Publications

• The enzymology of virus-infected bacteria. X. A biochemical-genetic study of the deoxynucleotide kinase induced by wild type and amber mutants of phage T4.

  Duckworth D.H., Bessman M.J.

  J. Biol. Chem. 242:2877-2885(1967) [PubMed] [EuropePMC]

• Identification, cloning, and expression of bacteriophage T5 dnk gene encoding a broad specificity deoxyribonucleoside monophosphate kinase (EC 2.7.4.13).

  Mikoulinskaia G.V., Zimin A.A., Feofanov S.A., Miroshnikov A.I.

  The nucleotide sequence corresponding to 13-19.5% of the bacteriophage T5 genome in early region C was determined (GenBank AY 140897). One of the five major single-stranded interruptions (nicks) of bacteriophage T5 DNA was identified at 18.5%. The sequenced region was annotated and the putative fu ... >> More

  The nucleotide sequence corresponding to 13-19.5% of the bacteriophage T5 genome in early region C was determined (GenBank AY 140897). One of the five major single-stranded interruptions (nicks) of bacteriophage T5 DNA was identified at 18.5%. The sequenced region was annotated and the putative functions of some open reading frames were proposed by comparison with databases. The dnk gene, encoding a deoxyribonucleoside monophosphate kinase, was identified using a previously defined N-terminal amino acid sequence. The gene was cloned and expressed in Escherichia coli, the enzyme was purified to homogeneity with high yield using two alternative methods, and the recombinant deoxyribonucleoside monophosphate kinase was found to have the same activity and specificity as the native enzyme. << Less

  Protein Expr. Purif. 33:166-175(2004) [PubMed] [EuropePMC]

• The human adenylate kinase 9 is a nucleoside mono- and diphosphate kinase.

  Amiri M., Conserva F., Panayiotou C., Karlsson A., Solaroli N.

  Adenylate kinases regulate adenine nucleotide levels and are present in different intracellular compartments. These enzymes also participate in the activation of pharmacologically active nucleoside and nucleotide analogs. We have in the present study identified the ninth isoform of the adenylate k ... >> More

  Adenylate kinases regulate adenine nucleotide levels and are present in different intracellular compartments. These enzymes also participate in the activation of pharmacologically active nucleoside and nucleotide analogs. We have in the present study identified the ninth isoform of the adenylate kinase family of enzymes and accordingly named the protein adenylate kinase 9 (AK9). Initially a full-length cDNA of a hypothetical protein containing a predicted adenylate kinase domain was identified and subsequently cloned and expressed in Escherichia coli. The substrate specificity of the recombinant protein showed that the enzyme catalyzed the phosphorylation of AMP, dAMP, CMP and dCMP with ATP as phosphate donor, while only AMP and CMP were phosphorylated when GTP was the phosphate donor. The kinetic parameters of AK9 were determined for AMP, dAMP and CMP with ATP as phosphate donor. Interestingly, in addition to the diphosphate products, a nucleoside diphosphate kinase (NDPK) activity was also present with subsequent triphosphates formed. With ATP or GTP as phosphate donor it was possible to detect the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and TTP as enzymatic products from the corresponding diphosphate substrates. A number of previously characterized adenylate kinases were also tested and found to possess a broad phosphotransferase activity similar to AK9. These enzymes are accordingly suggested to be regarded as nucleoside mono- and diphosphate kinases with catalytic activities possibly determined by local substrate concentrations. << Less

  Int. J. Biochem. Cell Biol. 45:925-931(2013) [PubMed] [EuropePMC]

  This publication is cited by 23 other entries.

• Crystal structure of bacteriophage T4 deoxynucleotide kinase with its substrates dGMP and ATP.

  Teplyakov A., Sebastiao P., Obmolova G., Perrakis A., Brush G.S., Bessman M.J., Wilson K.S.

  NMP kinases catalyse the phosphorylation of the canonical nucleotides to the corresponding diphosphates using ATP as a phosphate donor. Bacteriophage T4 deoxynucleotide kinase (DNK) is the only member of this family of enzymes that recognizes three structurally dissimilar nucleotides: dGMP, dTMP a ... >> More

  NMP kinases catalyse the phosphorylation of the canonical nucleotides to the corresponding diphosphates using ATP as a phosphate donor. Bacteriophage T4 deoxynucleotide kinase (DNK) is the only member of this family of enzymes that recognizes three structurally dissimilar nucleotides: dGMP, dTMP and 5-hydroxymethyl-dCMP while excluding dCMP and dAMP. The crystal structure of DNK with its substrate dGMP has been determined at 2.0 A resolution by single isomorphous replacement. The structure of the ternary complex with dGMP and ATP has been determined at 2.2 A resolution. The polypeptide chain of DNK is folded into two domains of equal size, one of which resembles the mononucleotide binding motif with the glycine-rich P-loop. The second domain, consisting of five alpha-helices, forms the NMP binding pocket. A hinge connection between the domains allows for large movements upon substrate binding which are not restricted by dimerization of the enzyme. The mechanism of active centre formation via domain closure is described. Comparison with other P-loop-containing proteins indicates an induced-fit mode of NTP binding. Protein-substrate interactions observed at the NMP and NTP sites provide the basis for understanding the principles of nucleotide discrimination. << Less

  EMBO J. 15:3487-3497(1996) [PubMed] [EuropePMC]

• THE ENZYMOLOGY OF VIRUS-INFECTED BACTERIA. VI. PURIFICATION AND PROPERTIES OF THE DEOXYNUCLEOTIDE KINASE INDUCED BY BACTERIOPHAGE T5.

  BESSMAN M.J., HERRIOTT S.T., ORR M.J.

  J Biol Chem 240:439-445(1965) [PubMed] [EuropePMC]