292:
study ligand binding, enzyme kinetics, modes of inhibition as well as protein conformational change. Mass spectrometry is also widely applied. It can be used to characterise enzyme kinetics, to guide enzyme inhibitor development, study ligand and metal binding as well as analyse protein conformational change. Assays using spectrophotometry were also used, for example those that measure 2OG oxidation, co-product succinate formation or product formation. Other biophysical techniques including (but not limited to) isothermal titration calorimetry (ITC) and electron paramagnetic resonance (EPR) were also applied. Radioactive assays that uses C labelled substrates were also developed and used. Given αKG-dependent dioxygenases require oxygen for their catalytic activity, oxygen consumption assay was also applied.
263:(NOG), pyridine-2,4-dicarboxylic acid (2,4-PDCA), 5-carboxy-8-hydroxyquinoline, FG-2216 and FG-4592, which were all designed mimic the co-substrate αKG and compete against the binding of αKG at the enzyme active site Fe(II). Although they are potent inhibitors of αKG-dependent dioxygenase, they lack selectivity and hence sometimes being referred to as so-called 'broad spectrum' inhibitors. Inhibitors that compete against the substrate were also developed, such as peptidyl-based inhibitors that target human
54:. In plants, αKG-dependent dioxygenases are involved in diverse reactions in plant metabolism. These include flavonoid biosynthesis, and ethylene biosyntheses. In mammals and humans, αKG-dependent dioxygenase have functional roles in biosyntheses (e.g. collagen biosynthesis and L-carnitine biosynthesis), post-translational modifications (e.g. protein hydroxylation), epigenetic regulations (e.g.
275:. Finally, as αKG-dependent dioxygenases require molecular oxygen as a co-substrate, it has also been shown that gaseous molecules such as carbon monoxide and nitric oxide are inhibitors of αKG-dependent dioxygenases, presumably by competing with molecular oxygen for the binding at the active site Fe(II) ion.
152:
The first step involves the binding of αKG and substrate to the active site. αKG coordinates as a bidentate ligand to Fe(II), while the substrate is held by noncovalent forces in close proximity. Subsequently, molecular oxygen binds end-on to Fe cis to the two donors of the αKG. The uncoordinated end
69:
Many αKG-dependent dioxygenase also catalyse uncoupled turnover, in which oxidative decarboxylation of αKG into succinate and carbon dioxide proceeds in the absence of substrate. The catalytic activity of many αKG-dependent dioxygenases are dependent on reducing agents (especially ascorbate) although
291:
Many assays were developed to study αKG-dependent dioxygenases so that information such as enzyme kinetics, enzyme inhibition and ligand binding can be obtained. Nuclear magnetic resonance (NMR) spectroscopy is widely applied to study αKG-dependent dioxygenases. For example, assays were developed to
2210:
Hopkinson RJ, Tumber A, Yapp C, Chowdhury R, Aik W, Che KH, Li XS, Kristensen JB, King ON, Chan MC, Yeoh KK, Choi H, Walport LJ, Thinnes CC, Bush JT, Lejeune C, Rydzik AM, Rose NR, Bagg EA, McDonough MA, Krojer T, Yue WW, Ng SS, Olsen L, Brennan PE, Oppermann U, Muller-Knapp S, Klose RJ, Ratcliffe
470:
Price JC, Barr EW, Tirupati B, Bollinger JM Jr, Krebs C (June 2003). "The first direct characterization of a high-valent iron intermediate in the reaction of an alpha-ketoglutarate-dependent dioxygenase: a high-spin FeIV complex in taurine/alpha-ketoglutarate dioxygenase (TauD) from
Escherichia
172:
238:
2946:
Demetriades M, Leung IK, Chowdhury R, Chan MC, McDonough MA, Yeoh KK, Tian YM, Claridge TD, Ratcliffe PJ, Woon EC, Schofield CJ (July 2012). "Dynamic combinatorial chemistry employing boronic acids/boronate esters leads to potent oxygenase inhibitors".
3025:
Stubbs CJ, Loenarz C, Mecinović J, Yeoh KK, Hindley N, Liénard BM, Sobott F, Schofield CJ, Flashman E (May 2009). "Application of a proteolysis/mass spectrometry method for investigating the effects of inhibitors on hydroxylase structure".
201:
The active site contains a highly conserved 2-His-1-carboxylate (HXD/E...H) amino acid residue triad motif, in which the catalytically-essential Fe(II) is held by two histidine residues and one aspartic acid/glutamic acid residue. The
2156:
Yeh TL, Leissing TM, Abboud MI, Thinnes CC, Atasoylu O, Holt-Martyn JP, Zhang D, Tumber A, Lippl K, Lohans CT, Leung IK, Morcrette H, Clifton IJ, Claridge TD, Kawamura A, Flashman E, Lu X, Ratcliffe PJ, Chowdhury R, Pugh CW,
2397:
Hayashi Y, Kirimoto T, Asaka N, Nakano M, Tajima K, Miyake H, Matsuura N (May 2000). "Beneficial effects of MET-88, a gamma-butyrobetaine hydroxylase inhibitor in rats with heart failure following myocardial infarction".
