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EC Tree
IUBMB Comments Also acts on UDP but not on other nucleoside diphosphates and triphosphates.
The enzyme appears in viruses and cellular organisms
Synonyms
gdap1, e-ntpdase, ecto-nucleoside triphosphate diphosphohydrolase, udpase, guanosine diphosphatase, gdp1p,
more
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ecto-nucleoside triphosphate diphosphohydrolase
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gda1p (GDA1 gene product)
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-
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phosphatase, guanosine di-
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-
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GDPase
-
-
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guanosine diphosphatase
-
-
-
-
guanosine diphosphatase
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-
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GDP + H2O = GMP + phosphate
GDP + H2O = GMP + phosphate
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-
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GDP + H2O = GMP + phosphate
stoichiometry of reaction
-
GDP + H2O = GMP + phosphate
also acts on UDP
-
GDP + H2O = GMP + phosphate
also acts on UDP but not on other nucleoside diphosphates and triphosphates
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hydrolysis of diphosphate bonds
-
-
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hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
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-
hydrolysis of phosphoric ester
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GDP phosphohydrolase
Also acts on UDP but not on other nucleoside diphosphates and triphosphates.
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ADP + H2O
AMP + phosphate
ATP + H2O
ADP + phosphate
-
low activity
-
-
?
GDP + H2O
5'-GMP + phosphate
GDP + H2O
GMP + phosphate
IDP + H2O
IMP + phosphate
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
AMP + adenosine 5'-tetraphosphate
-
reaction of EC 3.6.1.17
-
?
UDP + H2O
UMP + phosphate
additional information
?
-
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
low activity
-
-
?
GDP + H2O
5'-GMP + phosphate
-
best substrate
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?
GDP + H2O
5'-GMP + phosphate
-
hydrolyzes free GDP, unable to hydrolyze GDP bound to eIF-2, eukaryotic initiation factor 2, and unable to catalyze the exchange of bound GDP with GTP even in the presence of relatively high molar excess of GTP and Met-tRNA
-
?
GDP + H2O
5'-GMP + phosphate
-
possible biological function in maintaining the cellular pool of GTP-GDP
-
?
GDP + H2O
5'-GMP + phosphate
-
GTP is an important steric effector in many biological systems, GDP a potent inhibitor: GDPase activity could be involved in preventing potential inhibitory levels of GDP from accumulating
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?
GDP + H2O
5'-GMP + phosphate
-
PCPH and mt-PCPH proteins have intrinsic GDPase activity, are GDPases
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?
GDP + H2O
5'-GMP + phosphate
-
PCPH and mt-PCPH proteins have intrinsic GDPase activity, are GDPases
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?
GDP + H2O
5'-GMP + phosphate
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PCPH and mt-PCPH proteins have intrinsic GDPase activity, are GDPases
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?
GDP + H2O
5'-GMP + phosphate
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-
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?
GDP + H2O
5'-GMP + phosphate
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-
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?
GDP + H2O
5'-GMP + phosphate
-
best substrate
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?
GDP + H2O
5'-GMP + phosphate
-
best substrate
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?
GDP + H2O
5'-GMP + phosphate
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best substrate
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?
GDP + H2O
5'-GMP + phosphate
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highly specific for GDP
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?
GDP + H2O
5'-GMP + phosphate
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highly specific for GDP
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?
GDP + H2O
5'-GMP + phosphate
-
cleaves GDP that originates from GDP-mannose after mannosylation of glycoproteins in Golgi complex
-
?
GDP + H2O
5'-GMP + phosphate
-
GDP is a reaction product following outer-chain mannosylation of luminal proteins and inhibitor of mannosyltransferases. It is hypothesized that GMP then returns to the cytosol. GDPase presumably serves as an essential function in processing of yeast glycoproteins
-
?
GDP + H2O
5'-GMP + phosphate
-
GDPase plays a role in O- and N-mannosylation of proteins such as chitinase and carboxypeptidase Y and glycosylation of external invertase and of mannosylation of inositolphosphorylceramides
-
?
GDP + H2O
5'-GMP + phosphate
-
GDP is known to be an inhibitor of mannosylation reactions in the Golgi lumen, removal of GDP by conversion to GMP, the latter not being an inhibitor of these reactions, would allow mannosylation to proceed
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?
