From Wikipedia, the free encyclopedia
ribokinase
Ribokinase dimer, Human
Identifiers
EC no. 2.7.1.15
CAS no. 9026-84-0
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

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

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

  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. 65 (18): 2875–96. doi: 10.1007/s00018-008-8123-1. PMC  11131688. PMID  18560757. S2CID  11439854.
  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. Bibcode: 1996PNAS...93.1232S. doi: 10.1073/pnas.93.3.1232. 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. doi: 10.1021/bi0119161. 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. doi: 10.1016/s0969-2126(98)00020-3. PMID  9519409.

Further reading


From Wikipedia, the free encyclopedia
ribokinase
Ribokinase dimer, Human
Identifiers
EC no. 2.7.1.15
CAS no. 9026-84-0
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

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

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

  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. 65 (18): 2875–96. doi: 10.1007/s00018-008-8123-1. PMC  11131688. PMID  18560757. S2CID  11439854.
  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. Bibcode: 1996PNAS...93.1232S. doi: 10.1073/pnas.93.3.1232. 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. doi: 10.1021/bi0119161. 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. doi: 10.1016/s0969-2126(98)00020-3. PMID  9519409.

Further reading



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