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
two steps, very low activity with CDP
-
-
?
CTP + H2O
CDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
high activity
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
best substrate
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
very low activity with UDP
-
-
?
additional information
?
-
the clade II member AtAPY3 has a strong preference toward NTPs but also has significant activities toward ADP and GDP. No activity with CDP, CMP, and GMP
-
-
-
additional information
?
-
the clade II member AtAPY3 has a strong preference toward NTPs but also has significant activities toward ADP and GDP. No activity with CDP, CMP, and GMP
-
-
-
additional information
?
-
the clade II member AtAPY3 has a strong preference toward NTPs but also has significant activities toward ADP and GDP. No activity with CDP, CMP, and GMP
-
-
-
additional information
?
-
the clade II member AtAPY3 has a strong preference toward NTPs but also has significant activities toward ADP and GDP. No activity with CDP, CMP, and GMP
-
-
-
additional information
?
-
the clade II member AtAPY3 has a strong preference toward NTPs but also has significant activities toward ADP and GDP. No activity with CDP, CMP, and GMP
-
-
-
additional information
?
-
the clade II member AtAPY3 has a strong preference toward NTPs but also has significant activities toward ADP and GDP. No activity with CDP, CMP, and GMP
-
-
-
additional information
?
-
ATP, ADP, and AMP as well as ITP, UTP, CTP, GTP, TTP, and TDP are not hydrolyzed
-
-
?
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP , supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP , supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP , supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP , supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP , supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP , supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
no significant NTPase or NDPase activity is detected for AtAPY4 except for a slight affinity for CTP. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
-
-
-
additional information
?
-
no significant NTPase or NDPase activity is detected for AtAPY4 except for a slight affinity for CTP. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
-
-
-
additional information
?
-
no significant NTPase or NDPase activity is detected for AtAPY4 except for a slight affinity for CTP. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
-
-
-
additional information
?
-
no significant NTPase or NDPase activity is detected for AtAPY4 except for a slight affinity for CTP. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
-
-
-
additional information
?
-
no significant NTPase or NDPase activity is detected for AtAPY4 except for a slight affinity for CTP. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
-
-
-
additional information
?
-
no significant NTPase or NDPase activity is detected for AtAPY4 except for a slight affinity for CTP. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
-
-
-
additional information
?
-
the clade II member AtAPY6 significantly prefers NDPs but also has significant activities toward NTPs. No activity with CMP and GMP. Broad substrate specificity
-
-
-
additional information
?
-
the clade II member AtAPY6 significantly prefers NDPs but also has significant activities toward NTPs. No activity with CMP and GMP. Broad substrate specificity
-
-
-
additional information
?
-
the clade II member AtAPY6 significantly prefers NDPs but also has significant activities toward NTPs. No activity with CMP and GMP. Broad substrate specificity
-
-
-
additional information
?
-
the clade II member AtAPY6 significantly prefers NDPs but also has significant activities toward NTPs. No activity with CMP and GMP. Broad substrate specificity
-
-
-
additional information
?
-
the clade II member AtAPY6 significantly prefers NDPs but also has significant activities toward NTPs. No activity with CMP and GMP. Broad substrate specificity
-
-
-
additional information
?