23:
that catalyse a wide range of reactions. These reactions include hydroxylation reactions, demethylations, ring expansions, ring closures, and desaturations. Functionally, the αKG-dependent hydroxylases are comparable to
258:
Given the important biological roles that αKG-dependent dioxygenase play, many αKG-dependent dioxygenase inhibitors were developed. The inhibitors that were regularly used to target αKG-dependent dioxygenase include
3181:
Rydzik AM, Leung IK, Kochan GT, Thalhammer A, Oppermann U, Claridge TD, Schofield CJ (July 2012). "Development and application of a fluoride-detection-based fluorescence assay for γ-butyrobetaine hydroxylase".
3145:
Luo L, Pappalardi MB, Tummino PJ, Copeland RA, Fraser ME, Grzyska PK, Hausinger RP (June 2006). "An assay for Fe(II)/2-oxoglutarate-dependent dioxygenases by enzyme-coupled detection of succinate formation".
222:
The binding of αKG and substrate has been analyzed by X-ray crystallography, molecular dynamics calculations, and NMR spectroscopy. The binding of the ketoglutarate has been observed using enzyme inhibitors.
2433:
Mbenza NM, Nasarudin N, Vadakkedath PG, Patel K, Ismail AZ, Hanif M, Wright LJ, Sarojini V, Hartinger CG, Leung IK (June 2021). "Carbon monoxide is an inhibitor of HIF prolyl hydroxylase domain 2".
245:(PHD2), a human αKG-dependent dioxygenase. The Fe(II) is coordinated by two imidazoles and one carboxylate provided by the protein. Other ligands on iron, which are transiently occupied αKG and O
500:
Proshlyakov DA, Henshaw TF, Monterosso GR, Ryle MJ, Hausinger RP (February 2004). "Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/alpha-ketoglutarate dioxygenase".
226:
Some αKG-dependent dioxygenases bind their substrate through an induced fit mechanism. For example, significant protein structural changes have been observed upon substrate binding for human
842:
Scotti JS, Leung IK, Ge W, Bentley MA, Paps J, Kramer HB, Lee J, Aik W, Choi H, Paulsen SM, Bowman LA, Loik ND, Horita S, Ho CH, Kershaw NJ, Tang CM, Claridge TD, Preston GM, McDonough MA,
40:αKG-dependent hydroxylases have diverse roles. In microorganisms such as bacteria, αKG-dependent dioxygenases are involved in many biosynthetic and metabolic pathways; for example, in
2899:"Kinetic rationale for selectivity toward N- and C-terminal oxygen-dependent degradation domain substrates mediated by a loop region of hypoxia-inducible factor prolyl hydroxylases"
2982:
Mecinović J, Chowdhury R, Liénard BM, Flashman E, Buck MR, Oldham NJ, Schofield CJ (April 2008). "ESI-MS studies on prolyl hydroxylase domain 2 reveal a new metal binding site".
2029:
William C, Nicholls L, Ratcliffe P, Pugh C, Maxwell P (2004). "The prolyl hydroxylase enzymes that act as oxygen sensors regulating destruction of hypoxia-inducible factor α".
529:
Hewitson KS, Granatino N, Welford RW, McDonough MA, Schofield CJ (April 2005). "Oxidation by 2-oxoglutarate oxygenases: non-haem iron systems in catalysis and signalling".
1852:
McDonough MA, Li V, Flashman E, Chowdhury R, Mohr C, Liénard BM, Zondlo J, Oldham NJ, Clifton IJ, Lewis J, McNeill LA, Kurzeja RJ, Hewitson KS, Yang E, Jordan S, Syed RS,
1536:"Investigating the dependence of the hypoxia-inducible factor hydroxylases (factor inhibiting HIF and prolyl hydroxylase domain 2) on ascorbate and other reducing agents"
1434:"2-Oxoglutarate-dependent dioxygenases are sensors of energy metabolism, oxygen availability, and iron homeostasis: potential role in the regulation of aging process"
1580:(September 2005). "Incorporation of oxygen into the succinate co-product of iron(II) and 2-oxoglutarate dependent oxygenases from bacteria, plants and humans".
2350:"Mildronate, an inhibitor of carnitine biosynthesis, induces an increase in gamma-butyrobetaine contents and cardioprotection in isolated rat heart infarction"
2807:"Different modes of inhibitor binding to prolyl hydroxylase by combined use of X-ray crystallography and NMR spectroscopy of paramagnetic complexes"
2584:
Mbenza NM, Vadakkedath PG, McGillivray DJ, Leung IK (December 2017). "NMR studies of the non-haem Fe(II) and 2-oxoglutarate-dependent oxygenases".
2762:(March 2010). "Monitoring the activity of 2-oxoglutarate dependent histone demethylases by NMR spectroscopy: direct observation of formaldehyde".
1688:, Flashman E (April 2014). "Studies on deacetoxycephalosporin C synthase support a consensus mechanism for 2-oxoglutarate dependent oxygenases".
279:
2264:
Kwon HS, Choi YK, Kim JW, Park YK, Yang EG, Ahn DR (July 2011). "Inhibition of a prolyl hydroxylase domain (PHD) by substrate analog peptides".
807:(January 2011). "Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases".
2301:"Mildronate, a novel fatty acid oxidation inhibitor and antianginal agent, reduces myocardial infarct size without affecting hemodynamics"
1054:"Protein Dynamics Control the Progression and Efficiency of the Catalytic Reaction Cycle of the Escherichia coli DNA-Repair Enzyme AlkB"
3110:
McNeill LA, Bethge L, Hewitson KS, Schofield CJ (January 2005). "A fluorescence-based assay for 2-oxoglutarate-dependent oxygenases".
