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Ligand dATP
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Basic Ligand Information
2'-dATP, 2'-deoxy-adenosine 5'-triphosphate, 2'-deoxy-ATP, 2'-deoxyadenosine-3'-triphosphate, 2'-deoxyadenosine 5'-triphosphate, 2'-deoxyATP, 2-dATP, 2-deoxyadenosine 5'-triphosphate, 2-DeoxyATP, 5'-dATP, Deoxy-ATP, deoxyadenosine 5'-triphosphate, deoxyATP
BRENDA
KEGG
Show all BRENDA pathways known for dATP
close all tables 
open all tablesRoles as Enzyme Ligand
In Vivo Substrate in Enzyme-catalyzed Reactions (12 results)
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EC NUMBER 
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
In Vivo Product in Enzyme-catalyzed Reactions (1 result)
EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Substrate in Enzyme-catalyzed Reactions (593 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
deoxyATP + Photinus luciferin = oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
peroxiredoxin-(S-hydroxy-S-oxocysteine) + dATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + dADP + phosphate + R-S-S-R
-
2'-deoxy-ATP + L-methionine + H2O = ?
639047, 639045, 639049, 639056, 639041, 639052, 639039, 639042, 639043, 639044, 639053, 639054, 639058, 639051, 639055, 639057, 639038, 639040, 639048, 639074, 639046, 639050
-
2'-deoxy-ATP + sn-1,2-dihexanoylglycerol = 2'-deoxy-ADP + sn-1,2-dihexanoylglycerol 3-phosphate
-
dATP + D-fructose 6-phosphate = dADP + D-fructose 1,6-bisphosphate
-
2'-deoxyadenosine-3'-triphosphate + 2'-deoxyguanosine = 2'-deoxyadenosine-3'-diphosphate + 2'-deoxyguanosine 5'-phosphate
2'-deoxyadenosine-3'-triphosphate + 2'-deoxyguanosine = 2'-deoxyadenosine-3'-diphosphate + 2'-deoxyguanosine 5'-phosphate
dATP + 4-methyl-5-(2-hydroxyethyl)thiazole = dADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
2'-dATP + 1-phosphatidyl-1D-myo-inositol = 2'-dADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
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dATP + 1-phosphatidyl-1D-myo-inositol = dADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
-
2'-deoxyadenosine-3'-triphosphate + 2'-deoxyadenosine = 2'-deoxyadenosine-3'-diphosphate + 2'-deoxyadenosine 5'-phosphate
-
2'-deoxyadenosine-3'-triphosphate + 2'-deoxycytidine = 2'-deoxyadenosine-3'-diphosphate + 2'-deoxycytidine 5'-phosphate
-
dATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = dADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
dATP + 3-phospho-D-glycerate = dADP + 1,3-diphosphoglycerate
-
2'-deoxy-adenosine 5'-triphosphate + trans-farnesyl diphosphate = 2'-deoxyadenosine 5'-diphosphate + trans-farnesyl triphosphate
-
dATP + 5-methyldeoxycytidine 5'-phosphate = dADP + 5-methyldeoxycytidine diphosphate
-
dATP + AMP = dADP + ADP
-
dATP + dGMP = dADP + dGDP
-
dATP + dTMP = dADP + dTDP
-
dATP + D-ribose 5-phosphate = dAMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
dATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine = dAMP + 2-amino-7,8-dihydro-4-hydroxy-6-(diphosphooxymethyl)pteridine
-
dATP + GTP = dAMP + guanosine 3'-diphosphate 5'-triphosphate
-
dATP + nicotinamide ribonucleotide = diphosphate + nicotinamide deoxyadenosine dinucleotide
-
dATP + DNAn = diphosphate + DNAn+1
dATP + DNAn = diphosphate + DNAn+1
dATP + DNAn = diphosphate + DNAn+1
dATP + DNAn = diphosphate + DNAn+1
dATP + DNAn = diphosphate + DNAn+1
dATP + DNAn = diphosphate + DNAn+1
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + DNAn = ?
dATP + N-methylimidazolidine-2,4-dione + H2O = dADP + phosphate + N-carbamoylsarcosine
-
dATP + H2O = dADP + phosphate
756042, 756304, 692937, 694413, 692150, 694414, 693900, 692945, 693688, 690869, 692828, 692155, 692829, 692898, 694420, 656166, 692262, 694541, 690795, 692936, 758313
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2'-dATP + H2O + a dynein associated with a microtubule at position n = 2'-dADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
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2'-dATP + H2O + a kinesin associated with a microtubule at position n = 2'-dADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
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dATP + negatively supercoiled circular DNA = dADP + phosphate + relaxed circular DNA
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2'-deoxyadenosine 5'-triphosphate + L-arginine + tRNAArg = 2'-deoxyadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
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2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe = 2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
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dATP + a fatty acid + [acyl-carrier protein] = dAMP + diphosphate + fatty acid-[acyl-carrier protein]
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dATP + 5,10-methylene-5,6,7,8-tetrahydropteroyl-Glu + Glu = dADP + phosphate + 5,10-methylene-5,6,7,8-tetrahydropteroyl-gamma-Glu2
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dATP + 5,6,7,8-tetrahydropteroyl-Glu + Glu = dADP + phosphate + 5,6,7,8-tetrahydropteroyl-Glu2
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dATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m = dAMP + diphosphate + (deoxyribonucleotide)m+n
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dATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m = dAMP + diphosphate + (deoxyribonucleotide)n+m
-
dATP + (ribonucleotide)n + (ribonucleotide)m = dAMP + phosphate + (ribonucleotide)n+m
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dATP + hydrogenobyrinic acid a,c-diamide + Co2+ = dADP + phosphate + cob(II)yrinic acid a,c-diamide + H+
-
2'-deoxyATP + H2O + H+/in + K+/out = 2'-deoxyADP + phosphate + H+/out + K+/in
-
Product in Enzyme-catalyzed Reactions (15 results)
EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Enzyme Cofactor/Cosubstrate (21 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
73% of the activity with ATP and deoxycytidine, 6% of the activity with ATP and deoxyadenosine
-
best cofactor, Pcal_1127 exhibits slightly higher activity with dATP compared to ATP as diphosphate donor
-
Activator in Enzyme-catalyzed Reactions (302 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
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
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
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
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
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
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
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Inhibitor in Enzyme-catalyzed Reactions (531 results)
EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
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
0.05 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
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
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 bind