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D-luciferin + dATP + O2 = ?
-
deoxyATP + Photinus luciferin = oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
dATP + adenosylcobalamin = ?
dATP + adenosylcobalamin = ?
dATP + adenosylcobalamin = ?
peroxiredoxin-(S-hydroxy-S-oxocysteine) + dATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + dADP + phosphate + R-S-S-R
-
dATP + citrate + CoA = dADP + phosphate + acetyl-CoA + oxaloacetate
-
dimethylallyl diphosphate + dATP = ?
-
2'-deoxy-ATP + cob(I)alamin + H2O = ?
-
cob(I)alamin + dATP + H2O + H+ = deoxyadenosylcobalamin + diphosphate + phosphate
-
dATP + cob(I)alamin = tripolyphosphate + deoxyadenosylcobalamin
-
dATP + cobalamin = triphosphate + deoxyadenosylcob(III)alamin
-
dATP + cobalamin = triphosphate + deoxyadenosylcobalamin
-
dimethylallyl diphosphate + dATP = diphosphate + N6-(dimethylallyl)dATP
-
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
-
dATP + depurinated DNA = deoxyribose triphosphate + purinated DNA
-
dATP + depurinated poly(dA-dT) = deoxyribose triphosphate + purinated poly(dA-dT)
-
2'-dATP + D-glucose = 2'-dADP + D-glucose 6-phosphate
-
dATP + 5-methylthioribose = dADP + 5-methylthioribose 1-phosphate
-
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 + D-ribose = dADP + D-ribose 5-phosphate
-
dATP + adenosylcobinamide = adenosylcobinamide phosphate + dADP
-
dATP + L-seryl-tRNASec = dADP + O-phospho-L-seryl-tRNASec
-
dATP + 2-deoxy-D-ribose = dADP + 2-deoxy-D-ribose 5-phosphate
-
dATP + NAD+ = dADP + NADP+
-
dATP + NADH = dADP + NADPH
-
dATP + adenosine 5-phosphosulfate = dADP + 3'-phosphoadenosine 5'-phosphosulfate
-
2'-dATP + riboflavin = 2'-dADP + riboflavin 5'-phosphate
-
dATP + riboflavin = dADP + FMN
-
dATP + (R)-pantothenate = dADP + (R)-4'-phosphopantothenate
-
pantothenate + dATP = 4'-phosphopantothenate + dADP
-
dATP + mevalonate = dADP + phosphomevalonate
-
dATP + D-fructose = dADP + D-fructose 6-phosphate
-
dATP + D-glucuronate = dADP + 1-phospho-D-glucuronate
-
dATP + cytidine = dADP + CMP
-
dATP + uridine = dADP + UMP
-
dATP + 4-methyl-5-(2-hydroxyethyl)thiazole = dADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
-
dATP + N-acetyl-D-glucosamine = dADP + N-acetyl-D-glucosamine 6-phosphate
-
2'-dATP + D-galactose = 2'-dADP + alpha-D-galactose 1-phosphate
-
dATP + D-galactose = dADP + alpha-D-galactose 1-phosphate
-
deoxy-ATP + D-galactose = deoxyADP + alpha-D-galactose 1-phosphate
-
dATP + glucose = dADP + D-glucose 6-phosphate
-
2'-deoxy-ATP + scyllo-inosamine = 2'-deoxy-ADP + scyllo-inosamine phosphate
-
2'-dATP + 1-phosphatidyl-1D-myo-inositol = 2'-dADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
-
dATP + 1-phosphatidyl-1D-myo-inositol = dADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate
-
dATP + D-mannose = dADP + D-mannose 6-phosphate
-
2'-deoxyATP + shikimate = 2'-deoxyADP + shikimate 3-phosphate
-
dATP + streptomycin = dADP + streptomycin 6-phosphate
-
dATP + guanosine = dADP + GMP
-
dATP + inosine = dADP + IMP
-
dATP + deoxycytidine = dADP + dCMP
-
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 + deoxyadenosine = dADP + dAMP
-
dATP + 5'-CTAGAGCTACAATTGCGACCG-3' = dADP + 5'-phospho-CTAGAGCTACAATTGCGACCG-3'
dATP + 5'-dephospho-DNA = dADP + 5'-phospho-DNA
dATP + 5'-dephospho-RNA = dADP + 5'-phospho-RNA
dATP + [DNA-directed eukaryotic RNA polymerase II subunit IIa] = dADP + ?
