Rujukan Fosfofruktokinase 2

  1. 1 2 "Covalent control of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: insights into autoregulation of a bifunctional enzyme". Protein Science. 4 (6): 1023–37. June 1995. doi:10.1002/pro.5560040601. PMC 2143155. PMID 7549867.
  2. ↑ "A fresh view of glycolysis and glucokinase regulation: history and current status". The Journal of Biological Chemistry. 289 (18): 12189–94. May 2014. doi:10.1074/jbc.R114.557314. PMC 4007419. PMID 24637025.
  3. ↑ "Sequence and structure of the human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase heart isoform gene (PFKFB2)". European Journal of Biochemistry. 254 (1): 103–10. May 1998. doi:10.1046/j.1432-1327.1998.2540103.x. PMID 9652401.
  4. ↑ "An essential methionine residue involved in substrate binding by phosphofructokinases". Biochem. Biophys. Res. Commun. 250 (2): 466–8. September 1998. doi:10.1006/bbrc.1998.9311. PMID 9753654.
  5. 1 2 "6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis". The Biochemical Journal. 381 (Pt 3): 561–79. August 2004. doi:10.1042/BJ20040752. PMC 1133864. PMID 15170386.
  6. 1 2 3 "The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies". Structure. 4 (9): 1017–29. September 1996. doi:10.1016/S0969-2126(96)00109-8. PMID 8805587.
  7. ↑ "Expression of inducible 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase/PFKFB3 isoforms in adipocytes and their potential role in glycolytic regulation". Diabetes. 54 (12): 3349–57. December 2005. doi:10.2337/diabetes.54.12.3349. PMID 16306349.
  8. ↑ "Evolutionary reengineering of the phosphofructokinase active site: ARG-104 does not stabilize the transition state in 6-phosphofructo-2-kinase". Biochemical and Biophysical Research Communications. 213 (2): 663–72. August 1995. doi:10.1006/bbrc.1995.2183. PMID 7646523.
  9. ↑ "Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold". The EMBO Journal. 1 (8): 945–51. 1982. doi:10.1002/j.1460-2075.1982.tb01276.x. PMC 553140. PMID 6329717.
  10. 1 2 "Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2,6-bisphosphatase, acid phosphatase, and alkaline phosphatase". Progress in Biophysics and Molecular Biology. 73 (2–4): 263–87. 2000. doi:10.1016/S0079-6107(00)00007-9. PMID 10958932.
  11. ↑ "Hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. The role of surface loop basic residues in substrate binding to the fructose-2,6-bisphosphatase domain". The Journal of Biological Chemistry. 267 (30): 21588–94. October 1992. doi:10.1016/S0021-9258(19)36651-7. PMID 1328239.
  12. 1 2 Stryer L, Berg JM, Tymoczko JL (2008). "The Balance Between Glycolysis and Gluconeogenesis in the Liver Is Sensitive to Blood-Glucose Concentration". Biochemistry (Looseleaf). San Francisco: W. H. Freeman. m/s. 466–467. ISBN 978-1-4292-3502-0.
  13. ↑ "Significance of the amino terminus of rat testis fructose-6-phosphate, 2-kinase:fructose-2,6-bisphosphatase". The Journal of Biological Chemistry. 268 (21): 15951–7. July 1993. doi:10.1016/S0021-9258(18)82344-4. PMID 8393455.
  14. 1 2 "ENZYME entry 2.7.1.105". enzyme.expasy.org. Dicapai pada 2018-03-24.
  15. ↑ "6-phosphofructo-2-kinase (IPR013079)". InterPro. EMBL-EBI. Dicapai pada 2018-03-25.
  16. 1 2 "ENZYME entry 3.1.3.46". enzyme.expasy.org. Dicapai pada 2018-03-25.
  17. ↑ "PFK-2/FBPase-2: maker and breaker of the essential biofactor fructose-2,6-bisphosphate". Trends in Biochemical Sciences. 26 (1): 30–5. January 2001. doi:10.1016/S0968-0004(00)01699-6. PMID 11165514.
  18. ↑ "Phosphofructokinase 2: the enzyme that forms fructose 2,6-bisphosphate from fructose 6-phosphate and ATP". Biochemical and Biophysical Research Communications. 101 (3): 1078–84. August 1981. doi:10.1016/0006-291X(81)91859-3. PMID 6458291.
  19. ↑ "Balancing glycolytic flux: the role of 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatases in cancer metabolism". Cancer & Metabolism. 1 (1): 8. February 2013. doi:10.1186/2049-3002-1-8. PMC 4178209. PMID 24280138.
  20. ↑ "5' flanking sequence and structure of a gene encoding rat 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase". Proceedings of the National Academy of Sciences of the United States of America. 86 (17): 6543–7. September 1989. Bibcode:1989PNAS...86.6543D. doi:10.1073/pnas.86.17.6543. PMC 297880. PMID 2549541.
  21. 1 2 Salway JG (2017). Metabolism at a Glance. Wiley-Blackwell. ISBN 978-0-470-67471-0.
  22. ↑ Hue L, Rider MH, Rousseau GG (1990). "Fructose-2,6-bisphosphate in extra hepatic tissues". Dalam Pilkis SJ (penyunting). Fructose-2,6-bisphosphate. Boca Raton, Fla.: CRC Press. m/s. 173–193. ISBN 978-0-8493-4795-5.
  23. ↑ "Hormonal regulation of hepatic gluconeogenesis and glycolysis". Annual Review of Biochemistry. 57: 755–83. 1988. doi:10.1146/annurev.bi.57.070188.003543. PMID 3052289.
  24. ↑ "Glucocorticoid regulation of hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene expression". The Journal of Biological Chemistry. 264 (12): 7000–4. April 1989. doi:10.1016/S0021-9258(18)83531-1. PMID 2540168.
  25. ↑ "Identification of a novel Pfkfb1 mRNA variant in rat fetal liver". Biochemical and Biophysical Research Communications. 431 (1): 36–40. February 2013. doi:10.1016/j.bbrc.2012.12.109. PMID 23291237.
Artikel ini menggabungkan teks daripada domain awam Pfam dan InterPro: IPR013079