995:"Enzymological and structural studies of the mechanism of promiscuous substrate recognition by the oxidative DNA repair enzyme AlkB"
282:
Common inhibitors of αKG-dependent dioxygenases. They compete against the cosubstrate αKG for binding to the active site Fe(II).
1211:"Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase - the ethylene-forming enzyme"
272:
3318:"Assay of prolyl 4-hydroxylase by the chromatographic determination of [14C]succinic acid on ion-exchange minicolumns"
2676:, Claridge TD (January 2010). "Using NMR solvent water relaxation to investigate metalloenzyme-ligand binding interactions".
1491:"Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase"
1535:
3425:
206:
O triad binds to one face of the Fe center, leaving three labile sites available on the octahedron for binding αKG and O
768:
Prescott AG, Lloyd MD (August 2000). "The iron(II) and 2-oxoacid-dependent dioxygenases and their role in metabolism".
1766:(April 2006). "Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins".
78:αKG-dependent dioxygenases catalyse oxidation reactions by incorporating a single oxygen atom from molecular oxygen (O
2217:"5-Carboxy-8-hydroxyquinoline is a Broad Spectrum 2-Oxoglutarate Oxygenase Inhibitor which Causes Iron Translocation"
1052:
Ergel, Burçe; Gill, Michelle L.; Brown, Lewis; Yu, Bomina; Palmer, III, Arthur G.; Hunt, John F. (24 October 2014).
2897:
Flashman E, Bagg EA, Chowdhury R, Mecinović J, Loenarz C, McDonough MA, Hewitson KS, Schofield CJ (February 2008).
190:
2537:"Nitric oxide modulates oxygen sensing by hypoxia-inducible factor 1-dependent induction of prolyl hydroxylase 2"
427:
2845:
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2712:
2673:
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2212:
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2118:
2065:
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1331:
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959:
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843:
804:
623:
231:
162:
426:
Valegård K, Terwisscha van
Scheltinga AC, Dubus A, Ranghino G, Oster LM, Hajdu J, Andersson I (January 2004).
357:"The 2-His-1-carboxylate facial triad--an emerging structural motif in mononuclear non-heme iron(II) enzymes"
1156:"The function and catalysis of 2-oxoglutarate-dependent oxygenases involved in plant flavonoid biosynthesis"
674:
Hausinger RP (January–February 2004). "Fe(II)/α-ketoglutarate-dependent hydroxylases and related enzymes".
3365:
Ehrismann D, Flashman E, Genn DN, Mathioudakis N, Hewitson KS, Ratcliffe PJ, Schofield CJ (January 2007).
3269:"Screening chelating inhibitors of HIF-prolyl hydroxylase domain 2 (PHD2) and factor inhibiting HIF (FIH)"
2070:"Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation"
3227:"The different catalytic roles of the metal-binding ligands in human 4-hydroxyphenylpyruvate dioxygenase"
3367:"Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay"
1635:"Insight into the mechanism of an iron dioxygenase by resolution of steps following the FeIV=HO species"
20:
1985:
1869:
1006:
859:
538:
211:
63:
1925:"Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases"
2717:"Development and application of ligand-based NMR screening assays for γ-butyrobetaine hydroxylase"
1858:"Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)"
3207:
3007:
2928:
2787:
2566:
2468:
2379:
2330:
2099:
1615:
1471:
940:
699:
562:
458:
848:"Human oxygen sensing may have origins in prokaryotic elongation factor Tu prolyl-hydroxylation"
2348:
Liepinsh E, Vilskersts R, Loca D, Kirjanova O, Pugovichs O, Kalvinsh I, Dambrova M (Dec 2006).
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3347:
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1312:
1285:
Leung IK, Krojer TJ, Kochan GT, Henry L, von Delft F, Claridge TD, Oppermann U, McDonough MA,
1267:
1250:
Myllyharju J (March 2003). "Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis".
1232:
1187:
1136:
1085:
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2001:
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1347:
1302:
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1177:
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1116:
1075:
1065:
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967:
922:
877:
867:
816:
777:
740:
730:
683:
639:
587:
546:
509:
480:
442:
404:
393:"Mechanism of the prolyl hydroxylase reaction. 2. Kinetic analysis of the reaction sequence"
368:
333:
315:
90:
as substrate, the one label appears in the succinate and one in the hydroxylated substrate:
41:
2163:"Molecular and cellular mechanisms of HIF prolyl hydroxylase inhibitors in clinical trials"
1974:"Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases"
1684:
Tarhonskaya H, Szöllössi A, Leung IK, Bush JT, Henry L, Chowdhury R, Iqbal A, Claridge TD,
373:
356:
2488:"Nitric Oxide Impairs Normoxic Degradation of HIF-1α by Inhibition of Prolyl Hydroxylases"
1803:"Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis"
1105:"Functional diversity of 2-oxoglutarate/Fe(II)-dependent dioxygenases in plant metabolism"
278:
260:
82:) into their substrates. This conversion is coupled with the oxidation of the cosubstrate
25:
2805:
Poppe L, Tegley CM, Li V, Lewis J, Zondlo J, Yang E, Kurzeja RJ, Syed R (November 2009).
