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In
enzymology Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. A ...
, an inosine kinase () is an
enzyme Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. A ...
that
catalyzes Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recyc ...
the
chemical reaction A chemical reaction is a process that leads to the IUPAC nomenclature for organic transformations, chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the pos ...
:ATP + inosine \rightleftharpoons ADP + IMP Thus, the two substrates of this enzyme are ATP and
inosine Inosine is a nucleoside that is formed when hypoxanthine is attached to a ribose ring (also known as a ribofuranose) via a β-N9-glycosidic bond. It was discovered in 1965 in analysis of RNA transferase. Inosine is commonly found in tRNAs and is e ...
, whereas its two
products Product may refer to: Business * Product (business), an item that serves as a solution to a specific consumer problem. * Product (project management), a deliverable or set of deliverables that contribute to a business solution Mathematics * Produ ...
are ADP and
IMP IMP or imp may refer to: * Imp, a fantasy creature Arts and entertainment Fictional characters * Imp (She-Ra), a character in ''She-Ra: Princess of Power'' * Imp a character in '' Artemis Fowl: The Lost Colony'' * Imp, a character in the '' Clan ...
. Inosine kinase belongs to the phosphofructokinase B (PfkB) family of sugar kinases.Park J, Gupta RS: Adenosine kinase and ribokinase--the RK family of proteins. Cell Mol Life Sci 2008, 65: 2875-2896. Other members of this family (also known as the Ribokinase family) include ribokinase (RK) adenosine kinase (AK), fructokinase, and 1-phosphofructokinase.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.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. The members of the PfkB/RK family are identified by the presence of three conserved sequence motifs.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. 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.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. Despite low sequence similarity between inosine kinase and other PfkB family of proteins, these proteins are quite similar at structural levels. Other names in common use include inosine-guanosine kinase, and inosine kinase (phosphorylating). This enzyme participates in
purine metabolism Purine metabolism refers to the metabolic pathways to synthesize and break down purines that are present in many organisms. Biosynthesis Purines are biologically synthesized as nucleotides and in particular as ribotides, i.e. bases attached to ri ...
.


References

* EC 2.7.1 Enzymes of unknown structure {{2.7-enzyme-stub