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Hypoxia-inducible factor-proline dioxygenase

April 13, 2024

Hypoxia-inducible factor-proline dioxygenase (EC 1.14.11.29, HIF hydroxylase) is an enzyme with systematic name hypoxia-inducible factor-L-proline, 2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

Hypoxia-inducible factor-proline dioxygenase
Identifiers
EC no.1.14.11.29
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 hypoxia-inducible factor-trans-4-hydroxy-L-proline + succinate + CO2

Hypoxia-inducible factor-proline dioxygenase contains iron, and requires ascorbate.

Hypoxia-inducible factor (HIF) is an evolutionarily conserved transcription factor[7] that allows the cell to respond physiologically to low concentrations of oxygen.[8] A class of prolyl hydroxylases which act specifically on HIF has been identified;[9] hydroxylation of HIF allows the protein to be targeted for degradation.[9] HIF prolyl-hydroxylase has been targeted by a variety of inhibitors that aim to treat stroke,[10] kidney disease,[11] ischemia,[12] anemia,[13] and other important diseases. Clinically observed prolyl hydroxylase domain mutations, as in the case of erythrocytosis- and breast cancer-associated PHD2 mutations, affect its selectivity for its HIF substrate, which has important implication for drug design.[14]

In humans, there are three isoforms of hypoxia-inducible factor-proline dioxygenase. These are PHD1, PHD2 and PHD3. PHD2, in particular, was identified as the most important human oxygen sensors due to its slow reaction with oxygen.[15]

References edit

  1. ^ Jaakkola, P.; Mole, D.R.; Tian, Y.M.; Wilson, M.I.; Gielbert, J.; Gaskell, S.J.; Kriegsheim Av; Hebestreit, H.F.; Mukherji, M.; Schofield, C.J.; Maxwell, P.H.; Pugh, C.W.; Ratcliffe, P.J. (2001). "Targeting of HIF-α to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation". Science. 292 (5516): 468–472. Bibcode:2001Sci...292..468J. doi:10.1126/science.1059796. PMID 11292861.
  2. ^ Ivan, M.; Kondo, K.; Yang, H.; Kim, W.; Valiando, J.; Ohh, M.; Salic, A.; Asara, J.M.; Lane, W.S.; Kaelin, W.G. (2001). "HIFα targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing". Science. 292 (5516): 464–468. Bibcode:2001Sci...292..464I. doi:10.1126/science.1059817. PMID 11292862.
  3. ^ Bruick, R.K.; McKnight, S.L. (2001). "A conserved family of prolyl-4-hydroxylases that modify HIF". Science. 294 (5545): 1337–1340. Bibcode:2001Sci...294.1337B. doi:10.1126/science.1066373. PMID 11598268.
  4. ^ Epstein, A.C.; Gleadle, J.M.; McNeill, L.A.; Hewitson, K.S.; O'Rourke, J.; Mole, D.R.; Mukherji, M.; Metzen, E.; Wilson, M.I.; Dhanda, A.; Tian, Y.M.; Masson, N.; Hamilton, D.L.; Jaakkola, P.; Barstead, R.; Hodgkin, J.; Maxwell, P.H.; Pugh, C.W.; Schofield, C.J.; Ratcliffe, P.J. (2001). "C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation". Cell. 107 (1): 43–54. doi:10.1016/S0092-8674(01)00507-4. PMID 11595184.
  5. ^ Oehme, F.; Ellinghaus, P.; Kolkhof, P.; Smith, T.J.; Ramakrishnan, S.; Hutter, J.; Schramm, M.; Flamme, I. (2002). "Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors". Biochem. Biophys. Res. Commun. 296 (2): 343–349. doi:10.1016/S0006-291X(02)00862-8. PMID 12163023.
