Ribokinase

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ribokinase
5byf.jpg
Ribokinase dimer, Human
Identifiers
EC number2.7.1.15
CAS number9026-84-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a ribokinase (EC 2.7.1.15) is an enzyme that catalyzes the chemical reaction

ATP + D-ribose ⇌ ADP + D-ribose 5-phosphate

Thus, the two substrates of this enzyme are ATP and D-ribose, whereas its two products are ADP and D-ribose 5-phosphate.

The systematic name of this enzyme class is ATP:D-ribose 5-phosphotransferase. Other names in common use include deoxyribokinase, ribokinase (phosphorylating), and D-ribokinase. This enzyme participates in pentose phosphate pathway.

Ribokinase (RK) belongs to the phosphofructokinase B (PfkB) family of sugar kinases.[1] Other members of this family (also known as the RK family) include adenosine kinase (AK), inosine-guanosine kinase, fructokinase, and 1-phosphofructokinase.[1][2][3] The members of the PfkB/RK family are identified by the presence of three conserved sequence motifs and the enzymatic activity of this family of protein generally shows a dependence on the presence of pentavalent ions.[1][2][4] The conserved NXXE motif, which is a distinctive property of the PfkB family of proteins, is involved in pentavalent ion dependency. The structures of RK and several other PfK family of proteins have been determined from a number of organisms.[5] Despite low sequence similarity between AdK and other PfkB family of proteins, these proteins are quite similar at structural levels.[1]

Structural studies[edit]

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1GQT​, 1RK2​, 1RKA​, 1RKD​, 1RKS​, 1VM7​, and 2FV7​.

References[edit]

  1. ^ a b c d Park J, Gupta RS (September 2008). "Adenosine kinase and ribokinase--the RK family of proteins". Cellular and Molecular Life Sciences : CMLS. 65 (18): 2875–96. doi:10.1007/s00018-008-8123-1. PMID 18560757.
  2. ^ a b Bork P, Sander C, Valencia A (January 1993). "Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases". Protein Science. 2 (1): 31–40. doi:10.1002/pro.5560020104. PMC 2142297. PMID 8382990.
  3. ^ Spychala J, Datta NS, Takabayashi K, Datta M, Fox IH, Gribbin T, Mitchell BS (February 1996). "Cloning of human adenosine kinase cDNA: sequence similarity to microbial ribokinases and fructokinases". Proceedings of the National Academy of Sciences of the United States of America. 93 (3): 1232–7. PMC 40062. PMID 8577746.
  4. ^ Maj MC, Singh B, Gupta RS (March 2002). "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. 41 (12): 4059–69. PMID 11900549.
  5. ^ Sigrell JA, Cameron AD, Jones TA, Mowbray SL (February 1998). "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. 6 (2): 183–93. PMID 9519409.

Further reading[edit]

  • Agranoff BW, Brady RO (March 1956). "Purification and properties of calf liver ribokinase". The Journal of Biological Chemistry. 219 (1): 221–9. PMID 13295274.
  • Ginsburg A (March 1959). "A deoxyribokinase from Lactobacillus plantarum". The Journal of Biological Chemistry. 234 (3): 481–7. PMID 13641245.