GDP + H2O
5'-GMP + phosphate
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guanosine diphosphatase is required for protein and sphingolipid glycosylation in the Golgi lumen
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?
GDP + H2O
5'-GMP + phosphate
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best substrate
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?
GDP + H2O
GMP + phosphate
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-
-
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?
GDP + H2O
GMP + phosphate
-
best substrate
-
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?
GDP + H2O
GMP + phosphate
-
-
-
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?
GDP + H2O
GMP + phosphate
preferred substrate
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-
?
GDP + H2O
GMP + phosphate
GDP hydrolysis occurs in the Golgi lumen to give GMP, which is required as antiporter for GDP-mannose transport into the Golgi lumen
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-
?
GDP + H2O
GMP + phosphate
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-
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?
GDP + H2O
GMP + phosphate
the enzyme's GDPase activity plays a role in guanosine nucleotide sugar transport into Golgi vesicles
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-
?
GDP + H2O
GMP + phosphate
preferred substrate in presence of Ca2+ or Mn2+
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?
GDP + H2O
GMP + phosphate
-
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-
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?
GDP + H2O
GMP + phosphate
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?
GDP + H2O
GMP + phosphate
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the enzyme has a main role in protein glycosylation, enzyme deficiency leads to N-glycosylation defects of invertase
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?
GDP + H2O
GMP + phosphate
-
-
-
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?
IDP + H2O
IMP + phosphate
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-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
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?
IDP + H2O
IMP + phosphate
-
-
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?
IDP + H2O
IMP + phosphate
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?
UDP + H2O
UMP + phosphate
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?
UDP + H2O
UMP + phosphate
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much lower affinity than for GDP
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?
UDP + H2O
UMP + phosphate
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-
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?
UDP + H2O
UMP + phosphate
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?
UDP + H2O
UMP + phosphate
-
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?
UDP + H2O
UMP + phosphate
the enzyme's UDPase activity plays a role in uridine nucleotide sugar transport into Golgi vesicles
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?
UDP + H2O
UMP + phosphate
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?
UDP + H2O
UMP + phosphate
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?
UDP + H2O
UMP + phosphate
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about 21% as active with UDP compared to GDP
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?
UDP + H2O
UMP + phosphate
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about 10% as active with UDP compared to GDP
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?
UDP + H2O
UMP + phosphate
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in the presence of 10 mM Mn2+: 3fold activation of its activity toward UDP, but not GDP, compared to activation by 10 mM Ca2+
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?
UDP + H2O
UMP + phosphate
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-
-
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?
UDP + H2O
UMP + phosphate
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about 10% as active with UDP compared to GDP
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?
UDP + H2O
UMP + phosphate
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in the presence of 10 mM Mn2+: 3fold activation of its activity toward UDP, but not GDP, compared to activation by 10 mM Ca2+
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?
additional information
?
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ATP, ADP, CTP, CDP, GTP, ITO, TTP, UTP and TDP are no substrates
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additional information
?
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substrate specificity
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?
additional information
?
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hydrolyzes free GDP, unable to hydrolyze GDP bound to eIF-2, eukaryotic initiation factor 2, and unable to catalyze the exchange of bound GDP with GTP even in the presence of relatively high molar excess of GTP and Met-tRNA
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?
additional information
?
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only GDP and UDP are hydrolyzed, no activity with other nucleoside diphosphates and triphosphates, no activity with CDP, ADP, GTP, ATP
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?
additional information
?
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physiological function, role in O- and N-glycosylation, and cell and hyphae morphogenesis, affects the cell surface charge and phosphate content, enzyme is not required for the adhesion of Candida albicans to epithelial cells, overview
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?
additional information
?
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physiological function, GMP and UMP are required as antiporters for guanosine and uridine nucleotide sugar transport into the Golgi lumen, involved in O-glycosylation
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?
additional information
?
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physiological function, GMP and UMP are required as antiporters for guanosine and uridine nucleotide sugar transport into the Golgi lumen, involved in O-glycosylation
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?
additional information
?
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no activity with other nucleoside phosphates
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?
additional information
?
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no activity with other nucleoside phosphates
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?
additional information
?
