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aciclovir (ACV-MP)
?
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-
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ATP + (R)-3-((2-amino-1,6-dihydro-6-oxo-9H-purin-9-yl)methoxy)-4-hydroxybutylphosphonic acid
(R)-ganciclovir phosphonate monophosphate
ATP + (R)-ganciclovir phosphonate
?
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-
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-
?
ATP + 6-thioguanosine 5'-monophosphate
ADP + 8-thioguanosine 5'-diphosphate
ATP + 8-azaguanosine 5'-monophosphate
ADP + 8-azaguanosine 5'-diphosphate
ATP + 8-bromoguanosine 5'-monophosphate
ADP + 8-bromoguanosine 5'-diphosphate
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poor substrate
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-
?
ATP + 9-(1,3-dihydroxy-2-propoxymethyl)guanine 5'-monophosphate
ADP + 9-(1,3-dihydroxy-2-propoxymethyl)guanine 5'-diphosphate
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no substrate: 9-(5,5-difluoro-5-phosphonopentyl)guanine 5'-monophosphate
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?
ATP + 9-(2-hydroxyethoxymethyl)guanine 5'-monophosphate
ADP + 9-(2-hydroxyethoxymethyl)guanine 5'-diphosphate
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i.e. acyclovir 5'-monophosphate
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?
ATP + 9-(5-phosphonopentyl)guanine
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9-(5,5'-difluoro-5-phosphonopenthyl)guanine is not a substrate
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ATP + AMP
2 ADP
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ATP + AMP
ADP + ADP
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very low activity with AMP
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ATP + ganciclovir
ADP + ganciclovir phosphate
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ATP + ganciclovir monophosphate
?
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?
ATP + ganciclovir monophosphate
ADP + ganciclovir-diphosphate
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-
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?
ATP + IMP
ADP + IDP
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very poor substrate
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?
GDP + GDP
GTP + GMP
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-
?
GMP + MgATP2-
MgADP- + GDP
GTP + dAMP
GDP + dADP
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r
GTP + GDP
GMP + guanosine 5'-tetraphosphate
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?
guanosine monophosphate + adenosine triphosphate
guanosine diphosphate + adenosine diphosphate
additional information
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ATP + (R)-3-((2-amino-1,6-dihydro-6-oxo-9H-purin-9-yl)methoxy)-4-hydroxybutylphosphonic acid
(R)-ganciclovir phosphonate monophosphate
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i.e. R-ganciclovir phosphonate, (S) enantiomer 100fold less efficient, used for racemic resolution
-
?
ATP + (R)-3-((2-amino-1,6-dihydro-6-oxo-9H-purin-9-yl)methoxy)-4-hydroxybutylphosphonic acid
(R)-ganciclovir phosphonate monophosphate
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i.e. R-ganciclovir phosphonate, (S) enantiomer 100fold less efficient, used for racemic resolution
-
?
ATP + 6-thioguanosine 5'-monophosphate
ADP + 8-thioguanosine 5'-diphosphate
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?
ATP + 6-thioguanosine 5'-monophosphate
ADP + 8-thioguanosine 5'-diphosphate
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-
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-
?
ATP + 6-thioguanosine 5'-monophosphate
ADP + 8-thioguanosine 5'-diphosphate
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not thiodeoxyguanosine derivative
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-
?
ATP + 6-thioguanosine 5'-monophosphate
ADP + 8-thioguanosine 5'-diphosphate
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-
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?
ATP + 8-azaguanosine 5'-monophosphate
ADP + 8-azaguanosine 5'-diphosphate
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?
ATP + 8-azaguanosine 5'-monophosphate
ADP + 8-azaguanosine 5'-diphosphate
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-
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?
ATP + 8-azaguanosine 5'-monophosphate
ADP + 8-azaguanosine 5'-diphosphate
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?
ATP + dGMP
ADP + dGDP
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-
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-
r
ATP + dGMP
ADP + dGDP
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phosphorylation at 48% the rate of GMP
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r
ATP + dGMP
ADP + dGDP
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r
ATP + dGMP
ADP + dGDP
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r
ATP + dGMP
ADP + dGDP
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-
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-
r
ATP + dGMP
ADP + dGDP
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-
r
ATP + dGMP
ADP + dGDP
-
-
-
r
ATP + dGMP
ADP + dGDP
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-
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-
r
ATP + dGMP
ADP + dGDP
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-
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-
r
ATP + dGMP
ADP + dGDP
-
-
-
-
?