  6. ^ McNeill, L.A.; Hewitson, K.S.; Gleadle, J.M.; Horsfall, L.E.; Oldham, N.J.; Maxwell, P.H.; Pugh, C.W.; Ratcliffe, P.J.; Schofield, C.J. (2002). "The use of dioxygen by HIF prolyl hydroxylase (PHD1)". Bioorg. Med. Chem. Lett. 12 (12): 1547–1550. doi:10.1016/S0960-894X(02)00219-6. PMID 12039559.
  7. ^ Bacon, N. C.; Wappner, P; O'Rourke, J. F.; Bartlett, S. M.; Shilo, B; Pugh, C. W.; Ratcliffe, P. J. (1998). "Regulation of the Drosophila bHLH-PAS protein Sima by hypoxia: Functional evidence for homology with mammalian HIF-1 alpha". Biochemical and Biophysical Research Communications. 249 (3): 811–6. doi:10.1006/bbrc.1998.9234. PMID 9731218.
  8. ^ Smith, T. G.; Robbins, P. A.; Ratcliffe, P. J. (2008). "The human side of hypoxia-inducible factor". British Journal of Haematology. 141 (3): 325–34. doi:10.1111/j.1365-2141.2008.07029.x. PMC 2408651. PMID 18410568.
  9. ^ a b Bruick, R. K. (2001). "A Conserved Family of Prolyl-4-Hydroxylases That Modify HIF". Science. 294 (5545): 1337–40. Bibcode:2001Sci...294.1337B. doi:10.1126/science.1066373. PMID 11598268.
  10. ^ Karuppagounder, S. S.; Ratan, R. R. (2012). "Hypoxia-inducible factor prolyl hydroxylase inhibition: Robust new target or another big bust for stroke therapeutics?". Journal of Cerebral Blood Flow & Metabolism. 32 (7): 1347–1361. doi:10.1038/jcbfm.2012.28. PMC 3390817. PMID 22415525.
  11. ^ Warnecke, C.; Griethe, W.; Weidemann, A.; Jurgensen, J. S.; Willam, C.; Bachmann, S.; Ivashchenko, Y.; Wagner, I.; Frei, U.; Wiesener, M.; Eckardt, K. -U. (2003). "Activation of the hypoxia-inducible factor pathway and stimulation of angiogenesis by application of prolyl hydroxylase inhibitors". The FASEB Journal. 17 (9): 1186–8. doi:10.1096/fj.02-1062fje. PMID 12709400.
  12. ^ Selvaraju, V; Parinandi, N. L.; Adluri, R. S.; Goldman, J. W.; Hussain, N; Sanchez, J. A.; Maulik, N (2013). "Molecular Mechanisms of Action and Therapeutic Uses of Pharmacological Inhibitors of HIF-Prolyl 4-Hydroxylases for Treatment of Ischemic Diseases". Antioxidants & Redox Signaling. 20 (16): 2631–2665. doi:10.1089/ars.2013.5186. PMC 4026215. PMID 23992027.
  13. ^ Muchnik, E; Kaplan, J (2011). "HIF prolyl hydroxylase inhibitors for anemia". Expert Opinion on Investigational Drugs. 20 (5): 645–56. doi:10.1517/13543784.2011.566861. PMID 21406036.
  14. ^ Chowdhury, Rasheduzzaman; Leung, Ivanhoe K. H.; Tian, Ya-Min; Abboud, Martine I.; Ge, Wei; Domene, Carmen; Cantrelle, François-Xavier; Landrieu, Isabelle; Hardy, Adam P. (2016-08-26). "Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases". Nature Communications. 7: 12673. Bibcode:2016NatCo...712673C. doi:10.1038/ncomms12673. PMC 5007464. PMID 27561929.
  15. ^ Berra E, Benizri E, Ginouvès A, Volmat V, Roux D, Pouysségur J (Aug 2003). "HIF prolylhydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1α in normoxia". EMBO J. 22 (16): 4082–4090. doi:10.1093/emboj/cdg392. PMC 175782. PMID 12912907.