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substrate specificity
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?
additional information
?
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substrate specificity
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?
additional information
?
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ADP: not a substrate
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?
additional information
?
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CDP: not a substrate
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?
additional information
?
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no or only very poor activity with other nucleotide substrates than GDP and UDP
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?
additional information
?
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less than 2% of maximum activity with other nucleoside di-, mono-, and triphosphates
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?
additional information
?
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guanosine diphosphatase is required for protein and sphingolipid glycosylation in the Golgi lumen
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-
?
additional information
?
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-
GDPase is required to complete O-glycosylation of proteins
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-
?
additional information
?
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GDPase not essential for cell viability and growth
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-
?
additional information
?
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-
GDPase plays a role in O- and N-mannosylation of proteins such as chitinase and carboxypeptidase Y and glycosylation of external invertase and of mannosylation of inositolphosphorylceramides and in synthesis of cell wall
-
-
?
additional information
?
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GDPase plays an important role in mannosylation of proteins and lipids by regulating the amount of GDP-mannose available in Golgi lumen
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-
?
additional information
?
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GDPase plays an important role in mannosylation of proteins and lipids by regulating the amount of GDP-mannose available in Golgi lumen
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?
additional information
?
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GDPase plays an important role in mannosylation of proteins and lipids by regulating the amount of GDP-mannose available in Golgi lumen
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?
additional information
?
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necessary for Golgi-specific glycosylation reactions
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?
additional information
?
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GDPase has an important role in glycosylation reactions in Golgi lumen
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?
additional information
?
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GDPase has an important role in glycosylation reactions in Golgi lumen
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?
additional information
?
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GDPase has an important role in glycosylation reactions in Golgi lumen
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?
additional information
?
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role in mannosylation
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?
additional information
?
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role in mannosylation
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?
additional information
?
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role in mannosylation
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?
additional information
?
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substrate specificity
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?
additional information
?
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less than 2% of maximum activity with other nucleoside di-, mono-, and triphosphates
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-
?
additional information
?
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bifunctional enzyme showing GDPase and uridine diphosphatase activities in vitro
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?
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GDP + H2O
5'-GMP + phosphate
GDP + H2O
GMP + phosphate
UDP + H2O
UMP + phosphate
the enzyme's UDPase activity plays a role in uridine nucleotide sugar transport into Golgi vesicles
-
-
?
additional information
?
-
GDP + H2O
5'-GMP + phosphate
-
possible biological function in maintaining the cellular pool of GTP-GDP
-
?
GDP + H2O
5'-GMP + phosphate
-
GTP is an important steric effector in many biological systems, GDP a potent inhibitor: GDPase activity could be involved in preventing potential inhibitory levels of GDP from accumulating
-
?
GDP + H2O
5'-GMP + phosphate
-
-
-
?
GDP + H2O
5'-GMP + phosphate
-
cleaves GDP that originates from GDP-mannose after mannosylation of glycoproteins in Golgi complex
-
?
GDP + H2O
5'-GMP + phosphate
-
GDP is a reaction product following outer-chain mannosylation of luminal proteins and inhibitor of mannosyltransferases. It is hypothesized that GMP then returns to the cytosol. GDPase presumably serves as an essential function in processing of yeast glycoproteins
-
?
GDP + H2O
5'-GMP + phosphate
-
GDPase plays a role in O- and N-mannosylation of proteins such as chitinase and carboxypeptidase Y and glycosylation of external invertase and of mannosylation of inositolphosphorylceramides
-
?
GDP + H2O
5'-GMP + phosphate
-
GDP is known to be an inhibitor of mannosylation reactions in the Golgi lumen, removal of GDP by conversion to GMP, the latter not being an inhibitor of these reactions, would allow mannosylation to proceed
-
?
GDP + H2O
5'-GMP + phosphate
-
guanosine diphosphatase is required for protein and sphingolipid glycosylation in the Golgi lumen
-
?
GDP + H2O
GMP + phosphate
-
-
-
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?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
GDP hydrolysis occurs in the Golgi lumen to give GMP, which is required as antiporter for GDP-mannose transport into the Golgi lumen
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-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
the enzyme's GDPase activity plays a role in guanosine nucleotide sugar transport into Golgi vesicles
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
the enzyme has a main role in protein glycosylation, enzyme deficiency leads to N-glycosylation defects of invertase
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
additional information
?
