EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
    2.7.4.8 | ATP + (R)-3-((2-amino-1,6-dihydro-6-oxo-9H-purin-9-yl)methoxy)-4-hydroxybutylphosphonic acid |
i.e. R-ganciclovir phosphonate, (S) enantiomer 100fold less efficient, used for racemic resolution |
Homo sapiens |
(R)-ganciclovir phosphonate monophosphate |
- |
? |
| 2.7.4.8 | ATP + (R)-3-((2-amino-1,6-dihydro-6-oxo-9H-purin-9-yl)methoxy)-4-hydroxybutylphosphonic acid |
i.e. R-ganciclovir phosphonate, (S) enantiomer 100fold less efficient, used for racemic resolution |
Sus scrofa |
(R)-ganciclovir phosphonate monophosphate |
- |
? |
| 2.7.4.8 | ATP + AMP |
- |
Pyrococcus furiosus |
2 ADP |
- |
? |
| 2.7.4.8 | aciclovir (ACV-MP) |
- |
Homo sapiens |
? |
- |
? |
| 2.7.4.8 | ATP + (R)-ganciclovir phosphonate |
- |
Homo sapiens |
? |
- |
? |
| 2.7.4.8 | ATP + 9-(5-phosphonopentyl)guanine |
9-(5,5'-difluoro-5-phosphonopenthyl)guanine is not a substrate |
Sus scrofa |
? |
- |
? |
| 2.7.4.8 | ATP + ganciclovir monophosphate |
- |
Homo sapiens |
? |
- |
? |
| 2.7.4.8 | more |
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 |
Mus musculus |
? |
- |
? |
| 2.7.4.8 | more |
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 |
Rattus norvegicus |
? |
- |
? |
| 2.7.4.8 | more |
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 |
Homo sapiens |
? |
- |
? |