-
the clade II member AtAPY6 significantly prefers NDPs but also has significant activities toward NTPs. No activity with CMP and GMP. Broad substrate specificity
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + H2O
AMP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
CTP + H2O
CDP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
very low activity with UDP
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
1 mM, about 3fold stimulation. Ca2+ and Mn2+ are best activators
Mn2+
1 mM, about 3fold stimulation. Ca2+ and Mn2+ are best activators
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-[N-(4-bromophenyl)sulfamoyl]-N-(3-nitrophenyl) benzamide
-
N'-(2-hydroxy-5-methybenzylidene)-2-(1-naphthyl) acetohydrazide
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21.7
recombinant protein lacking transmembrane domain, pH 6.5, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
assay at room temperature
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
AtAPY6 exhibits a defined expression pattern during Arabidopsis thaliana development, namely mature pollen, high expression in mature pollen
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
AtAPY3 probably localizes to the endosome
AtAPY3 contains a single putative N-terminal transmembrane domain typical of type II membrane proteins
-
additional information
cis-Golgi localization. Isozymes AtAPY1, 2, 4, 5 and 7 are probably cis-Golgi resident proteins
isozyme AtAPY1 is able to function as internal Golgi lumenal NDPase. Isozymes AtAPY1, 2, 4, 5 and 7 are probably cis-Golgi resident proteins
isozyme AtAPY2 is able to function as internal Golgi lumenal NDPase. Isozymes AtAPY1, 2, 4, 5 and 7 are probably cis-Golgi resident proteins
isozymes AtAPY1, 2, 4, 5 and 7 are probably cis-Golgi resident proteins
AtAPY6 (clade II) appears to be type a IV-A membrane protein, AtAPY6 appears to possess both an N- and a C-terminal transmembrane domain
isozyme AtAPY5 contains a single putative N-terminal transmembrane domain typical of type II membrane proteins
plant members of the GDA-like clade, such as isozymes AtAPY1 and AtAPY2, are typical type II membrane proteins
the isozyme contains a single putative N-terminal transmembrane domain typical of type II membrane proteins
additional information
the AtAPY3 C-terminal YFP construct results in an internal punctate signal with minimal cis-Golgi marker overlap. Neither the AtAPY3 nor the AtAPY6 constructs significantly overlap with the cis-Golgi marker
-
additional information
the AtAPY3 C-terminal YFP construct results in an internal punctate signal with minimal cis-Golgi marker overlap. Neither the AtAPY3 nor the AtAPY6 constructs significantly overlap with the cis-Golgi marker
-
additional information
the AtAPY3 C-terminal YFP construct results in an internal punctate signal with minimal cis-Golgi marker overlap. Neither the AtAPY3 nor the AtAPY6 constructs significantly overlap with the cis-Golgi marker
-
additional information
the AtAPY3 C-terminal YFP construct results in an internal punctate signal with minimal cis-Golgi marker overlap. Neither the AtAPY3 nor the AtAPY6 constructs significantly overlap with the cis-Golgi marker
-
additional information
the AtAPY3 C-terminal YFP construct results in an internal punctate signal with minimal cis-Golgi marker overlap. Neither the AtAPY3 nor the AtAPY6 constructs significantly overlap with the cis-Golgi marker
-
additional information
the AtAPY3 C-terminal YFP construct results in an internal punctate signal with minimal cis-Golgi marker overlap. Neither the AtAPY3 nor the AtAPY6 constructs significantly overlap with the cis-Golgi marker
-
additional information
not detected at the plasma membrane or in the extracellular space
-
additional information
neither the AtAPY3 nor the AtAPY6 constructs significantly overlap with the cis-Golgi marker
-
additional information
neither the AtAPY3 nor the AtAPY6 constructs significantly overlap with the cis-Golgi marker
-
additional information
neither the AtAPY3 nor the AtAPY6 constructs significantly overlap with the cis-Golgi marker
-
additional information
neither the AtAPY3 nor the AtAPY6 constructs significantly overlap with the cis-Golgi marker
-
additional information
neither the AtAPY3 nor the AtAPY6 constructs significantly overlap with the cis-Golgi marker
-
additional information
neither the AtAPY3 nor the AtAPY6 constructs significantly overlap with the cis-Golgi marker
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the seven member Arabidopsis apyrase family contains representatives in each clade and are clustered into the AtAPY1-2 clade I (GDA1-like), the AtAPY3-6 (clade II) and AtAPY7 in clade III. Isozymes AtAPY3, AtAPY4, and AtAPY5 occur as recurrent tandem duplications and share 68% identity, all three are expressed during Arabidopsis thaliana development with AtAPY3 predominately in the roots and both AtAPY4/AtAPY5 in the vegetative rosette. The protein structure of the seven Arabidopsis apyrase proteins outline the apyrase conserved domain GDA1_CD39 and predicted transmembrane helices
metabolism
roles of the Arabidopsis thaliana apyrase family in regulating endomembrane NDP/NMP homoeostasis, overview. The AtAPY1-6 Arabidopsis thaliana enzymes all exhibit classic apyrase-like NTPase and/or NDPases activities, with an absence of NMP activity
physiological function
the Arabidopsis apyrases family members have possible roles in regulating endomembrane NDP/NMP (nucleoside monophosphate) homoeostasis