-
physiological function, role in O- and N-glycosylation, and cell and hyphae morphogenesis, affects the cell surface charge and phosphate content, enzyme is not required for the adhesion of Candida albicans to epithelial cells, overview
-
-
?
additional information
?
-
physiological function, GMP and UMP are required as antiporters for guanosine and uridine nucleotide sugar transport into the Golgi lumen, involved in O-glycosylation
-
-
?
additional information
?
-
-
physiological function, GMP and UMP are required as antiporters for guanosine and uridine nucleotide sugar transport into the Golgi lumen, involved in O-glycosylation
-
-
?
additional information
?
-
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guanosine diphosphatase is required for protein and sphingolipid glycosylation in the Golgi lumen
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?
additional information
?
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GDPase is required to complete O-glycosylation of proteins
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?
additional information
?
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GDPase not essential for cell viability and growth
-
-
?
additional information
?
-
-
GDPase plays a role in O- and N-mannosylation of proteins such as chitinase and carboxypeptidase Y and glycosylation of external invertase and of mannosylation of inositolphosphorylceramides and in synthesis of cell wall
-
-
?
additional information
?
-
-
GDPase plays an important role in mannosylation of proteins and lipids by regulating the amount of GDP-mannose available in Golgi lumen
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-
?
additional information
?
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GDPase plays an important role in mannosylation of proteins and lipids by regulating the amount of GDP-mannose available in Golgi lumen
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?
additional information
?
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GDPase plays an important role in mannosylation of proteins and lipids by regulating the amount of GDP-mannose available in Golgi lumen
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?
additional information
?
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necessary for Golgi-specific glycosylation reactions
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?
additional information
?
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GDPase has an important role in glycosylation reactions in Golgi lumen
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?
additional information
?
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GDPase has an important role in glycosylation reactions in Golgi lumen
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?
additional information
?
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GDPase has an important role in glycosylation reactions in Golgi lumen
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?
additional information
?
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role in mannosylation
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?
additional information
?
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role in mannosylation
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?
additional information
?
-
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role in mannosylation
-
-
?
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divalent cations
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required
Fe2+
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less than 10% activation
additional information
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-
Ca2+
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Ca2+ strongly activates the enzyme
Ca2+
stimulates both GDPase and UDPase activity
Ca2+
-
required for maximal activity
Ca2+
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highly dependent on
Mg2+
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Mg2+ strongly activates the enzyme. 1 mM is used in assay conditions
Mn2+
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Mn2+ strongly activates the enzyme
Mn2+
stimulates, preferred metal ion
Mn2+
stimulates both GDPase and UDPase activity, stimulates UDPase activity by 5fold compared to stimulation with Ca2+
Mn2+
-
activation, enzyme with Mn2+ is 60-95% as active as compared with Ca2+
Mn2+
-
in the presence of 10 mM Mn2+: 3fold activation of its activity toward UDP, but not GDP, compared to activation by 10 mM Ca2+
Mn2+
-
highly dependent on, best at 20 mM
Ni2+
-
Ni2+ has no effect on the enzyme activity
Ni2+
-
less than 10% activation
Zn2+
-
Zn2+ slightly activates the enzyme
Zn2+
-
less than 10% activation
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azide
-
42% inhibition at 10 mM
fluoride
-
27% inhibition at 10 mM
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,4,5,6-pentaphosphate
competitive
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
competitive
inositol 4-butyl-1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
