[{"scheme":"dUDP + ATP -> dUTP + ADP + H+","substrates":{"s1":{"theSubstance":{"name":"dUDP","type":"substance","synonyms":["2'-Deoxyuridine 5'-diphosphate","dUDP"],"links":[],"id":"SS0000049"},"theState":null,"compartment":""},"s2":{"theSubstance":{"name":"ATP","type":"substance","synonyms":["Adenosine 5'-triphosphate","ATP"],"links":[],"id":"SS0000065"},"theState":null,"compartment":""}},"products":{"p1":{"theSubstance":{"name":"dUTP","type":"substance","synonyms":["2'-Deoxyuridine 5'-triphosphate","dUTP"],"links":[],"id":"SS0000048"},"theState":null,"compartment":""},"p2":{"theSubstance":{"name":"ADP","type":"substance","synonyms":["Adenosine 5'-diphosphate","ADP"],"links":[],"id":"SS0000069"},"theState":null,"compartment":""},"p3":{"theSubstance":{"name":"H+","type":"substance","synonyms":["H","H+","hydrogen ion","proton"],"links":[],"id":"SS0000063"},"theState":null,"compartment":""}},"regulators":{"r1":{"theSubstance":{"name":"Ndk","type":"protein","synonyms":["Ndk","NDP kinase","nucleoside diphosphate kinase"],"links":[],"id":"SS0000154"},"theState":null,"compartment":"","theInfluence":"enzyme"}},"theMathModel":"(r1*kcat*(s1/kmdudp)*(s2/kmatp))/((1+(s1/kmdudp))*(1+(s2/kmatp)))","theSubMathModel":null,"theInformation":{"Mathematical model information":"dUDP is phosphorylated to dUTP [Roisin et al., 1978, Ginther et al., 1974, Jong et al., 1991]. We proposed a simple model without competitive substrates such as dCDP,dGDP,dADP... as they are rapidly consumed in their reactions.","Mathematical model links":" ID: Ginther et al., 1974 Nucleoside diphosphokinase of Salmonella typhimurium. ; Value:http://www.ncbi.nlm.nih.gov/pubmed/4364654 ; ID: Jong et al., 1991 Saccharomyces cerevisiae nucleoside-diphosphate kinase: purification, characterization, and substrate specificity. ; Value:http://www.ncbi.nlm.nih.gov/pubmed/1659321 ; ID: Roisin et al., 1978 Nucleosidediphosphate kinase of Escherichia coli, a periplasmic enzyme. ; Value:http://www.ncbi.nlm.nih.gov/pubmed/214126 ;","Parameter set information":"Parameters kmdudp and kmatp were evaluated basing on [Roisin, 1978] data.","Parameter set links":" ID: Roisin et al., 1978 Nucleosidediphosphate kinase of Escherichia coli, a periplasmic enzyme. ; Value:http://www.ncbi.nlm.nih.gov/pubmed/214126 ;","Structural model information":" Nucleoside diphosphate kinase catalyzes the reaction in which the terminal phosphate of a nucleoside-triphosphate is transferred to a nucleoside-diphosphate. The enzyme exhibits broad substrate specificity. The reaction mechanism is an ordered bi-molecular ping-pong type. The intracellular levels of ATP are considerably higher than other nucleoside triphosphates. In addition, ATP is far more abundant than ADP or AMP, so there is a strong thermodynamic tendency for the potential energy of ATP to be used in the synthesis of other high-energy compounds. Therefore nucleoside diphosphate kinase is unlikely to be involved in the synthesis of ATP. The purified enzyme is tetrameric and was detected in the periplasmic fraction after cold osmotic shock. A periplasmic location for the enzyme appears inconsistent with its function. ","Structural model links":" ID: EcoCyc ; Value:http://biocyc.org/ECOLI/NEW-IMAGE?type=REACTION&object=DUDPKIN-RXN ;"},"mmid":"MM0000130","psid":"PS0000160","gnid":"GN0000067","reversible":false,"information":{"Mathematical model information":"dUDP is phosphorylated to dUTP [Roisin et al., 1978, Ginther et al., 1974, Jong et al., 1991]. We proposed a simple model without competitive substrates such as dCDP,dGDP,dADP... as they are rapidly consumed in their reactions.","Mathematical model links":" ID: Ginther et al., 1974 Nucleoside diphosphokinase of Salmonella typhimurium. ; Value:http://www.ncbi.nlm.nih.gov/pubmed/4364654 ; ID: Jong et al., 1991 Saccharomyces cerevisiae nucleoside-diphosphate kinase: purification, characterization, and substrate specificity. ; Value:http://www.ncbi.nlm.nih.gov/pubmed/1659321 ; ID: Roisin et al., 1978 Nucleosidediphosphate kinase of Escherichia coli, a periplasmic enzyme. ; Value:http://www.ncbi.nlm.nih.gov/pubmed/214126 ;","Parameter set information":"Parameters kmdudp and kmatp were evaluated basing on [Roisin, 1978] data.","Parameter set links":" ID: Roisin et al., 1978 Nucleosidediphosphate kinase of Escherichia coli, a periplasmic enzyme. ; Value:http://www.ncbi.nlm.nih.gov/pubmed/214126 ;","Structural model information":" Nucleoside diphosphate kinase catalyzes the reaction in which the terminal phosphate of a nucleoside-triphosphate is transferred to a nucleoside-diphosphate. The enzyme exhibits broad substrate specificity. The reaction mechanism is an ordered bi-molecular ping-pong type. The intracellular levels of ATP are considerably higher than other nucleoside triphosphates. In addition, ATP is far more abundant than ADP or AMP, so there is a strong thermodynamic tendency for the potential energy of ATP to be used in the synthesis of other high-energy compounds. Therefore nucleoside diphosphate kinase is unlikely to be involved in the synthesis of ATP. The purified enzyme is tetrameric and was detected in the periplasmic fraction after cold osmotic shock. A periplasmic location for the enzyme appears inconsistent with its function. ","Structural model links":" ID: EcoCyc ; Value:http://biocyc.org/ECOLI/NEW-IMAGE?type=REACTION&object=DUDPKIN-RXN ;"},"parameters":[{"units":"1/sec","information":"","name":"kcat","value":"1"},{"units":"mM","information":"","name":"kmatp","value":"1.43"},{"units":"mM","information":"","name":"kmdudp","value":"0.47"}]}]