ATP + dGMP
ADP + dGDP
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-
-
-
r
ATP + dGMP
ADP + dGDP
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-
-
-
?
ATP + dGMP
ADP + dGDP
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low activity, dGMP acts also as inhibitor
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?
ATP + dGMP
ADP + dGDP
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dGMP is a poor substrate, the Kcat for dGMP is about 22fold lower than that observed for GMP. The value of kcat/Km for dGMP is at least 70fold lower than that of GMP
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?
ATP + dGMP
ADP + dGDP
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-
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r
ATP + dGMP
ADP + dGDP
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-
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-
r
ATP + dGMP
ADP + dGDP
-
-
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-
r
ATP + GDP
ADP + GTP
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-
-
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?
ATP + GDP
ADP + GTP
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?
ATP + GMP
ADP + GDP
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?
ATP + GMP
ADP + GDP
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-
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?
ATP + GMP
ADP + GDP
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specificity
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?, r
ATP + GMP
ADP + GDP
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best substrates
-
?
ATP + GMP
ADP + GDP
-
no donor substrates are ITP, dGTP, dCTP or dTTP
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-
?, r
ATP + GMP
ADP + GDP
-
dCMP is no acceptor substrate
-
-
?, r
ATP + GMP
ADP + GDP
-
dTMP is no acceptor substrate
-
-
?, r
ATP + GMP
ADP + GDP
-
AMP is no acceptor substrate
-
?
ATP + GMP
ADP + GDP
-
AMP is no acceptor substrate
-
-
?, r
ATP + GMP
ADP + GDP
-
dAMP is no acceptor substrate
-
?
ATP + GMP
ADP + GDP
-
dAMP is no acceptor substrate
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-
?, r
ATP + GMP
ADP + GDP
-
no donor substrates are GTP, CTP, UTP
-
?
ATP + GMP
ADP + GDP
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no donor substrates are GTP, CTP, UTP
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-
?, r
ATP + GMP
ADP + GDP
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CMP, UMP are no acceptor substrates
-
?
ATP + GMP
ADP + GDP
-
CMP, UMP are no acceptor substrates
-
-
?, r
ATP + GMP
ADP + GDP
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first step in 'cGMP-cycle' toward re-synthesis of cGMP
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?
ATP + GMP
ADP + GDP
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?
ATP + GMP
ADP + GDP
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r
ATP + GMP
ADP + GDP
GMP and ATP served as the most effective phosphate acceptor and donor, respectively
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r
ATP + GMP
ADP + GDP
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?
ATP + GMP
ADP + GDP
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r
ATP + GMP
ADP + GDP
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specificity
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?
ATP + GMP
ADP + GDP
-
signal transduction
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?
ATP + GMP
ADP + GDP
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specificity
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?
ATP + GMP
ADP + GDP
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?
ATP + GMP
ADP + GDP
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signal transduction
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?
ATP + GMP
ADP + GDP
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?
ATP + GMP
ADP + GDP
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?
ATP + GMP
ADP + GDP
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?
ATP + GMP
ADP + GDP
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?
ATP + GMP
ADP + GDP
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specificity
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?
ATP + GMP
ADP + GDP
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nucleoside monophosphate binding site is highly specific for guanine moiety
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-
?
ATP + GMP
ADP + GDP
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deoxyguanosine, guanosine are no acceptor substrates
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-
?
ATP + GMP
ADP + GDP
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6-thio-IMP is no acceptor substrate
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-
?
ATP + GMP
ADP + GDP
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XMP is no acceptor substrate
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-
?
ATP + GMP
ADP + GDP
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AMP is no acceptor substrate
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-
?
ATP + GMP
ADP + GDP
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CMP, UMP are no acceptor substrates
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-
?
ATP + GMP
ADP + GDP
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-
-
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?
ATP + GMP
ADP + GDP
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-
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?
ATP + GMP
ADP + GDP
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specificity
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-
?
ATP + GMP
ADP + GDP
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AMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
dAMP is no acceptor substrate
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-
?
ATP + GMP
ADP + GDP
guanylate kinase is an essential enzyme
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-
?
ATP + GMP
ADP + GDP
upon substrate binding, the LID and nucleotide-monophosphate-binding domains are brought together and toward the CORE with large concerted movements about the alpha3, helix 3, axis
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-
?