competitive
vanadate
-
54% inhibition at 1 mM
additional information
-
not inhibited by NGXT191 and dithiothreitol
-
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Calmodulin
-
5fold increase of activity at 0.001 mM
Triton X-100
-
0.1% Triton X-100: 6-10fold activation
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0.166
IDP
-
at pH 6.5 and 37°C
0.0744
UDP
-
at pH 6.5 and 37°C
0.0597
GDP
-
at pH 6.5 and 37°C
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0.00011
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,4,5,6-pentaphosphate
pH not specified in the publication, temperature not specified in the publication
0.00027
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
pH not specified in the publication, temperature not specified in the publication
0.000023
inositol 4-butyl-1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
pH not specified in the publication, temperature not specified in the publication
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0.33
-
unpurified enzyme, at pH 6.5 and 37°C
21.7
-
after 70fold purification, at pH 6.5 and 37°C
additional information
-
-
additional information
enzyme activity of wild-type and mutant enzyme in presence of Ca2+ or Mn2+ with substrates GDP or UDP
additional information
-
enzyme activity of wild-type and mutant enzyme in presence of Ca2+ or Mn2+ with substrates GDP or UDP
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7.4 - 8.2
-
broad pH optimum
7.5
-
assay at
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5.5 - 9.5
-
the enzyme shows the highest and same level of activity from pH 5.5 to 9.5. There is a significant drop in activity at pH 5.0 and the activity decreases further with increasing acidity. At pH 4.0 the activity is down to 3% of the highest activity observed
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30
assay at
37
-
assay at
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ecotype Wassilewskija
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brenda
calf
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brenda
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brenda
enzyme KlGdap1
SwissProt
brenda
Syrian hamster, normal and transforming PCPH proteins: PCPH, PCPH proto-oncogene and mt-PCPH, PCPH oncogene having guanosine diphosphatase activity
-
-
brenda
normal and transforming PCPH proteins: PCPH, PCPH proto-oncogene and mt-PCPH, PCPH oncogene having guanosine diphosphatase activity
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-
brenda
-
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-
brenda
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brenda
-
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brenda
gene gda1
SwissProt
brenda
-
SwissProt
brenda
normal and transforming PCPH proteins: PCPH, PCPH proto-oncogene and mt-PCPH, PCPH oncogene having guanosine diphosphatase activity
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-
brenda
-
-
-
brenda
strains G2-25, wild-type and null-mutants for GDA-1
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-
brenda
wild-type and mutants
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-
brenda
wild-type and null mutant for guanosine diphosphatase
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-
brenda
-
-
-
brenda
several strains, gene gdp1+
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-
brenda
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-
brenda
-
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brenda
-
-
brenda
-
-
brenda
-
-
brenda
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brenda
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brenda
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brenda
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Golgi localization
brenda
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distribution in multiple compartments
brenda
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brenda
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large catalytic lumenal domain
brenda
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brenda
with the catalytic domain being lumenal
brenda
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brenda
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brenda
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Golgi-like vesicles
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brenda
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Golgi-like vesicles
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brenda
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brenda
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type II transmembrane protein with a single hydrophobic domain, which acts as an uncleaved signal sequence and membrane anchor, and is preceded by a short hydrophilic cytosolic tail
brenda
-
type II membrane protein with a single hydrophobic stretch acting as an uncleaved signal sequence and anchor to the membrane preceded by a short hydrophilic, cytosolic tail
brenda
-