-
dATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = dADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
dATP + carbamate = dADP + carbamoyl phosphate
-
2'-dATP + 3-phospho-D-glycerate = 2'-dADP + 3-phospho-D-glyceroyl phosphate
-
dATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
-
dATP + 3-phospho-D-glycerate = dADP + 1,3-diphosphoglycerate
-
dATP + N-acetyl-L-glutamate = dADP + N-acetyl-L-glutamate 5-phosphate
-
dATP + dGMP = dADP + dGDP
-
dATP + dTMP = dADP + dTDP
-
dATP + CMP = dADP + CDP
-
dATP + dCMP = dADP + dCDP
-
dATP + UMP = dADP + ADP
-
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 + CMP = dADP + CDP
-
dATP + AMP = dADP + ADP
663243, 642602, 642598, 642609, 642592, 642574, 642572, 642567, 642603, 642580, 642582, 673656
-
dATP + dAMP = dADP + dADP
-
dATP + ADP = dADP + ATP
-
dATP + CDP = dADP + CTP
-
dATP + GDP = dADP + GTP
-
dATP + IDP = dADP + ITP
-
dATP + UDP = dADP + UTP
-
dATP + dGMP = dADP + dGDP
-
dATP + GMP = dADP + GDP
-
dATP + dTMP = dADP + dTDP
645196, 645201, 645203, 645188, 645189, 645191, 645193, 645198, 692915, 695005, 737398
-
dATP + UMP = dADP + UDP
-
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 + ADP = dAMP + adenosine 3'-diphosphate 5'-diphosphate
-
dATP + AMP = dAMP + adenosine 3'-diphosphate 5'-phosphate
-
dATP + ApG = dAMP + ApGpp
-
dATP + ApUpG = dAMP + ApUpGpp
-
dATP + ATP = dAMP + adenosine 3'-diphosphate 5'-triphosphate
-
dATP + beta-NADH = dAMP + ?
-
dATP + CTP = dAMP + cytidine 3'-diphosphate 5'-triphosphate
-
dATP + GDP = dAMP + guanosine 3'-diphosphate 5'-diphosphate
-
dATP + GDP-glucose = dAMP + ?
-
dATP + GMP = dAMP + guanosine 3'-diphosphate 5'-phosphate
-
dATP + GpA = dAMP + GpApp
-
dATP + GpG = dAMP + GpGpp
-
dATP + GTP = dAMP + guanosine 3'-diphosphate 5'-triphosphate
-
dATP + IDP = dAMP + inosine 3'-diphosphate 5'-triphosphate
-
dATP + IMP = dAMP + inosine 3'-diphosphate 5'-phosphate
-
dATP + ITP = dAMP + inosine 3'-diphosphate 5'-triphosphate
-
dATP + UDP-glucose = dAMP + ?
-
dATP + UpG = dAMP + UpGpp
-
dATP + UTP = dAMP + uridine 3'-diphosphate 5'-triphosphate
-
dATP + GTP = dAMP + guanosine 3'-diphosphate 5'-triphosphate
-
dATP + nicotinamide ribonucleotide = diphosphate + ?
-
dATP + nicotinamide ribonucleotide = diphosphate + nicotinamide deoxyadenosine dinucleotide
-
deoxy-ATP + nicotinamide ribonucleotide = ?
-
deoxy-ATP + nicotinate ribonucleotide = ?
-
deoxy-ATP + nicotinamide ribonucleotide = ?
-
deoxy-ATP + nicotinate ribonucleotide = ?
-
dATP + RNA = diphosphate + ?