576:"Structural Insight into the Prolyl Hydroxylase PHD2: A Molecular Dynamics and DFT Study"
1989:
1873:
1458:
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1010:
863:
542:
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3293:
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2006:
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83:
2844:
Bleijlevens B, Shivarattan T, Flashman E, Yang Y, Simpson PJ, Koivisto P, Sedgwick B,
2512:
2487:
2411:
1507:
1490:
1263:
745:
718:
3414:
3063:"Spectroscopic analyses of 2-oxoglutarate-dependent oxygenases: TauD as a case study"
2472:
2103:
1965:
1916:
1602:
3284:
3211:
3011:
2932:
2791:
2597:
2570:
2334:
2042:
1779:
1727:(December 2010). "Structural studies on human 2-oxoglutarate dependent oxygenases".
1619:
1475:
703:
2383:
1307:
1290:
1227:
1210:
944:
566:
462:
210:. A similar facial Fe-binding motif, but featuring his-his-his array, is found in
3226:
1593:
2619:
Leung IK, Demetriades M, Hardy AP, Lejeune C, Smart TJ, Szöllössi A, Kawamura A,
428:"The structural basis of cephalosporin formation in a mononuclear ferrous enzyme"
271:, a drug molecule that is commonly used in Russia and Eastern Europe that target
2277:
1410:
820:
3078:
2625:"Reporter ligand NMR screening method for 2-oxoglutarate oxygenase inhibitors"
1941:
1924:
1740:
1449:
1397:(December 2012). "Mechanisms of human histone and nucleic acid demethylases".
687:
268:
3159:
3123:
1361:
329:
2503:
1915:
Chowdhury R, McDonough MA, Mecinović J, Loenarz C, Flashman E, Hewitson KS,
1882:
1651:
1489:
Myllylä R, Majamaa K, Günzler V, Hanauske-Abel HM, Kivirikko KI (May 1984).
1352:
1121:
1070:
1019:
872:
735:
644:
627:
320:
230:(PHD2), a αKG-dependent dioxygenase that is involved in oxygen sensing, and
3400:
3302:
3253:
3203:
3195:
3167:
3131:
3096:
3047:
3003:
2995:
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2015:
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1191:
1140:
1089:
1038:
979:
936:
927:
910:
891:
828:
789:
754:
695:
653:
592:
575:
558:
550:
521:
492:
454:
347:
175:
Consensus catalytic mechanism of the αKG-dependent dioxygenase superfamily.
3351:
2095:
1968:, Cantrelle FX, Landrieu I, Hardy AP, Pugh CW, Ratcliffe PJ, Claridge TD,
1516:
962:(September 2005). "The enzymology of clavam and carbapenem biosynthesis".
382:
3225:
Huang CW, Liu HC, Shen CP, Chen YT, Lee SJ, Lloyd MD, Lee HJ (May 2016).
1172:
418:
304:"Catalytic Mechanisms of Fe(II)- and 2-Oxoglutarate-dependent Oxygenases"
3245:
2535:
Berchner-Pfannschmidt U, Yamac H, Trinidad B, Fandrey J (January 2007).
2455:
1997:
1336:"Protein Hydroxylation Catalyzed by 2-Oxoglutarate-dependent Oxygenases"
153:
of the superoxide ligand attacks the keto carbon, inducing release of CO
3382:
3267:
Flagg SC, Martin CB, Taabazuing CY, Holmes BE, Knapp MJ (August 2012).
2850:"Dynamic states of the DNA repair enzyme AlkB regulate product release"
2733:
2716:
2711:
Khan A, Leśniak RK, Brem J, Rydzik AM, Choi H, Leung IK, McDonough MA,
2232:
2178:
2134:
1554:
55:
3333:
3039:
2822:
2743:
2689:
2640:
1701:
513:
484:
971:
781:
193:(DSBH, also known as cupin) fold, which is formed with two β-sheets.
2121:(August 2011). "Inhibition of 2-oxoglutarate dependent oxygenases".
1633:
Grzyska PK, Appelman EH, Hausinger RP, Proshlyakov DA (March 2010).
446:
1291:"Structural and mechanistic studies on γ-butyrobetaine hydroxylase"
2086:
2069:
277:
264:
242:
236:
227:
170:
32:
and reducing equivalents as cosubstrates and both generate water.
574:
Wick CR, Lanig H, Jäger CM, Burzlaff N, Clark T (November 2012).
2486:
Metzen E, Zhou J, Jelkmann W, Fandrey J, Brüne B (August 2003).
1762:
Clifton IJ, McDonough MA, Ehrismann D, Kershaw NJ, Granatino N,
905:
Clifton IJ, Doan LX, Sleeman MC, Topf M, Suzuki H, Wilmouth RC,
47:
59:
51:
1801:
You, Z.; Omura, S.; Ikeda, H.; Cane, D.E.; Jogl, G. (2007).
1576:
Welford RW, Kirkpatrick JM, McNeill LA, Puri M, Oldham NJ,
2299:
Sesti C, Simkhovich BZ, Kalvinsh I, Kloner RA (Mar 2006).
3061:
Proshlyakov DA, McCracken J, Hausinger RP (April 2016).