type II integral membrane glycoprotein with a short amino-terminal cytoplasmic domain, which is not sufficient for Golgi localization, a single transmembrane domain , and a large catalytic lumenal domain, which is required for activity
brenda
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brenda
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brenda
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brenda
additional information
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subcellular localization
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brenda
additional information
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subcellular localization
-
brenda
additional information
-
Golgi localization
-
brenda
additional information
-
Golgi localization
-
brenda
additional information
-
Golgi localization
-
brenda
additional information
-
Golgi localization
-
brenda
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GDA1_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
503
1
55250
Swiss-Prot
Secretory Pathway (Reliability: 3 )
GDA1_CANAL
Candida albicans (strain SC5314 / ATCC MYA-2876)
599
1
65953
Swiss-Prot
Secretory Pathway (Reliability: 2 )
GDA1_KLULA
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
522
1
56863
Swiss-Prot
Secretory Pathway (Reliability: 3 )
GDA1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
556
1
61589
Swiss-Prot
Secretory Pathway (Reliability: 2 )
GDA1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
518
1
56822
Swiss-Prot
Secretory Pathway (Reliability: 3 )
ENTP4_HUMAN
616
2
70255
Swiss-Prot
Secretory Pathway (Reliability: 5 )
ENTP4_MOUSE
613
2
69746
Swiss-Prot
Secretory Pathway (Reliability: 5 )
M5C0Z3_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
546
1
59953
TrEMBL
other Location (Reliability: 4 )
Q9VQI8_DROME
464
1
51120
TrEMBL
other Location (Reliability: 4 )
A3LQ03_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
565
1
61439
TrEMBL
Secretory Pathway (Reliability: 4 )
Q8IPZ6_DROME
271
0
30025
TrEMBL
other Location (Reliability: 1 )
B8MK47_TALSN
Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006)
547
1
59716
TrEMBL
Mitochondrion (Reliability: 5 )
A0A8J8WAV5_9EURO
557
0
60869
TrEMBL
other Location (Reliability: 3 )
A0A8J5BSG0_9ASCO
402
0
45197
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A0F4YKH3_TALEM
681
0
74764
TrEMBL
other Location (Reliability: 5 )
A4H5Z8_LEIBR
691
1
74840
TrEMBL
Secretory Pathway (Reliability: 2 )
K0KWT5_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
614
1
66400
TrEMBL
Secretory Pathway (Reliability: 3 )
A4HUC4_LEIIN
677
1
73579
TrEMBL
Secretory Pathway (Reliability: 1 )
Q4QHK3_LEIMA
674
1
73394
TrEMBL
Secretory Pathway (Reliability: 1 )
W1Q7Y3_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
576
1
62783
TrEMBL
Secretory Pathway (Reliability: 2 )
Q9VGN8_DROME
419
1
47679
TrEMBL
Mitochondrion (Reliability: 3 )
A0A1U7Q2R2_MESAU
428
2
47363
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A1W2TLE0_ROSNE
546
1
59987
TrEMBL
other Location (Reliability: 4 )
A0A8J5BKP1_9ASCO
402
0
45078
TrEMBL
Secretory Pathway (Reliability: 1 )
A0A084FX85_PSEDA
551
1
60543
TrEMBL
other Location (Reliability: 4 )
B9WEJ2_CANDC
Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841)
594
1
65531
TrEMBL
Secretory Pathway (Reliability: 2 )
A0A0B7FNH9_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
643
0
70570
TrEMBL
Mitochondrion (Reliability: 4 )
A3GH82_PICST
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
678
1
76318
TrEMBL
other Location (Reliability: 2 )
A0A0F8CTY7_CERFI
580
1
63007
TrEMBL
other Location (Reliability: 4 )
C5PCP9_COCP7
Coccidioides posadasii (strain C735)
552
1
60690
TrEMBL
other Location (Reliability: 3 )
A0A8J5EBH5_9ASCO
534
0
59333
TrEMBL
other Location (Reliability: 2 )
A0A3S7WR18_LEIDO
677
1
73487
TrEMBL
Secretory Pathway (Reliability: 1 )
M9PBV2_DROME
524
1
57863
TrEMBL
other Location (Reliability: 4 )
O76268_DROME
461
1
50845
TrEMBL
other Location (Reliability: 4 )
A0A8J5B8F4_9ASCO
534
0
59335
TrEMBL
other Location (Reliability: 2 )
A0A088RJK1_9TRYP
691
1
74782
TrEMBL
Secretory Pathway (Reliability: 3 )
A0A3G2SAF1_9BASI
552
1
60810
TrEMBL
Secretory Pathway (Reliability: 2 )
NUDT3_HUMAN
172
0
19471
Swiss-Prot
other Location (Reliability: 3 )
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120000
-
functional target size, irradiation of membranes from wild-type and gda1 null mutants
46000
-
calf, gel filtration and glycerol density gradient centrifugation
47000
-
deglycosylated GDPase, result of proteolytic cleavage of the 55000 Da enzyme during purification, SDS-PAGE
48000
-
deglycosylated GDPase, result of proteolytic cleavage of the 57000 Da enzyme during purification, SDS-PAGE
56820
-
calculated from amino acid sequence
57000
-
before signal sequence cleavage, metabolic labeling and immunoprecipitation, SDS-PAGE
55000
-
-
55000
-
after signal sequence cleavage, metabolic labeling and immunoprecipitation, SDS-PAGE
additional information
-
-
additional information
-
determination of structural and functional target sizes of GDPase activity in situ
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monomer
-
1 * 46000, calf, SDS-PAGE
?