-
dATP + alpha-D-glucosamine 1-phosphate = diphosphate + dADP-alpha-D-glucosamine
dATP + alpha-D-glucose 1-phosphate = dADP-glucose + diphosphate
2'-deoxy-ATP + pantetheine 4'-phosphate = ?
-
dATP + DNAn = diphosphate + DNAn+1
-
dATP + poly(dA)50 = diphosphate + poly(dA)51
-
dATP + SO42- = diphosphate + deoxyadenylylsulfate
-
dATP + tobramycin = diphosphate + 2''-adenylyltobramycin
-
dATP + tobramycin = diphosphate + 2''-deoxyadenylyltobramycin
-
dATP + RNAn = diphosphate + RNAn+1
-
2'-deoxyadenosine 5'-triphosphate + DNAn = diphosphate + DNAn+1
2'-deoxyadenosine 5'-triphosphate + DNAn = diphosphate + DNAn+1
2'-deoxyadenosine 5'-triphosphate + DNAn = diphosphate + DNAn+1
2'-deoxyadenosine 5'-triphosphate + DNAn = diphosphate + DNAn+1
2'-deoxyadenosine 5'-triphosphate + DNAn = diphosphate + DNAn+1
2'-deoxyadenosine 5'-triphosphate + 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 = diphosphate + DNAn+1
2'-deoxy-ATP + RNAn = diphosphate + RNAn+1
-
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
dATP + DNAn = diphosphate + ?
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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = 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 = diphosphate + DNAn+1
dATP + DNAn = diphosphate + DNAn+1
dATP + DNAn = diphosphate + DNAn+1
dATP + DNAn = diphosphate + DNAn+1
dATP + DNAn = diphosphate + DNAn+1
p-tRNAHis + dATP + GTP = pppGp-tRNAHis + dAMP + diphosphate
-
dATP + dATP = dA(pdA)n + n diphosphate
-
dATP + glycerol = dAMP-glycerol + diphosphate
-
dATP + Tris = dAMP-Tris + diphosphate
-
dATP + alpha-D-glucose 1-phosphate = diphosphate + dADP-alpha-D-glucose
-
2'-dATP + pyruvate + phosphate = ?
-
dATP + H2O = ? + phosphate
-
dATP + H2O = dADP + phosphate
-
dATP + H2O = ? + phosphate
-
dATP + H2O = dADP + phosphate
-
dATP + H2O = deoxyadenosine + triphosphate
-
dATP + H2O = deoxyadeonsine + triphosphate
-
dATP + dihydrouracil + H2O = ?
-
dATP + N-methylimidazolidine-2,4-dione + H2O = dADP + phosphate + N-carbamoylsarcosine
-
dATP + H2O = dITP + NH3
-
dATP + H2O = dITP + NH3
-
dATP + H2O = dADP + phosphate
-
dATP + H2O = dADP + phosphate
-
dATP + H2O = dAMP + diphosphate
-
dATP + H2O = dADP + phosphate
-
dATP + H2O = dAMP + diphosphate
-
dATP + 2 H2O = dAMP + 2 phosphate
-
dATP + H2O = dAMP + phosphate
-
dATP + H2O = dAMP + phosphate + H+
-
dATP + H2O = dADP + phosphate
-
dATP + H2O = dAMP + diphosphate
-
dATP + H2O = dAMP + diphosphate
-
dATP + H2O = dAMP + diphosphate
-
dATP + H2O = dAMP + diphosphate
-
dATP + H2O = dAMP + diphosphate
-
dATP + H2O = dADP + phosphate
-
dATP + H2O = dAMP + diphosphate
-
2'-dATP + H2O = 2'-dADP + phosphate
-
dATP + H2O = ADP + phosphate
-
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
-
2'-deoxy-ATP + H2O = 2'-deoxy-ADP + phosphate
-
dATP + H2O = dADP + phosphate
-
dATP + 5-diphosphomevalonate = dADP + phosphate + isopentenyl diphosphate + CO2
-
dATP = deoxy-cAMP + diphosphate
-
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)
-
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)
-
dATP + H2O + closed Cl- channel = dADP + phosphate + open Cl- channel
-
dATP + negatively supercoiled circular DNA = dADP + phosphate + relaxed circular DNA
-