External links edit

April 13, 2024
hypoxia, inducible, factor, proline, dioxygenase, hydroxylase, enzyme, with, systematic, name, hypoxia, inducible, factor, proline, oxoglutarate, oxygen, oxidoreductase, hydroxylating, this, enzyme, catalyses, following, chemical, reactionidentifiersec, 29data. Hypoxia inducible factor proline dioxygenase EC 1 14 11 29 HIF hydroxylase is an enzyme with systematic name hypoxia inducible factor L proline 2 oxoglutarate oxygen oxidoreductase 4 hydroxylating 1 2 3 4 5 6 This enzyme catalyses the following chemical reactionHypoxia inducible factor proline dioxygenaseIdentifiersEC no 1 14 11 29DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins hypoxia inducible factor L proline 2 oxoglutarate O2 displaystyle rightleftharpoons hypoxia inducible factor trans 4 hydroxy L proline succinate CO2Hypoxia inducible factor proline dioxygenase contains iron and requires ascorbate Hypoxia inducible factor HIF is an evolutionarily conserved transcription factor 7 that allows the cell to respond physiologically to low concentrations of oxygen 8 A class of prolyl hydroxylases which act specifically on HIF has been identified 9 hydroxylation of HIF allows the protein to be targeted for degradation 9 HIF prolyl hydroxylase has been targeted by a variety of inhibitors that aim to treat stroke 10 kidney disease 11 ischemia 12 anemia 13 and other important diseases Clinically observed prolyl hydroxylase domain mutations as in the case of erythrocytosis and breast cancer associated PHD2 mutations affect its selectivity for its HIF substrate which has important implication for drug design 14 In humans there are three isoforms of hypoxia inducible factor proline dioxygenase These are PHD1 PHD2 and PHD3 PHD2 in particular was identified as the most important human oxygen sensors due to its slow reaction with oxygen 15 References edit Jaakkola P Mole D R Tian Y M Wilson M I Gielbert J Gaskell S J Kriegsheim Av Hebestreit H F Mukherji M Schofield C J Maxwell P H Pugh C W Ratcliffe P J 2001 Targeting of HIF a to the von Hippel Lindau ubiquitylation complex by O2 regulated prolyl hydroxylation Science 292 5516 468 472 Bibcode 2001Sci 292 468J doi 10 1126 science 1059796 PMID 11292861 Ivan M Kondo K Yang H Kim W Valiando J Ohh M Salic A Asara J M Lane W S Kaelin W G 2001 HIFa targeted for VHL mediated destruction by proline hydroxylation implications for O2 sensing Science 292 5516 464 468 Bibcode 2001Sci 292 464I doi 10 1126 science 1059817 PMID 11292862 Bruick R K McKnight S L 2001 A conserved family of prolyl 4 hydroxylases that modify HIF Science 294 5545 1337 1340 Bibcode 2001Sci 294 1337B doi 10 1126 science 1066373 PMID 11598268 Epstein A C Gleadle J M McNeill L A Hewitson K S O Rourke J Mole D R Mukherji M Metzen E Wilson M I Dhanda A Tian Y M Masson N Hamilton D L Jaakkola P Barstead R Hodgkin J Maxwell P H Pugh C W Schofield C J Ratcliffe P J 2001 C elegans EGL 9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation Cell 107 1 43 54 doi 10 1016 S0092 8674 01 00507 4 PMID 11595184 Oehme F Ellinghaus P Kolkhof P Smith T J Ramakrishnan S Hutter J Schramm M Flamme I 2002 Overexpression of PH 4 a novel putative proline 4 hydroxylase modulates activity of hypoxia inducible transcription factors Biochem Biophys Res Commun 296 2 343 349 doi 10 1016 S0006 291X 02 00862 8 PMID 12163023 McNeill L A Hewitson K S Gleadle J M Horsfall L E Oldham N J Maxwell P H Pugh C W Ratcliffe P J Schofield C J 2002 The use of dioxygen by HIF prolyl hydroxylase PHD1 Bioorg Med Chem Lett 12 12 1547 1550 doi 10 1016 S0960 894X 02 00219 6 PMID 12039559 Bacon N C Wappner P O Rourke J F Bartlett S M Shilo B Pugh C W Ratcliffe P J 1998 Regulation of the Drosophila bHLH PAS protein Sima by hypoxia Functional evidence for homology with mammalian HIF 1 alpha Biochemical and Biophysical Research Communications 249 3 811 6 doi 10 1006 bbrc 1998 9234 PMID 9731218 Smith T G Robbins P A Ratcliffe P J 2008 The human side of hypoxia inducible factor British Journal of Haematology 141 3 325 34 doi 10 1111 j 1365 2141 2008 07029 x PMC 2408651 PMID 18410568 a b Bruick R K 2001 A Conserved Family of Prolyl 4 Hydroxylases That Modify HIF Science 294 5545 1337 40 Bibcode 2001Sci 294 1337B doi 10 1126 science 1066373 PMID 11598268 Karuppagounder S S Ratan R R 2012 Hypoxia inducible factor prolyl hydroxylase inhibition Robust new target or another big bust for stroke therapeutics Journal of Cerebral Blood Flow amp Metabolism 32 7 1347 1361 doi 10 1038 jcbfm 2012 28 PMC 3390817 PMID 22415525 Warnecke C Griethe W Weidemann A Jurgensen J S Willam C Bachmann S Ivashchenko Y Wagner I Frei U Wiesener M Eckardt K U 2003 Activation of the hypoxia inducible factor pathway and stimulation of angiogenesis by application of prolyl hydroxylase inhibitors The FASEB Journal 17 9 1186 8 doi 10 1096 fj 02 1062fje PMID 12709400 Selvaraju V Parinandi N L Adluri R S Goldman J W Hussain N Sanchez J A Maulik N 2013 Molecular Mechanisms of Action and Therapeutic Uses of Pharmacological Inhibitors of HIF Prolyl 4 Hydroxylases for Treatment of Ischemic Diseases Antioxidants amp Redox Signaling 20 16 2631 2665 doi 10 1089 ars 2013 5186 PMC 4026215 PMID 23992027 Muchnik E Kaplan J 2011 HIF prolyl hydroxylase inhibitors for anemia Expert Opinion on Investigational Drugs 20 5 645 56 doi 10 1517 13543784 2011 566861 PMID 21406036 Chowdhury Rasheduzzaman Leung Ivanhoe K H Tian Ya Min Abboud Martine I Ge Wei Domene Carmen Cantrelle Francois Xavier Landrieu Isabelle Hardy Adam P 2016 08 26 Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases Nature Communications 7 12673 Bibcode 2016NatCo 712673C doi 10 1038 ncomms12673 PMC 5007464 PMID 27561929 Berra E Benizri E Ginouves A Volmat V Roux D Pouyssegur J Aug 2003 HIF prolylhydroxylase 2 is the key oxygen sensor setting low steady state levels of HIF 1a in normoxia EMBO J 22 16 4082 4090 doi 10 1093 emboj cdg392 PMC 175782 PMID 12912907 External links editHypoxia inducible factor proline dioxygenase at the U S National Library of Medicine Medical Subject Headings MeSH Portal nbsp Biology Retrieved from https en wikipedia org w index php title Hypoxia inducible factor proline dioxygenase amp oldid 1216273351, wikipedia, wiki, book, books, library,

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