-
x * 52000, His6-tagged enzyme, calculated from amino acid sequence
?
-
x * 61000, His6-tagged enzyme, SDS-PAGE
dimer
enzyme contains a unique sequence in the stem region predicted with high probability to adopt a coil-coil conformation that favors dimerization
dimer
-
2 * 55000, guanosine diphosphatase functions in situ as a homodimer and does not require association with other membrane proteins for its function, immunodetection, SDS-PAGE
additional information
-
-
additional information
-
guanosine diphosphatase functions in situ as a homodimer and does not require association with other membrane proteins for its function
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glycoprotein
-
-
glycoprotein
-
three potential N-glycosylation sites
glycoprotein
-
N-linked oligosaccharides
glycoprotein
-
high mannose glycoprotein
proteolytic modification
-
-
proteolytic modification
-
probably proteolytic cleavage of the enzyme during purification
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additional information
disruption of gene gda1 leads to a mutant with 90% reduced GDP hydrolysis activity compared to the wild-type, the mutant also shows severely impaired O-mannosylation and reduced cell wall phosphate content and other phenotypes, but the formation of hyphae is uneffected, overview
additional information
enzyme null mutants show 95% reduced activity in vitro and inhibition of glycosyltransferases utilizing uridine and guanosine nucleotide sugars due to accumulation of nucleoside diphosphates, the transport of both GDP-mannose and UDP-GlcNAc into the Golgi lumen is reduced in the null mutants, complementation of the disruption mutant by recombinant expression of the wild-type enzyme or the Saccharomyces cerevisiae enzyme
additional information
-
enzyme null mutants show 95% reduced activity in vitro and inhibition of glycosyltransferases utilizing uridine and guanosine nucleotide sugars due to accumulation of nucleoside diphosphates, the transport of both GDP-mannose and UDP-GlcNAc into the Golgi lumen is reduced in the null mutants, complementation of the disruption mutant by recombinant expression of the wild-type enzyme or the Saccharomyces cerevisiae enzyme
additional information
-
construction of s disruption mutant showing defects in N-glycosylation of other proteins
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stable to several cycles of freezing and thawing
-
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-80°C, separated into aliquots, stable for a long time
-
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Ni-NTA resin column chromatography
-
normal and transforming PCPH proteins: PCPH, PCPH proto-oncogene and mt-PCPH, PCPH oncogene having guanosine diphosphatase activity, recombinant proteins from Escherichia coli BL21, DE3. Purified bacterial recombinant PCPH and mt-PCPH proteins have GDPase activity
-
partial
-
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DNA and amino acid sequence determination and analysis, functional complementation of a Saccharomyces GDPase null mutant
DNA sequence determination and analysis, enzyme can complement and restore activity in Saccharomyces cerevisiae deletion mutant gda1, complementation of N-glycosylation defects
expressed in HEK-293 cells
-
normal and transforming PCPH proteins: PCPH, PCPH proto-oncogene and mt-PCPH, PCPH oncogene having guanosine diphosphatase activity
normal and transforming PCPH proteins: PCPH, PCPH proto-oncogene and mt-PCPH, PCPH oncogene having guanosine diphosphatase activity, expression in Escherichia coli BL21, DE3
-
overexpression in Schizosaccharomyces pombe, functional complementation of a Saccharomyces cerevisiae enzyme mutant defective in chitinase O-mannosylation
-
overexpression of GDA1 gene
-
normal and transforming PCPH proteins: PCPH, PCPH proto-oncogene and mt-PCPH, PCPH oncogene having guanosine diphosphatase activity
-
normal and transforming PCPH proteins: PCPH, PCPH proto-oncogene and mt-PCPH, PCPH oncogene having guanosine diphosphatase activity
-
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the enzyme activity significantly decreases at high concentrations of menadione, H2O2 and O2-
the enzyme activity significantly decreases at high concentrations of menadione, H2O2 and O2-
-
the enzyme activity significantly decreases at high concentrations of menadione, H2O2 and O2-
-
the enzyme activity significantly decreases at high concentrations of menadione, H2O2 and O2-
-
the enzyme activity significantly decreases at high concentrations of menadione, H2O2 and O2-
-
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Raychaudhuri, P.; Ghosh, S.; Maitra, U.