evolution
malfunction
metabolism
roles of the Arabidopsis thaliana apyrase family in regulating endomembrane NDP/NMP homoeostasis, overview. The AtAPY1-6 Arabidopsis thaliana enzymes all exhibit classic apyrase-like NTPase and/or NDPases activities, with an absence of NMP activity
physiological function
evolution
the seven member Arabidopsis apyrase family contains representatives in each clade and are clustered into the AtAPY1-2 clade I (GDA1-like), the AtAPY3-6 (clade II) and AtAPY7 in clade III. Isozymes AtAPY3, AtAPY4, and AtAPY5 occur as recurrent tandem duplications and share 68% identity, all three are expressed during Arabidopsis thaliana development with AtAPY3 predominately in the roots and both AtAPY4/AtAPY5 in the vegetative rosette. The protein structure of the seven Arabidopsis apyrase proteins outline the apyrase conserved domain GDA1_CD39 and predicted transmembrane helices
evolution
the seven member Arabidopsis apyrase family contains representatives in each clade and are clustered into the AtAPY1-2 clade I (GDA1-like), the AtAPY3-6 (clade II) and AtAPY7 in clade III. The clade I (GDA-like) Arabidopsis members (AtAPY1 andAtAPY2) form a distinct clade with the other characterized plant apyrases, human apyrases and the yeast GDA1 enzyme. The protein structure of the seven Arabidopsis apyrase proteins outline the apyrase conserved domain GDA1_CD39 and predicted transmembrane helices
evolution
the seven member Arabidopsis apyrase family contains representatives in each clade and are clustered into the AtAPY1-2 clade I (GDA1-like), the AtAPY3-6 (clade II) and AtAPY7 in clade III. The protein structure of the seven Arabidopsis apyrase proteins outline the apyrase conserved domain GDA1_CD39 and predicted transmembrane helices
malfunction
-
suppression of apyrase expression affects the regulation of stomatal aperture
malfunction
-
single knockout mutants of isoforms APY6 and 7 display a minor change in pollen exine pattern without obvious change in fertility, while double knockout mutants of APY6 and 7 display severe defects in pollen exine pattern, deformed pollen shape and reduced male fertility
malfunction
-
the suppression of isoforms APY1 and APY2 blocks growth in Arabidopsis thaliana. The basal halves of apyrase-suppressed hypocotyls contain considerably lower free indole-3-acetic acid levels when compared with wild type plants, and disrupted auxin transport in the apyrase-suppressed roots is reflected by their significant morphological abnormalities, such as unusual root hair distribution and meristematic disorganization. A critical step connecting apyrase suppression to growth suppression is the inhibition of polar auxin transport
malfunction
apy2 single knockout roots show increased skewing compared with wild-type roots when grown on phytagel
malfunction
immunochemical and genetic suppression of AtAPY1 and AtAPY2 results in an increase in extracellular ATP
malfunction
the primary roots of seedlings overexpressing APY1 show less skewing than wild-type plants. Plants suppressed in their expression of APY1 show more skewing than wild-type plants. The primary roots of apy1 single knockout (APY1 KO) seedlings (Ws background) exhibit increased rightward skewing and have an HGI that is significantly higher than that of wild-type roots. The apy1 single knockout roots show increased skewing compared with wild-type roots when grown on phytagel. 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. Apy1 mutant roots show altered cell file rotation. Phenotypes, overview
physiological function
-
expression of the two apyrase isozymes in Arabidopsis thaliana, APY1 and APY2, is strongly correlated with cell growth and secretory activity. Ectoapyrases and extracellular nucleotides play key roles in regulating stomatal functions, overview
physiological function
-
apyrase enzyme blocks abscisic acid-induced stomatal closure
physiological function
isoform APY1 exerts its growth and developmental effects by possibly regulating glycosylation reactions in the Golgi
physiological function
-
isoforms APY6 and AtAPY7 play an important role in exine development of pollen grains, possibly through regulating the production of key polysaccharides needed for proper assembly of the exine layer
physiological function
-
the basal halves of apyrase-suppressed hypocotyls contain considerably lower free indole-3-acetic acid levels when compared with wild type plants, and disrupted auxin transport in the apyrase-suppressed roots is reflected by their significant morphological abnormalities, such as unusual root hair distribution and meristematic disorganization
physiological function
biochemical analysis of AtAPY4 results in the lowest NDPase activates measured, exhibiting a substrate preference for CTP. But even with this reduced NDPase activity, the isozyme's localization to the Golgi lumen probably assists in the positive complementation phenotype in Saccharomyces cerevisiae DELTAgda1DELTAynd1 dKO. The Arabidopsis apyrases family members have possible roles in regulating endomembrane NDP/NMP (nucleoside monophosphate) homoeostasis
physiological function
both AtAPY1 and AtAPY2 have been shown to play numerous physiological roles in pollen development, vegetative growth and stomata opening/closure. AtAPY1 and AtAPY2 function as plant endo-apyrases and are necessary for lumenal glycosylation. The Arabidopsis apyrases family members have possible roles in regulating endomembrane NDP/NMP (nucleoside monophosphate) homoeostasis. AtAPY 1 and AtAPY2 are able to function as internal Golgi lumenal NDPases