161:. This Fe=O center then oxygenates the substrate by an
3316:
Cunliffe CJ, Franklin TJ, Gaskell RM (December 1986).
302:
Martinez, Salette; Hausinger, Robert P. (2015-08-21).
391:
Myllylä R, Tuderman L, Kivirikko KI (November 1977).
719:"Non-heme iron enzymes: contrasts to heme catalysis"
168:
Alternative mechanisms have failed to gain support.
999:
Proceedings of the
National Academy of Sciences USA
628:"The most versatile of all reactive intermediates?"
189:All αKG-dependent dioxygenases contain a conserved
1723:McDonough MA, Loenarz C, Chowdhury R, Clifton IJ,
1432:Salminen, A; Kauppinen, A; Kaarniranta, K (2015).
86:into succinate and carbon dioxide. With labeled O
1964:Chowdhury R, Leung IK, Tian YM, Abboud MI, Ge W,
911:"Crystal structure of carbapenem synthase (CarC)"
1154:Cheng AX, Han XJ, Wu YF, Lou HX (January 2014).
50:enzyme is associated with the repair of damaged
617:
615:
613:
611:
234:(IPNS), a microbial αKG-dependent dioxygenase.
2758:Hopkinson RJ, Hamed RB, Rose NR, Claridge TD,
2064:Roach PL, Clifton IJ, Hensgens CM, Shibata N,
717:Solomon EI, Decker A, Lehnert N (April 2003).
669:
667:
665:
663:
8:
2117:Rose NR, McDonough MA, King ON, Kawamura A,
993:Yu, Bomina; Hunt, John F. (25 August 2009).
17:Alpha-ketoglutarate-dependent hydroxylases
3390:
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2648:
2552:
2511:
2454:
2365:
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2186:
2085:
2005:
1940:
1891:
1881:
1828:
1818:
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1650:
1601:
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1181:
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1079:
1069:
1028:
1018:
926:
881:
871:
744:
734:
643:
591:
408:
372:
337:
319:
1330:Markolovic, Suzana; Wilkins, Sarah E.;
1103:Farrow SC, Facchini PJ (October 2014).
607:
2354:Journal of Cardiovascular Pharmacology
2305:Journal of Cardiovascular Pharmacology
374:10.1111/j.1432-1033.1997.t01-1-00625.x
241:Simplified view of the active site of
62:demethylation), as well as sensors of
7:
70:the exact roles are not understood.
2068:, Hajdu J, Baldwin JE (June 1997).
1340:The Journal of Biological Chemistry
958:Kershaw NJ, Caines ME, Sleeman MC,
355:Hegg EL, Que L Jr (December 1997).
308:The Journal of Biological Chemistry
2367:10.1097/01.fjc.0000250077.07702.23
2318:10.1097/01.fjc.0000211732.76668.d2
410:10.1111/j.1432-1033.1977.tb11889.x
14:
218:Substrate and cosubstrate binding
2848:, Matthews SJ (September 2008).
2400:European Journal of Pharmacology
1530:Flashman E, Davies SL, Yeoh KK,
3285:10.1016/j.jinorgbio.2012.03.002
2715:, Claridge TD (February 2017).
2672:Leung IK, Flashman E, Yeoh KK,
2598:10.1016/j.jinorgbio.2017.08.032
2541:Journal of Biological Chemistry
2043:10.1016/j.advenzreg.2003.11.017
1780:10.1016/j.jinorgbio.2006.01.024
1058:Journal of Biological Chemistry
273:gamma-butyrobetaine dioxygenase
2623:, Claridge TD (January 2013).
1308:10.1016/j.chembiol.2010.09.016
1228:10.1016/j.chembiol.2004.08.012
1:
2492:Molecular Biology of the Cell
2412:10.1016/S0014-2999(00)00098-4
1594:10.1016/j.febslet.2005.08.033
1508:10.1016/S0021-9258(18)91023-9
1264:10.1016/S0945-053X(03)00006-4
1205:Zhang Z, Ren JS, Clifton IJ,
676:Crit. Rev. Biochem. Mol. Biol
2215:, Kawamura A (August 2013).
1862:Proc. Natl. Acad. Sci. U.S.A
1639:Proc. Natl. Acad. Sci. U.S.A
852:Proc. Natl. Acad. Sci. U.S.A
723:Proc. Natl. Acad. Sci. U.S.A
243:prolyl hydroxylase isoform 2
228:prolyl hydroxylase isoform 2
265:prolyl hydroxylase domain 2
3442:
2278:10.1016/j.bmcl.2011.05.050
1411:10.1016/j.cbpa.2012.09.015
1393:Walport LJ, Hopkinson RJ,
821:10.1016/j.tibs.2010.07.002
249:, are omitted for clarity.
3079:10.1007/s00775-016-1406-3
1942:10.1016/j.str.2009.06.002
1741:10.1016/j.sbi.2010.08.006
1450:10.1007/s00018-015-1978-z
1332:Schofield, Christopher J.