ATP + GMP
ADP + GDP
guanylate kinase is an essential enzyme
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-
?
ATP + GMP
ADP + GDP
upon substrate binding, the LID and nucleotide-monophosphate-binding domains are brought together and toward the CORE with large concerted movements about the alpha3, helix 3, axis
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?
ATP + GMP
ADP + GDP
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-
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?
ATP + GMP
ADP + GDP
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-
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?
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
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-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
specificity
-
-
?
ATP + GMP
ADP + GDP
-
nucleoside monophosphate binding site is highly specific for guanine moiety
-
-
?
ATP + GMP
ADP + GDP
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deoxyguanosine, guanosine are no acceptor substrates
-
-
?
ATP + GMP
ADP + GDP
-
TMP is not an acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
dCMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
IMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
6-thio-IMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
XMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
AMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
dAMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
CMP, UMP are no acceptor substrates
-
-
?
ATP + GMP
ADP + GDP
-
regulation of cellular adhesion and signal transduction at sites of cell-cell contact
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-
?
ATP + GMP
ADP + GDP
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CASK construct has no activity
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?
ATP + GMP
ADP + GDP
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PSD-95 construct has no activity
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?
ATP + GMP
ADP + GDP
-
-
-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
-
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r
ATP + GMP
ADP + GDP
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-
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?
ATP + GMP
ADP + GDP
-
best substrates
-
-
?
ATP + GMP
ADP + GDP
-
best substrates
-
?
ATP + GMP
ADP + GDP
-
IMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
XMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
AMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
AMP is no acceptor substrate
-
?
ATP + GMP
ADP + GDP
GMP binding induces conformational changes in non-acetylated N-terminus mutants
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-
?
ATP + GMP
ADP + GDP
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two specific binding sites: ATP- and GMP-binding site
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?
ATP + GMP
ADP + GDP
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CMP, UMP are no acceptor substrates
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-
?
ATP + GMP
ADP + GDP
-
regulation of cellular adhesion and signal transduction at sites of cell-cell contact
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-
?
ATP + GMP
ADP + GDP
-
-
-
-
?
ATP + GMP
ADP + GDP
-
specificity
-
-
?
ATP + GMP
ADP + GDP
-
nucleoside monophosphate binding site is highly specific for guanine moiety
-
-
?
ATP + GMP
ADP + GDP
-
deoxyguanosine, guanosine are no acceptor substrates
-
-
?
ATP + GMP
ADP + GDP
-
6-thio-IMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
XMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
AMP is no acceptor substrate
-
-
?
ATP + GMP
ADP + GDP
-
CMP, UMP are no acceptor substrates
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-
?
ATP + GMP
ADP + GDP
-
key enzyme of biosynthetic pathway of GTP or dGTP
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r
ATP + GMP
ADP + GDP
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-
-
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?
ATP + GMP
ADP + GDP
-
-
-
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?
dATP + dGMP
dADP + dGDP
-
as good as ATP
-
-
?
dATP + dGMP
dADP + dGDP
-
phosphorylation at 22% the rate of ATP
-
?
dATP + dGMP
dADP + dGDP
-
-
-
?
dATP + dGMP
dADP + dGDP
-
-
-
?
dATP + dGMP
dADP + dGDP
-
-
-
-
?
dATP + dGMP
dADP + dGDP
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-
-
-
?
dATP + dGMP
dADP + dGDP
-
-
-
-
?
dATP + dGMP
dADP + dGDP
-
-
-
-
?
dATP + dGMP
dADP + dGDP
-
-
-
-
?
dATP + GMP
dADP + GDP
-
as good as ATP
-
-
?
dATP + GMP
dADP + GDP
-
phosphorylation at 81% the rate of ATP
-
?
dATP + GMP
dADP + GDP
-
-
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r
dATP + GMP
dADP + GDP
-
-
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?
dATP + GMP
dADP + GDP
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?
dATP + GMP
dADP + GDP
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-
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?
dATP + GMP
dADP + GDP
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-
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?
dATP + GMP
dADP + GDP
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-
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?
dATP + GMP
dADP + GDP
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-
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?
dGMP + ATP
dGDP + ADP
GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor.