physiological function
ectoapyrases (ect-NTPDases) function to decrease levels of extracellular ATP and ADP in animals and plants. Ectopic expression of a pea ectoapyrase, psNTP9, enhances growth in Arabidopsis thaliana seedlings and the overexpression of the two Arabidopsis apyrases most closely related to psNTP9 enhances auxin transport and growth in Arabidopsis thaliana. Ectopic expression of psNTP9 can promote a more extensive root system architecture (RSA) in Arabidopsis thaliana. Transgenic Arabidopsis thaliana seedlings have longer primary roots, more lateral roots, and more and longer root hairs than wild-type plants. Transcriptomic analyses reveal gene expression changes in the transgenic plants that help account for their enhanced RSA and improved drought tolerance
physiological function
ectoapyrases (ecto-NTPDases) function to decrease levels of extracellular ATP and ADP in animals and plants. Ectopic expression of a pea ectoapyrase, psNTP9, enhances growth in Arabidopsis thaliana seedlings and the overexpression of the two Arabidopsis apyrases most closely related to psNTP9 enhances auxin transport and growth in Arabidopsis thaliana. Ectopic expression of psNTP9 can promote a more extensive root system architecture (RSA) in Arabidopsis thaliana. Transgenic Arabidopsis thaliana seedlings have longer primary roots, more lateral roots, and more and longer root hairs than wild-type plants. Transcriptomic analyses reveal gene expression changes in the transgenic plants that help account for their enhanced RSA and improved drought tolerance
physiological function
isozyme AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, demonstrating that the enzyme is also able to function as internal Golgi lumenal NDPases. Analysis of atapy6 mutants indicate a minor role in pollen development associated with abnormal exine patterning. An endoapyrase role for AtAPY6. The Arabidopsis apyrases family members have possible roles in regulating endomembrane NDP/NMP (nucleoside monophosphate) homoeostasis
physiological function
modulation of root skewing in Arabidopsis thaliana by apyrases and extracellular ATP. Skewing is induced by touch stimuli which the roots experience as they grow along the surface. Touch stimuli also induce the release of extracellular ATP (eATP) into the plant's extracellular matrix, and two apyrases (NTPDases) in Arabidopsis thaliana, APY1 and APY2, can help regulate the concentration of eATP. Exogenous application of ATP or ATPgammaS also increases skewing in wild-type roots, which can be blocked by co-incubation with a purinergic receptor antagonist. APY1 and, to a lesser extent, APY2 help control root skewing in Arabidopsis thaliana, and application of extracellular nucleotides also affects this directional growth response of roots. Treatment with ATP and ATPgammaS increases root skewing. Blocking auxin transport with 1-N-naphthylphthalamic acid (NPA) also increases root skewing
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). APY3_ARATH
483
1
53426
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
x * 80000, protein with green fluorescent protein tag, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 80000, protein with green fluorescent protein tag, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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. 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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene AtAPY3, sequence comparisons and phylogenetic analysis, apyrase members AtAPY3, AtAPY4 and AtAPY5 are recurrent tandem gene duplications on chromosome 1, recombinant expression of C-terminally YFP-tagged isozyme AtAPY3 in Arabidopsis thaliana resulting in an internal punctate signal with minimal cis-Golgi marker overlap
expressed in Arabidopsis thaliana, fused to a SNAP-(O6-alkylguanine-DNA alkyltransferase)-tag, green fluorescent protein or yellow fluorescent protein
expression of the full-length protein and a soluble form without the transmembrane domain near the N-terminus in HEK-293 cells
gene APY2, real-time PCR enzyme expression analysis by RNAi
gene AtAPY1, sequence comparisons and phylogenetic analysis
gene AtAPY2, sequence comparisons and phylogenetic analysis
gene AtAPY4, sequence comparisons and phylogenetic analysis, apyrase members AtAPY3, AtAPY4 and AtAPY5 are recurrent tandem gene duplications on chromosome 1, recombinant expression of YFP-tagged isozyme AtAPY4 in Arabidopsis thaliana in the cis-Golgi of rosette leaves
gene AtAPY5, apyrase members AtAPY3, AtAPY4 and AtAPY5 are recurrent tandem gene duplications on chromosome 1, sequence comparisons and phylogenetic analysis
gene AtAPY6, sequence comparisons and phylogenetic analysis. recombinant expression of C-terminally YFP-tagged isozyme AtAPY6 in Arabidopsis thaliana in colocalization with the endoplasmic reticulum marker
isozymes APY1 and APY2, expression analysis, APY1 and APY2 promoter activity is high under conditions that induced stomata opening
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APY expression in guard cell protoplasts rises quickly when these cells are moved from darkness into light
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Clark, G.; Fraley, D.; Steinebrunner, I.; Cervantes, A.; Onyirimba, J.; Liu, A.; Torres, J.; Tang, W.; Kim, J.; Roux, S.J.