688:10.1080/10409230490440541
3160:10.1016/j.ab.2006.03.033
3124:10.1016/j.ab.2004.09.019
1729:Curr. Opin. Struct. Biol
232:isopenicillin N synthase
163:oxygen rebound mechanism
2504:10.1091/mbc.E02-12-0791
2266:Bioorg. Med. Chem. Lett
1883:10.1073/pnas.0601283103
1652:10.1073/pnas.0911565107
1353:10.1074/jbc.R115.662627
1122:10.3389/fpls.2014.00524
1071:10.1074/jbc.M114.575647
1020:10.1073/pnas.0812938106
873:10.1073/pnas.1409916111
736:10.1073/pnas.0336792100
645:10.1038/nchembio0207-86
321:10.1074/jbc.R115.648691
191:double-stranded β-helix
159:Fe(IV)-oxo intermediate
3196:10.1002/cbic.201200256
2996:10.1002/cmdc.200700233
2961:10.1002/anie.201202000
2916:10.1074/jbc.M707411200
2866:10.1038/embor.2008.120
2776:10.1002/cbic.200900713
2554:10.1074/jbc.M607065200
2447:10.1002/cbic.202100181
1820:10.1074/jbc.M706358200
1399:Curr. Opin. Chem. Biol
928:10.1074/jbc.M213054200
593:10.1002/ejic.201200391
551:10.1098/rsta.2004.1540
531:Phil. Trans. R. Soc. A
435:Nat. Struct. Mol. Biol
283:
250:
176:
21:non-heme iron proteins
1603:10536/DRO/DU:30019701
281:
240:
174:
19:are a major class of
3426:Human 2OG oxygenases
3067:J. Biol. Inorg. Chem
2949:Angew. Chem. Int. Ed
1173:10.3390/ijms15011080
212:cysteine dioxygenase
28:enzymes. Both use O
3246:10.1042/BCJ20160146
2817:(46): 16654–16655.
2031:Advan. Enzyme Regul
1998:10.1038/ncomms12673
1990:2016NatCo...712673C
1874:2006PNAS..103.9814M
1346:(34): 20712–20722.
1064:(43): 29584–29601.
1011:2009PNAS..10614315Y
1005:(34): 14315–14320.
921:(23): 20843–20850.
864:2014PNAS..11113331S
858:(37): 13331–13336.
809:Trends Biochem. Sci
580:Eur. J. Inorg. Chem
543:2005RSPTA.363..807H
314:(34): 20702–20711.
74:Catalytic mechanism
36:Biological function
3383:10.1042/BJ20061151
2734:10.1039/C6MD00004E
2233:10.1039/C3SC51122G
2179:10.1039/C7SC02103H
2161:(September 2017).
2135:10.1039/c0cs00203h
1555:10.1042/BJ20091609
846:(September 2014).
284:
251:
177:
3334:10.1042/bj2400617
3273:J. Inorg. Biochem
3190:(11): 1559–1563.
3040:10.1021/jm900285r
2955:(27): 6672–6675.
2823:10.1021/ja907933p
2721:Med. Chem. Commun
2690:10.1021/jm901537q
2641:10.1021/jm301583m
2586:J. Inorg. Biochem
2441:(15): 2521–2525.
2272:(14): 4325–4328.
2173:(11): 7651–7668.
2080:(6635): 827–830.
1868:(26): 9814–9819.
1768:J. Inorg. Biochem
1702:10.1021/bi500086p
1696:(15): 2483–2493.
1588:(23): 5170–5174.
1438:Cell Mol Life Sci
1301:(12): 1316–1324.
1289:(December 2010).
1221:(10): 1383–1394.
966:(34): 4251–4263.
626:(February 2007).
586:(31): 4973–4985.
537:(1829): 807–828.
514:10.1021/ja039113j
485:10.1021/bi030011f
479:(24): 7497–7508.
64:energy metabolism
3433:
3405:
3404:
3394:
3362:
3356:
3355:
3345:
3313:
3307:
3306:
3296:
3264:
3258:
3257:
3240:(9): 1179–1189.
3231:
3222:
3216:
3215:
3178:
3172:
3171:
3142:
3136:
3135:
3107:
3101:
3100:
3090:
3073:(2–3): 367–379.
3058:
3052:
3051:
3034:(9): 2799–2805.
3022:
3016:
3015:
2979:
2973:
2972:
2943:
2937:
2936:
2918:
2909:(7): 3808–3815.
2894:
2888:
2887:
2877:
2841:
2835:
2834:
2811:J. Am. Chem. Soc
2802:
2796:
2795:
2755:
2749:
2748:
2746:
2736:
2708:
2702:
2701:
2669:
2663:
2662:
2652:
2616:
2610:
2609:
2581:
2575:
2574:
2556:
2547:(3): 1788–1796.
2532:
2526:
2525:
2515:
2498:(8): 3470–3481.
2483:
2477:
2476:
2458:
2430:
2424:
2423:
2394:
2388:
2387:
2369:
2345:
2339:
2338:
2320:
2296:
2290:
2289:
2261:
2255:
2254:
2244:
2227:(8): 3110–3117.
2207:
2201:
2200:
2190:
2153:
2147:
2146:
2129:(8): 4364–4397.
2114:
2108:
2107:
2089:
2061:
2055:
2054:
2026:
2020:
2019:
2009:
1961:
1955:
1954:
1944:
1912:
1906:
1905:
1895:
1885:
1849:
1843:
1842:
1832:
1822:
1798:
1792:
1791:
1759:
1753:
1752:
1720:
1714:
1713:
1681:
1675:
1674:
1664:
1654:
1645:(9): 3982–3987.