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r
dGMP + ATP
dGDP + ADP
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-
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?
dGMP + ATP
dGDP + ADP
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-
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?
dGMP + ATP
dGDP + ADP
-
Catalyses reversible phosphoryl transfer from a nucleotide donor to a nucleotide acceptor. Phosphorylation of (d)GMP to (d)GDP using ATP as phosphoryl donor. Guanylate monophosphate kinases are involved in the synthesis of nucleotide precursors, they indirectly modulate the synthesis of DNA and RNA.
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r
GMP + ATP
GDP + ADP
GMPKs catalyze the reversible phosphorylation of GMP and dGMP to their diphosphate form in the cell using ATP as a preferred phosphate donor.
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r
GMP + ATP
GDP + ADP
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-
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?
GMP + ATP
GDP + ADP
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-
-
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?
GMP + ATP
GDP + ADP
-
Catalyses reversible phosphoryl transfer from a nucleotide donor to a nucleotide acceptor. Phosphorylation of (d)GMP to (d)GDP using ATP as phosphoryl donor. Guanylate monophosphate kinases are involved in the synthesis of nucleotide precursors, they indirectly modulate the synthesis of DNA and RNA.
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r
GMP + MgATP2-
MgADP- + GDP
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-
-
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?
GMP + MgATP2-
MgADP- + GDP
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-
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?
guanosine monophosphate + adenosine triphosphate
guanosine diphosphate + adenosine diphosphate
Guanylate kinase (GK) is an essential enzyme that catalyzes the transfer of a phosphate from adenosine triphosphate (ATP) to guanosine monophosphate (GMP).
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?
guanosine monophosphate + adenosine triphosphate
guanosine diphosphate + adenosine diphosphate
in the presence of Mg2+
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-
r
additional information
?
-
recombinant enzyme BmGK utilizes both GMP and dGMP as substrates. No activity with dTMP, UMP, CMP, dCMP, IMP, XMP, CTP, UTP, and TTP
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?
additional information
?
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-
recombinant enzyme BmGK utilizes both GMP and dGMP as substrates. No activity with dTMP, UMP, CMP, dCMP, IMP, XMP, CTP, UTP, and TTP
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?
additional information
?
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MAGUKs contain three PSD-95/Discs large/Zona occludens 1, i.e. PDZ, domains, an src-homology 3, i.e. SH3, domain and a C-terminal guanylate kinase domain and play a key role in the regulation of the intracellular trafficking and synaptic localization of ionotropic glutamate receptors. In particular, the postsynaptic density-95-like subfamily of MAGUKs, PSD-MAGUKs, organizes ionotropic glutamate receptors and their associated signaling proteins in the postsynaptic density of the excitatory synapse regulating the strength of synaptic activity. Alterations of PSD-MAGUK protein interaction with N-methyl-D-aspartate, NMDA, receptors regulatory subunits are common events in several CNS disorders, overview. NMDA receptors' synaptic localization and binding to PSD-MAGUK protein family play a key role in the control of downstream signals resulting from receptor activation, physiological function, overview. The enzyme plays a role in excitotoxicity and neurodegenerative disorders, e.g. in Parkinson disease and Alzheimer disease. Physiological functions, detailed overview
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?
additional information
?
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the post-synaptic density-95 membrane associated guanylate kinase family of scaffolding proteins, MAGUK, associate with N-methyl-D-aspartate receptor NR2 subunits via their C-terminal glutamate serine, or aspartate/glutamate, valine motifs. N-methyl-D-aspartate receptors are a subclass of ionotropic glutamate receptors that are trafficked and/or clustered at synapses by MAGUK. Receptor binding of PSD variants differin the impact on the stabilisation, turnover and compartmentalisation of N-methyl-D-aspartate receptor subtypes in neurones during development and in the mature brain
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?
additional information
?
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-
binding of N-methyl-D-aspartate receptors NR2B and NR2A, wild-type and mutant proteins, by PSD variants, overview
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-
?
additional information
?
-
-
MAGUKs contain three PSD-95/Discs large/Zona occludens 1, i.e. PDZ, domains, an src-homology 3, i.e. SH3, domain and a C-terminal guanylate kinase domain and play a key role in the regulation of the intracellular trafficking and synaptic localization of ionotropic glutamate receptors. In particular, the postsynaptic density-95-like subfamily of MAGUKs, PSD-MAGUKs, organizes ionotropic glutamate receptors and their associated signaling proteins in the postsynaptic density of the excitatory synapse regulating the strength of synaptic activity. Alterations of PSD-MAGUK protein interaction with N-methyl-D-aspartate, NMDA, receptors regulatory subunits are common events in several CNS disorders, overview, NMDA receptors' synaptic localization and binding to PSD-MAGUK protein family play a key role in the control of downstream signals resulting from receptor activation, physiological function, overview
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?
additional information
?