Extracellular nucleotides and apyrases regulate stomatal aperture in Arabidopsis
Plant Physiol.
156
1740-1753
2011
Arabidopsis thaliana
Schiller, M.; Massalski, C.; Kurth, T.; Steinebrunner, I.
The Arabidopsis apyrase AtAPY1 is localized in the Golgi instead of the extracellular space
BMC Plant Biol.
12
123
2012
Arabidopsis thaliana (Q9SQG2)
Yang, J.; Wu, J.; Romanovicz, D.; Clark, G.; Roux, S.J.
Co-regulation of exine wall patterning, pollen fertility and anther dehiscence by Arabidopsis apyrases 6 and 7
Plant Physiol. Biochem.
69
62-73
2013
Arabidopsis thaliana
Liu, X.; Wu, J.; Clark, G.; Lundy, S.; Lim, M.; Arnold, D.; Chan, J.; Tang, W.; Muday, G.K.; Gardner, G.; Roux, S.J.
Role for apyrases in polar auxin transport in Arabidopsis
Plant Physiol.
160
1985-1995
2012
Arabidopsis thaliana
Clark, G.; Darwin, C.; Mehta, V.; Jackobs, F.; Perry, T.; Hougaard, K.; Roux, S.
Effects of chemical inhibitors and apyrase enzyme further document a role for apyrases and extracellular ATP in the opening and closing of stomates in Arabidopsis
Plant Signal. Behav.
8
e26093
2013
Arabidopsis thaliana
Massalski, C.; Bloch, J.; Zebisch, M.; Steinebrunner, I.
The biochemical properties of the Arabidopsis ecto-nucleoside triphosphate diphosphohydrolase AtAPY1 contradict a direct role in purinergic signaling
PLoS ONE
10
e0115832
2015
Arabidopsis thaliana (Q9SQG2)
Chiu, T.Y.; Lao, J.; Manalansan, B.; Loque, D.; Roux, S.J.; Heazlewood, J.L.
Biochemical characterization of Arabidopsis APYRASE family reveals their roles in regulating endomembrane NDP/NMP homoeostasis
Biochem. J.
472
43-54
2015
no activity by Arabidopsis thaliana isozyme AtAPY7, Arabidopsis thaliana (O80612), Arabidopsis thaliana (Q6NQA8), Arabidopsis thaliana (Q8H1D8), Arabidopsis thaliana (Q9SPM5), Arabidopsis thaliana (Q9SQG2), Arabidopsis thaliana (Q9XI62)
Veerappa, R.; Slocum, R.D.; Siegenthaler, A.; Wang, J.; Clark, G.; Roux, S.J.
Ectopic expression of a pea apyrase enhances root system architecture and drought survival in Arabidopsis and soybean
Plant Cell Environ.
42
337-353
2019
Pisum sativum (Q9FEA6), Pisum sativum, Arabidopsis thaliana (Q9SPM5), Arabidopsis thaliana (Q9SQG2), Arabidopsis thaliana ecotype Columbia, CS907 (Q9SPM5), Arabidopsis thaliana ecotype Columbia, CS907 (Q9SQG2)
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