Английская Википедия:Inosine kinase

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Шаблон:Short description Шаблон:Infobox enzyme In enzymology, an inosine kinase (Шаблон:EC number) is an enzyme that catalyzes the chemical reaction

ATP + inosine <math>\rightleftharpoons</math> ADP + IMP

Thus, the two substrates of this enzyme are ATP and inosine, whereas its two products are ADP and IMP.

Inosine kinase belongs to the phosphofructokinase B (PfkB) family of sugar kinases.[1] Other members of this family (also known as the Ribokinase family) include ribokinase (RK) adenosine kinase (AK), fructokinase, and 1-phosphofructokinase.[1][2][3] The members of the PfkB/RK family are identified by the presence of three conserved sequence motifs.[1][2][4] The structures of several PfK family of proteins have been determined from a number of organisms and the enzymatic activity of this family of this family of protein shows a dependence on the presence of pentavalent ions.[5][1][4] Despite low sequence similarity between inosine kinase and other PfkB family of proteins, these proteins are quite similar at structural levels.[1] Other names in common use include inosine-guanosine kinase, and inosine kinase (phosphorylating). This enzyme participates in purine metabolism.

References

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Шаблон:2.7-enzyme-stub

  1. 1,0 1,1 1,2 1,3 1,4 Park J, Gupta RS: Adenosine kinase and ribokinase--the RK family of proteins. Cell Mol Life Sci 2008, 65: 2875-2896.
  2. 2,0 2,1 Bork P, Sander C, Valencia A: Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases. Protein Sci 1993, 2: 31-40.
  3. Spychala J, Datta NS, Takabayashi K, Datta M, Fox IH, Gribbin T, Mitchell BS: Cloning of human adenosine kinase cDNA: sequence similarity to microbial ribokinases and fructokinases. Proc Natl Acad Sci U S A 1996, 93: 1232-1237.
  4. 4,0 4,1 Maj MC, Singh B, Gupta RS: Pentavalent ions dependency is a conserved property of adenosine kinase from diverse sources: identification of a novel motif implicated in phosphate and magnesium ion binding and substrate inhibition. Biochemistry 2002, 41: 4059-4069.
  5. Sigrell JA, Cameron AD, Jones TA, Mowbray SL: Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 A resolution: insights into a new family of kinase structures. Structure 1998, 6: 183-193.