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-
the enzyme forms complexes with DNA
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?
additional information
?
-
the enzyme forms complexes with DNA
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?
additional information
?
-
the enzyme forms complexes with DNA
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?
additional information
?
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-
the cytosolic isozyme is indispensable for the growth and development of plants, but not for chloroplast development, while the plastid/mitochondrial isozyme is is essential for chloroplast differentiation, overview
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?
additional information
?
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-
no activity with CMP, dTMP, dAMP, dCMP, and UMP
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-
?
additional information
?
-
-
MAGUKs contain three PSD-95/Discs large/Zona occludens 1, i.e. PDZ, domains, an src-homology 3, i.e. SH3, domain and a C-terminal guanylate kinase domain and play a key role in the regulation of the intracellular trafficking and synaptic localization of ionotropic glutamate receptors. In particular, the postsynaptic density-95-like subfamily of MAGUKs, PSD-MAGUKs, organizes ionotropic glutamate receptors and their associated signaling proteins in the postsynaptic density of the excitatory synapse regulating the strength of synaptic activity. Alterations of PSD-MAGUK protein interaction with N-methyl-D-aspartate, NMDA, receptors regulatory subunits are common events in several CNS disorders, overview, NMDA receptors' synaptic localization and binding to PSD-MAGUK protein family play a key role in the control of downstream signals resulting from receptor activation, physiological function, overview
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-
?
additional information
?
-
-
synaptic scaffolding molecule, S-SCAM, is a synaptic protein, which harbors five or six PSD-95/Discs large/ZO-1, a guanylate kinase, and two WW domains. S-SCAM is associated with beta-DG and neuroligin 2 at inhibitory synapses, and functions as a linker between the dystrophin glycoprotein complex and the neurexin-neuroligin complex, complex formation analysis, overview
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?
additional information
?
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-
the voltage-gated calcium channel beta1b contains a conserved guanylate kinase domain, which is alone recapitulating calcium channel beta-subunit CaVbeta-mediated modulation of channel activation facilitating inactivation of the voltage-gated channel. CaVbeta can switch the inactivation phenotype conferred to CaV2.3 from slow to fast after posttranslational modifications during channel biogenesis, modulation mechanism, overview
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?
additional information
?
-
the voltage-gated calcium channel beta1b contains a conserved guanylate kinase domain, which is alone recapitulating calcium channel beta-subunit CaVbeta-mediated modulation of channel activation facilitating inactivation of the voltage-gated channel. CaVbeta can switch the inactivation phenotype conferred to CaV2.3 from slow to fast after posttranslational modifications during channel biogenesis, modulation mechanism, overview
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?
additional information
?
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the voltage-gated calcium channel beta2a contains a conserved guanylate kinase domain, which is alone recapitulating calcium channel beta-subunit CaVbeta-mediated modulation of channel activation inhibiting inactivation of the voltage-gated channel. CaVbeta can switch the inactivation phenotype conferred to CaV2.3 from slow to fast after posttranslational modifications during channel biogenesis, modulation mechanism, overview
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?
additional information
?
-
the voltage-gated calcium channel beta2a contains a conserved guanylate kinase domain, which is alone recapitulating calcium channel beta-subunit CaVbeta-mediated modulation of channel activation inhibiting inactivation of the voltage-gated channel. CaVbeta can switch the inactivation phenotype conferred to CaV2.3 from slow to fast after posttranslational modifications during channel biogenesis, modulation mechanism, overview
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?
additional information
?
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guanylate kinase binds a fragment of microtubule-associated protein-1a, i.e. MAP1a, in the GMP-binding site, the minimal GK binding site comprised by residues 1862-1878. MAP1a, which helps remodel the microtubule cytoskeleton in an activity-dependent manner, a is a common binding partner of PSD-95 GK and binds GK in an extended conformation, PSD-95 GK ligand consensus is not strongly constrained, binding via binding intermediate, structure, molecular dynamics simulation, overview
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?
additional information
?
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functionally, the guanylate kinase domain is able to interact with a variety of phospho-peptide ligands with high affinity but its binding ability to GMP is low
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?