1630:
1624:
1623:
1605:
1573:
1567:
1566:
1540:
1527:
1521:
1520:
1510:
1501:(9): 5403–5405.
1486:
1480:
1479:
1461:
1444:(20): 3897–914.
1429:
1423:
1422:
1405:(5–6): 525–534.
1390:
1384:
1383:
1373:
1355:
1327:
1321:
1320:
1310:
1282:
1276:
1275:
1247:
1241:
1240:
1230:
1209:(October 2004).
1202:
1196:
1195:
1185:
1175:
1166:(1): 1080–1095.
1160:Int. J. Mol. Sci
1151:
1145:
1144:
1134:
1124:
1109:Front. Plant Sci
1100:
1094:
1093:
1083:
1073:
1049:
1043:
1042:
1032:
1022:
990:
984:
983:
972:10.1039/b505964j
955:
949:
948:
930:
902:
896:
895:
885:
875:
839:
833:
832:
800:
794:
793:
782:10.1039/A902197C
765:
759:
758:
748:
738:
729:(7): 3589–3594.
714:
708:
707:
671:
658:
657:
647:
619:
597:
595:
570:
525:
508:(4): 1022–1023.
502:J. Am. Chem. Soc
496:
466:
432:
422:
412:
386:
376:
351:
341:
323:
136:
128:
104:
3441:
3440:
3436:
3435:
3434:
3432:
3431:
3430:
3411:
3410:
3409:
3408:
3364:
3363:
3359:
3315:
3314:
3310:
3266:
3265:
3261:
3229:
3224:
3223:
3219:
3180:
3179:
3175:
3144:
3143:
3139:
3109:
3108:
3104:
3060:
3059:
3055:
3024:
3023:
3019:
2981:
2980:
2976:
2945:
2944:
2940:
2896:
2895:
2891:
2843:
2842:
2838:
2804:
2803:
2799:
2757:
2756:
2752:
2710:
2709:
2705:
2671:
2670:
2666:
2618:
2617:
2613:
2583:
2582:
2578:
2534:
2533:
2529:
2485:
2484:
2480:
2432:
2431:
2427:
2396:
2395:
2391:
2347:
2346:
2342:
2298:
2297:
2293:
2263:
2262:
2258:
2209:
2208:
2204:
2155:
2154:
2150:
2116:
2115:
2111:
2063:
2062:
2058:
2028:
2027:
2023:
1972:(August 2016).
1963:
1962:
1958:
1914:
1913:
1909:
1851:
1850:
1846:
1813:(2): 36552–60.
1800:
1799:
1795:
1761:
1760:
1756:
1722:
1721:
1717:
1683:
1682:
1678:
1632:
1631:
1627:
1575:
1574:
1570:
1538:
1529:
1528:
1524:
1488:
1487:
1483:
1431:
1430:
1426:
1392:
1391:
1387:
1329:
1328:
1324:
1284:
1283:
1279:
1249:
1248:
1244:
1204:
1203:
1199:
1153:
1152:
1148:
1102:
1101:
1097:
1051:
1050:
1046:
992:
991:
987:
957:
956:
952:
904:
903:
899:
841:
840:
836:
802:
801:
797:
767:
766:
762:
716:
715:
711:
673:
672:
661:
632:Nat. Chem. Biol
621:
620:
609:
604:
573:
528:
499:
469:
447:10.1038/nsmb712
430:
425:
397:Eur. J. Biochem
390:
361:Eur. J. Biochem
354:
301:
298:
296:Further reading
289:
261:N-oxalylglycine
256:
248:
220:
209:
205:
199:
197:Metallocofactor
187:
182:
157:and forming an
156:
148:
144:
140:
134:
132:
126:
124:
120:
116:
112:
108:
103:
99:
97:
89:
81:
76:
38:
31:
26:cytochrome P450
12:
11:
5:
3439:
3437:
3429:
3428:
3423:
3413:
3412:
3407:
3406:
3377:(1): 227–234.
3357:
3328:(2): 617–619.
3308:
3259:
3217:
3173:
3137:
3118:(1): 125–131.
3102:
3053:
3017:
2990:(4): 569–572.
2974:
2938:
2889:
2860:(9): 872–877.
2836:
2797:
2770:(4): 506–510.
2750:
2727:(5): 873–880.
2703:
2684:(2): 867–875.
2664:
2635:(2): 547–555.
2611:
2576:
2527:
2478:
2425:
2389:
2340:
2291:
2256:
2202:
2148:
2123:Chem. Soc. Rev
2109:
2056:
2021:
1956:
1935:(7): 981–989.
1907:
1844:
1793:
1774:(4): 644–669.
1754:
1735:(6): 659–672.
1715:
1676:
1625:
1568:
1549:(1): 135–142.
1534:(March 2010).
1522:
1481:
1424:
1385:
1334:(2015-08-21).
1322:
1277:
1242:
1197:
1146:
1095:
1044:
985:
950:
897:
834:
795:
776:(4): 367–383.
770:Nat. Prod. Rep
760:
709:
659:
606:
605:
603:
600:
599:
598:
571:
526:
497:
467:
423:
403:(2): 349–357.
388:
367:(3): 625–629.