2'-dATP + L-serine + tRNASer = 2'-dAMP + diphosphate + L-seryl-tRNASer
-
dATP + L-serine + tRNASer = dAMP + diphosphate + L-seryl-tRNASer
-
2'-deoxyadenosine 5'-triphosphate + L-arginine + tRNAArg = 2'-deoxyadenosine 5'-monophosphate + diphosphate + L-arginyl-tRNAArg
-
2'-deoxyadenosine 5'-triphosphate + L-phenylalanine + tRNAPhe = 2'-deoxyadenosine 5'-monophosphate + diphosphate + L-phenylalanyl-tRNAPhe
-
dATP + L-histidine + tRNAHis = dAMP + diphosphate + L-histidyl-tRNAHis
-
2'-dATP + L-leucine + tRNALeu = 2'-dAMP + diphosphate + L-leucyl-tRNALeu
-
dATP + lysine + tRNALys = dAMP + L-lysyl-tRNALys + diphosphate
-
dATP + acetate + CoA = dAMP + diphosphate + acetyl-CoA
-
dATP + a fatty acid + [acyl-carrier protein] = dAMP + diphosphate + fatty acid-[acyl-carrier protein]
-
dATP + acetate + citrate (pro-3S)-lyase = dAMP + diphosphate + citrate(pro-3S)-lyase
-
dATP + fatty acid + CoA = dAMP + diphosphate + acyl-CoA
-
dATP + cholate + CoA = dAMP + diphosphate + choloyl-CoA
-
dATP + deamido-NAD+ + NH3 = dAMP + diphosphate + NAD+
-
dATP + 7,8-dihydropteroate + L-Glu = dADP + phosphate + 7,8-dihydrofolate
-
dATP + 5,10-methylene-5,6,7,8-tetrahydropteroyl-Glu + Glu = dADP + phosphate + 5,10-methylene-5,6,7,8-tetrahydropteroyl-gamma-Glu2
-
dATP + 5,6,7,8-tetrahydropteroyl-Glu + Glu = dADP + phosphate + 5,6,7,8-tetrahydropteroyl-Glu2
-
dATP + aminopterin + Glu = dADP + phosphate + aminopteryl-Glu
-
dATP + gamma-Glu-L-Cys + Gly = dADP + phosphate + glutathione
-
dATP + 5-formyltetrahydrofolate = dADP + phosphate + 5,10-methylenetetrahydrofolate
-
deoxyATP + UTP + NH4+ = deoxyADP + phosphate + CTP
-
dATP + formate + tetrahydrofolate = dADP + phosphate + 10-formyltetrahydrofolate
-
dATP + L-citrulline + L-Asp = dAMP + diphosphate + L-argininosuccinate
-
dATP + urea + HCO3- = ?
-
dATP + L-Asp + L-Gln = dAMP + diphosphate + Asn + Glu
-
dATP + L-Asp + NH3 = dAMP + diphosphate + Asn
-
dATP + acetyl-CoA + HCO3- = dADP + phosphate + malonyl-CoA
-
dATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m = dAMP + diphosphate + (deoxyribonucleotide)m+n
-
dATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m = dAMP + diphosphate + (deoxyribonucleotide)n+m
-
dATP + (ribonucleotide)n + (ribonucleotide)m = dAMP + phosphate + (ribonucleotide)n+m
-
dATP + hydrogenobyrinic acid a,c-diamide + Co2+ = dADP + phosphate + cob(II)yrinic acid a,c-diamide + H+
-
dATP + H2O + H+/in = dADP + phosphate + H+/out
-
2'-deoxy-ATP + H2O = 2'-deoxy-ADP + phosphate + H+/out
-
dATP + H2O + H+/in = dADP + phosphate + H+/out
-
2'-deoxyATP + H2O + H+/in + K+/out = 2'-deoxyADP + phosphate + H+/out + K+/in
-
dATP + H2O = dADP + H2O
-
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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
0.2-0.4 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
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
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 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
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
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
-
the enzyme's helicase activity requires ATP or dATP
-
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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