| 词条 | Ribokinase |
| 释义 |
| Name = ribokinase | EC_number = 2.7.1.15 | CAS_number = 9026-84-0 | IUBMB_EC_number = 2/7/1/15 | GO_code = 0004747 | image = 5byf.jpg | width = 270 | caption = Ribokinase dimer, Human }} In enzymology, a ribokinase ({{EC number|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 studiesAs of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes {{PDB2|1GQT}}, {{PDB2|1RK2}}, {{PDB2|1RKA}}, {{PDB2|1RKD}}, {{PDB2|1RKS}}, {{PDB2|1VM7}}, and {{PDB2|2FV7}}. References1. ^1 2 3 {{cite journal | vauthors = Park J, Gupta RS | title = Adenosine kinase and ribokinase--the RK family of proteins | journal = Cellular and Molecular Life Sciences : CMLS | volume = 65 | issue = 18 | pages = 2875–96 | date = September 2008 | pmid = 18560757 | doi = 10.1007/s00018-008-8123-1 }} 2. ^1 {{cite journal | vauthors = Bork P, Sander C, Valencia A | title = Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases | journal = Protein Science | volume = 2 | issue = 1 | pages = 31–40 | date = January 1993 | pmid = 8382990 | pmc = 2142297 | doi = 10.1002/pro.5560020104 }} 3. ^{{cite journal | vauthors = Spychala J, Datta NS, Takabayashi K, Datta M, Fox IH, Gribbin T, Mitchell BS | title = Cloning of human adenosine kinase cDNA: sequence similarity to microbial ribokinases and fructokinases | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 93 | issue = 3 | pages = 1232–7 | date = February 1996 | pmid = 8577746 | pmc = 40062 | doi = }} 4. ^{{cite journal | vauthors = Maj MC, Singh B, Gupta RS | title = 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 | journal = Biochemistry | volume = 41 | issue = 12 | pages = 4059–69 | date = March 2002 | pmid = 11900549 | doi = }} 5. ^{{cite journal | vauthors = Sigrell JA, Cameron AD, Jones TA, Mowbray SL | title = 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 | journal = Structure | volume = 6 | issue = 2 | pages = 183–93 | date = February 1998 | pmid = 9519409 | doi = }} Further reading{{refbegin}}
2 : EC 2.7.1|Enzymes of known structure |
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