352:
297:
294:
288:
285:
255:
252:
246:
219:
216:
207:
203:
198:
195:
186:
183:
181:
178:
154:
150:
149:
146:
142:
138:
130:
122:
118:
114:
110:
106:
101:
95:
87:
79:
75:
72:
37:
34:
29:
13:
10:
9:
6:
4:
3:
2:
3438:
3427:
3424:
3422:
3419:
3418:
3416:
3402:
3398:
3393:
3388:
3384:
3380:
3376:
3372:
3368:
3361:
3358:
3353:
3349:
3344:
3339:
3335:
3331:
3327:
3323:
3319:
3312:
3309:
3304:
3300:
3295:
3290:
3286:
3282:
3278:
3274:
3270:
3263:
3260:
3255:
3251:
3247:
3243:
3239:
3235:
3228:
3221:
3218:
3213:
3209:
3205:
3201:
3197:
3193:
3189:
3185:
3177:
3174:
3169:
3165:
3161:
3157:
3153:
3149:
3148:Anal. Biochem
3141:
3138:
3133:
3129:
3125:
3121:
3117:
3113:
3112:Anal. Biochem
3106:
3103:
3098:
3094:
3089:
3084:
3080:
3076:
3072:
3068:
3064:
3057:
3054:
3049:
3045:
3041:
3037:
3033:
3029:
3021:
3018:
3013:
3009:
3005:
3001:
2997:
2993:
2989:
2985:
2978:
2975:
2970:
2966:
2962:
2958:
2954:
2950:
2942:
2939:
2934:
2930:
2926:
2922:
2917:
2912:
2908:
2904:
2903:J. Biol. Chem
2900:
2893:
2890:
2885:
2881:
2876:
2871:
2867:
2863:
2859:
2855:
2851:
2847:
2840:
2837:
2832:
2828:
2824:
2820:
2816:
2812:
2808:
2801:
2798:
2793:
2789:
2785:
2781:
2777:
2773:
2769:
2765:
2761:
2754:
2751:
2745:
2740:
2735:
2730:
2726:
2722:
2718:
2714:
2707:
2704:
2699:
2695:
2691:
2687:
2683:
2679:
2675:
2668:
2665:
2660:
2656:
2651:
2646:
2642:
2638:
2634:
2630:
2626:
2622:
2615:
2612:
2607:
2603:
2599:
2595:
2591:
2587:
2580:
2577:
2572:
2568:
2564:
2560:
2555:
2550:
2546:
2542:
2538:
2531:
2528:
2523:
2519:
2514:
2509:
2505:
2501:
2497:
2493:
2489:
2482:
2479:
2474:
2470:
2466:
2462:
2457:
2452:
2448:
2444:
2440:
2436:
2429:
2426:
2421:
2417:
2413:
2409:
2406:(3): 217–24.
2405:
2401:
2393:
2390:
2385:
2381:
2377:
2373:
2368:
2363:
2359:
2355:
2351:
2344:
2341:
2336:
2332:
2328:
2324:
2319:
2314:
2310:
2306:
2302:
2295:
2292:
2287:
2283:
2279:
2275:
2271:
2267:
2260:
2257:
2252:
2248:
2243:
2238:
2234:
2230:
2226:
2222:
2218:
2214:
2206:
2203:
2198:
2194:
2189:
2184:
2180:
2176:
2172:
2168:
2164:
2160:
2152:
2149:
2144:
2140:
2136:
2132:
2128:
2124:
2120:
2113:
2110:
2105:
2101:
2097:
2093:
2088:
2087:10.1038/42990
2083:
2079:
2075:
2071:
2067:
2060:
2057:
2052:
2048:
2044:
2040:
2036:
2032:
2025:
2022:
2017:
2013:
2008:
2003:
1999:
1995:
1991:
1987:
1983:
1979:
1975:
1971:
1967:
1960:
1957:
1952:
1948:
1943:
1938:
1934:
1930:
1926:
1923:(July 2009).
1922:
1918:
1911:
1908:
1903:
1899:
1894:
1889:
1884:
1879:
1875:
1871:
1867:
1863:
1859:
1856:(June 2006).
1855:
1848:
1845:
1840:
1836:
1831:
1826:
1821:
1816:
1812:
1808:
1807:J. Biol. Chem
1804:
1797:
1794:
1789:
1785:
1781:
1777:
1773:
1769:
1765:
1758:
1755:
1750:
1746:
1742:
1738:
1734:
1730:
1726:
1719:
1716:
1711:
1707:
1703:
1699:
1695:
1691:
1687:
1680:
1677:
1672:
1668:
1663:
1658:
1653:
1648:
1644:
1640:
1636:
1629:
1626:
1621:
1617:
1613:
1609:
1604:
1599:
1595:
1591:
1587:
1583:
1579:
1572:
1569:
1564:
1560:
1556:
1552:
1548:
1544:
1537:
1533:
1526:
1523:
1518:
1514:
1509:
1504:
1500:
1496:
1495:J. Biol. Chem
1492:
1485:
1482:
1477:
1473:
1469:
1465:
1460:
1455:
1451:
1447:
1443:
1439:
1435:
1428:
1425:
1420:
1416:
1412:
1408:
1404:
1400:
1396:
1389:
1386:
1381:
1377:
1372:
1367:
1363:
1359:
1354:
1349:
1345:
1341:
1337:
1333:
1326:
1323:
1318:
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