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positive effector for CTP reduction
-
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.005 mM, stimulation of CDP reduction in absence of ATP, inhibition in presence of ATP
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
6fold stimulation of GDP reduction
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors (ATP/dATP, dGTP, and dTTP) modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of ADP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP and UDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of CDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
stimulation of GDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
strong stimulation of CDP reduction
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell
specific activator for CTP reduction
specific activator for CTP reduction
specific activator for CTP reduction
stimulation of CTP reduction
stimulation of CTP reduction
stimulation of CTP reduction
nearly as effective as ATP
-
activates cytosolic 5'-nucleotidase II
activates cytosolic 5'-nucleotidase II
activates cytosolic 5'-nucleotidase II
both dATP and dGTP are co-activators for hydrolysis of dTTP, dATP might bind at the secondary allosteric site
-
at least 2fold enhancement of enzyme activity, maximal at 20 microM, similar results with all four deoxynucleoside triphosphates
-
poor allosteric activator
-
20 fold increase in activity
-
lower activating effect compared to ATP
-
stabilizes the dimeric form of the enzyme
-
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18% inhibition at 0.5 mM
-
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.0033 mM, 50% inhibition of CDP reduction, 0.0036 mM, 50% inhibition of GDP reduction; inhibition of CDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.005 mM, 50% inhibition of CDP and UDP reduction, 0.005 mM, 50% inhibition of GDP and ADP reduction; inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 10% residual activity
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.05 mM, 50% inhibition of CDP reduction in presence of optimum ATP concentration i.e. 6 mM, stimulation in absence of ATP; inhibition of CDP reduction
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
0.1 mM, 96% inhibition of CDP reductase activity in dextran sulfate-treated cells, 85% inhibition of GDP reductase activity
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
2.1 mM, 50% inhibition; inhibition of CDP reduction; weak inhibition of ADP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
3.5 mM, 92% inhibition of activity in extracts; inhibition of CDP reduction
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activating at low concentration, inhibitory at higher concentration. dATP induces a stable alpha4beta4 complex that dissociates in the presence of ATP
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
activation at low concentration with a KL1 value for specificity site binding of 0.0032 mM, inhibition at higher concentration with a KL2 value for activity site binding of 0.0173 mM
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
allosteric inhibitor, dATP binding to the cone domain at the N-terminus of alpha2 has an inhibitory effect, whereas ATP binding reverses this inhibition. As RNR produces deoxyribonucleotides, levels of DNA building blocks in the cell rise. To avoid overstocking the cell, RNR contains an off switch that is triggered when levels of one of the DNA building blocks, dATP, is high enough to occupy a particular site on the alpha unit. Binding of dATP to this site results in three pairs of alpha units getting together to form a stable ring of six units (called alpha6). Binding structure to the cone domain in the human alpha6 ring structure, overview. 0.05 mM dATP is sufficient to almost completely eliminate CDP reductase activity in the presence of 3 mM ATP
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP at 2 mM clearly inhibits the enzyme activity. dATP is a negative allosteric regulator
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
HSV type 2, 1 mM, 20% inhibition
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition by dATP has a regulatory function
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of ADP reduction; inhibition of CDP reduction; inhibition of GDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP and UDP reduction is reversed by ATP; inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction in the presence of ATP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of CDP, UDP, GDP and ADP reduction; noncompetitive inhibition vs. ADP, GDP and CDP
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP reduction; inhibition of UDP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
inhibition of CDP, UDP, GDP and ADP reduction
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
many RNRs possess an overall activity regulation site (a-site) positioned in an N-terminal domain of about 85-100 amino acid residues called the ATP-cone. Acting as a regulatory master switch, the a-site senses intracellular nucleotide concentrations by competitive binding of ATP and dATP. In the presence of ATP the enzyme is active, and when concentrations of dNTPs rise, binding of dATP switches the enzyme off. This mechanism ensures sufficient but not excessive amounts of nucleotides that may also cause increased mutation rates. The ATP-cone is an example of allosteric regulation controlled by a domain that acts relatively independent of the catalytic core of proteins. This type of allosteric regulation has been shown to provide an evolutionarily dynamic process by which allosteric regulation can be lost or gained both in RNRs and other enzymes. dATP binding to enzyme subunit NrdB induces formation of higher oligomeric complexes. dATP-NrdB structure complex analysis
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction
1 mM, 71% inhibition at pH 6.0
1 mM, 71% inhibition at pH 6.0
strong feedback inhibition, tight binding at the active site in stoichiometric amount
-
0.05 mM, 68% inhibition
-
0.5 mM, 90% inhibition of recombinant dAK, end product inhibition
-
kinetic, mechanism, protects corresponding active site against trypsin inactivation
-
more than 95% inhibition at 0.3 mM
0.4 mM, 12% inhibition, adult liver
-
0.25 mM, 50% inhibition, major poly(A) polymerase, 15% inhibition, minor poly(A) polymerase
-
mechanism of Mn2+-dependent inhibition
-
replacement of dATP by ATP completely prevents synthesis
replacement of dATP by ATP completely prevents synthesis
replacement of dATP by ATP completely prevents synthesis
replacement of dATP by ATP completely prevents synthesis
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive
5 mM, 28°C, presence of MgCl2, 39% residual activity
-
synthesis of the short RNA chains is inhibited at all levels of dATP added, and the size of oligo(rA) chains formed and the amount of ATP incorporated are reduced
-
purine triphosphate nucleotides (RTP) behave as non-competitive inhibitors, furthermore PARN does not discriminate whether there is ribose or deoxyribose in the nucleotides, Mg2+ releases the inhibition by RDPs and RTPs, but not by RMPs
-
0.2 mM, 15% residual activity
-
50% inhibition by 0.001 mM dATP
-
the 8-oxo-dGTPase activity of wild type hMTH1 decreases to 79.6% of the control in the presence of 0.1 mM dATP
-
inhibition influenced by pH, enhanced inhibition at pH 7.5
-
83% and 27% inhibition of RNA and DNA helicase activity at 2.5 mM, respectively
-
substrate with optimal concentration range between 1 and 2 mM. At high concentrations inhibition of activity can be observed
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
-
inhibits unwinding; is a poor substrates and potent inhibitor of unwinding
-
83% and 27% inhibition of RNA and DNA helicase activity at 2.5 mM, respectively
-
inhibition of NTPase activity of NS3 protein by NTP derivatives
-
inhibits unwinding; is a poor substrates and potent inhibitor of unwinding
-
competitive with respect to ATP
-
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