Purification and characterization of a guanosine diphosphatase activity from calf liver microsomal salt wash proteins
J. Biol. Chem.
260
8306-8311
1985
Bos taurus
brenda
Berninsone, P.; Lin, Z.Y.; Kempner, E.; Hirschberg, C.B.
Regulation of yeast Golgi glycosylation. Guanosine diphosphatase functions as a homodimer in the membrane
J. Biol. Chem.
270
14564-14567
1995
Saccharomyces cerevisiae
brenda
Vowels, J.J.; Payne, G.S.
A role for the lumenal domain in Golgi localization of the Saccharomyces cerevisiae guanosine diphosphatase
Mol. Biol. Cell
9
1351-1365
1998
Saccharomyces cerevisiae
brenda
Recio, J.A.; Paez, J.G.; Maskeri, B.; Loveland, M.; Velasco, J.A.; Notario, V.
Both normal and transforming PCPH proteins have guanosine diphosphatase activity but only the oncoprotein cooperates with ras in activating extracellular signal-regulated kinase ERK1
Cancer Res.
60
1720-1728
2000
Homo sapiens, Mesocricetus auratus, Mus musculus
brenda
Yanagisawa, K.; Resnick, D.; Abeijon, C.; Robbins, P.W.; Hirschberg, C.B.
A guanosine diphosphatase enriched in Golgi vesicles of Saccharomyces cerevisiae. Purification and characterization
J. Biol. Chem.
265
19351-19355
1990
Saccharomyces cerevisiae, Schizosaccharomyces pombe
brenda
Abeijon, C.; Orlean, P.; Robbins, P.W.; Hirschberg, C.B.
Topography of glycosylation in yeast: characterization of GDPmannose transport and lumenal guanosine diphosphatase activities in Golgi-like vesicles
Proc. Natl. Acad. Sci. USA
86
6935-6939
1989
Saccharomyces cerevisiae
brenda
Abeijon, C.; Yanagisawa, K.; Mandon, E.C.; Husler, A.; Moremen, K.; Hirschberg, C.B.; Robbins, P.W.
Guanosine diphosphatase is required for protein and sphingolipid glycosylation in the Golgi lumen of Saccharomyces cerevisiae
J. Cell Biol.
122
307-323
1993
Saccharomyces cerevisiae
brenda
Lopez-Avalos, M.D.; Uccelletti, D.; Abeijon, C.; Hirschberg, C.B.
The UDPase activity of the Kluyveromyces lactis Golgi GDPase has a role in uridine nucleotide sugar transport into Golgi vesicles
Glycobiology
11
413-422
2001
Kluyveromyces lactis (Q9HEM6), Kluyveromyces lactis
brenda
Herrero, A.B.; Uccelletti, D.; Hirschberg, C.B.; Dominguez, A.; Abeijon, C.
The Golgi GDPase of the fungal pathogen Candida albicans affects morphogenesis, glycosylation, and cell wall properties
Eukaryot. Cell
1
420-431
2002
Candida albicans (Q8TGH6)
brenda
Sanchez, R.; Franco, A.; Gacto, M.; Notario, V.; Cansado, J.
Characterization of gdp1+ as encoding a GDPase in the fission yeast Schizosaccharomyces pombe
FEMS Microbiol. Lett.
228
33-38
2003
Schizosaccharomyces pombe
brenda
Wu, M.; Chong, L.S.; Capolicchio, S.; Jessen, H.J.; Resnick, A.C.; Fiedler, D.
Elucidating diphosphoinositol polyphosphate function with nonhydrolyzable analogues
Angew. Chem. Int. Ed. Engl.
53
7192-7197
2014
Homo sapiens (O95989)
brenda
Delgado-Carmona, J.D.; Ramirez-Quijas, M.D.; Vega-Gonzalez, A.; Lopez-Romero, E.; Cuellar-Cruz, M.
Changes in GDPase/UDPase enzymatic activity in response to oxidative stress in four Candida species
Folia Microbiol. (Praha)
60
343-350
2015
Candida albicans, Candida parapsilosis, Pichia kudriavzevii, [Candida] glabrata
brenda
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
brenda
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