2-Oxoglutarate dioxygenase

This enzyme [EC 1.14.11.3], also known as thymidine 2-oxoglutarate dioxygenase, catalyzes the reaction of 2-deoxyuridine with a-ketoglutarate (or, 2-oxoglutarate) and dioxygen to produce uridine, succinate, and carbon dioxide. The enzyme, which also can act on thymidine, requires iron ions and ascorbate. 

The storage role of (Cu,Zn)-SOD in seeds e.g. seems plausible, when the Cu-carrier function of ceruloplasmin is considered The lipophilic anti-inflammatory and anti-ulcer Cu-chelates could also raise the Cu concentration in certain tissues and thus enhance their lysyl oxidase activity. But especially Cu(acetylsalicylate)2 inhibited protine,2-oxoglutarate dioxygenase (EC 1.14.11.2) and lysine,2-oxoglutarate dioxygenase (EC 1.14.1.4), which are also important enzymes in the processing of collagen... 

Thymidine, 2 oxoglutarate dioxygenase 1.14.11.3 (Pyrimidine deoxyribonucleoside 2 -hydroxylase... 

High-valent iron intermediates have been proposed as the active species in OAT and C-H oxidation reactions for nonheme iron enzymes. In some cases, such intermediates have been trapped by rapid fireeze-quench studies and characterized. In ribonucleotide reductase from E. coli and MMO, intermediates X and Q with Fem-( l-0)2-Ferv and Ferv-( 0,-O)2-FeIV diamond core, respectively, have been characterized (Figure 3.11).35 Also, Fe,v oxo intermediates have been observed for mononuclear proteins such as taurine/2-oxoglutarate dioxygenase (TauD) (Figure 3.11).36... 

Structure and Mechanism of 2-Oxoglutarate Dioxygenase Histone Demethylases... 

Biosynthesis of carnitine. v-Butyrobetaine, 2-oxoglutarate dioxygenase (EC 1.14.11.1) occurs in liver, kidney and brain, whereas the other enzymes occur in most tissues. The aldolase cleaving 3-hydroxy-NMrimethyl-L-lysine may be identical with glycine hydroxymethyltransferase (EC 2.1.2.1). (W. A. Dunn etal. J. Biol. Chem. 259(1984) 10764-107701... 

Trimethylaminobutyrate, 2-oxoglutarale oxygen oxi-doreductase (3-hydroxylaling), or y-Butyrobetaine, 2-oxoglutarate dioxygenase (EC 1.14.11.1). It catalyses the hydroxylation of 4-trimethylaminobutyrate to l-3-hydroxy-4-Ai-trimethylaminobutyrate, or Carnitine (see). 

Thymidine, 2-oxoglutarate oxygen oxidoreductase (2 -hydroxylating), or Thymidine, 2-oxoglutarate dioxygenase, or Thymidine 2 -hydroxylase, or Pyrimidine deoxyribonucleoside 2 -hydroxylase (EC 1.14.11.3). It catalyses hydroxylation of C2 of the deoxyribose moiety of thymidine. 

Proline, 2-Oxoglutarate Dioxygenases.—Part of the enzymic activity was lost when the proline, 2-oxoglutarate dioxygenase from chicken embryos interacted with [ H-acetyl]concanavalin A, suggesting that the enzyme contains a carbohydrate component. ... 

Fig. 2. Active site of taurine dioxygenase (TauD) with 2-oxoglutarate bound to Fe(II) and a taurine substrate (PDB-Code 1GY9) (31).

Prolyl 4-hydroxylation is the most abundant posttranslational modification of collagens. 4-Hydroxylation of proline residues increases the stability of the triple helix and is a key element in the folding of the collagen triple helix. " In vertebrates, almost all the Yaa position prolines of the Gly-Xaa-Yaa repeat are modified to 4(I( )-hydroxylproline by the enzyme P4H (EC 1.14.11.2), a member of Fe(II)- and 2-oxoglutarate-dependent dioxygenases. This enzyme is an 0 2/ b2-type heterotetramer in which the / subunit is PDI (EC 5.3.4.1), which is a ubiquitous disulfide bond catalyst. The P4H a subunit needs the 13 subunit for solubility however, the 13 subunit, PDI, is soluble by itself and is present in excess in the ER. Three isoforms of the a subunit have been identified and shown to combine with PDI to form [a(I)]2/ 2) [< (II)]2/32> or [a(III)]2/32 tetramers, called the type... 

Fig. 6.2 The flavonoid core biosynthetic pathway. The P450s and 2-oxoglutarate-dependent dioxygenases (2-ODDs) are indicated by underlined and bolded titles, respectively. F3 H and F3 5 H are capable of using flavanones (2-3 = single bond, R1 = H), flavones (2-3 = double bond, R1 = H), dihydroflavonols (2-3 = single bond, R1 = OH), or flavonols (2-3 = double bond, R1 = OH) for a substrate. FNS activity has been indicated with two different enzymes, FNS-11 (P450) and the less-common FNS-I (2-ODD)...

Flavone synthase (FNS EC 1.14.11.22) introduces a double bond between C2 and C3 of a flavanone to produce the corresponding flavone. This activity was initially identified in parsley cell suspension cultures and subsequently shown to be encoded by a 2-oxoglutarate-dependent dioxygenase [67, 78, 79], This enzyme, now known as FNS-I, appears to have very limited distribution. To date, it has only been identified in the Apiaceae family (Umbellifers). The more widely occurring FNS-II (CYP93B) was initially identified from snapdragon (Antirrhinum majus) flowers [80] and was subsequently shown to be a P450 enzyme. FNS-I, FNS-II, and the various roles flavones play in plant species have recently been reviewed by Martens and Mithofer [81], Subsequent to this review, Yu et al. [82] demonstrated that the characteristic lack of natural accumulation of flavones in Brassicaceae could not be overcome in A. thaliana even by overexpression of recombinant parsley FNS-I. 

Flavonol synthase (FLS E.C.l.14.11.23) catalyzes the committed step in the production of fiavonols by introduction of a double bond between C2 and C3 of the corresponding dihydroflavonols. Like E3H, ELS has been described as a 2-oxoglutatarate-dependent dioxygenase based on its cofactor requirements for 2-oxoglutarate, Fe, and ascorbate. FLS was initially identified in enzyme preparations from illuminated parsley cell suspension cultures [67]. Subsequently, FLS was characterized from the flower buds of Matthiola incana and carnation (Dianthus caryophyllus L.), and it was suggested that there was regulation between flavonol and anthocyanidin biosynthesis [83, 84]. 

Halbwirth H, Fischer TC, Schlangen K, Rademacher W, Schleifer K, Forkmann G, Stitch K (2006) Screening for inhibitors of 2-oxoglutarate-dependent dioxygenases flavanone 3-hydroxylase and flavonol synthase. Plant Sd 171 194-205... 

Martens S, Forkmann G, Britsch L, WeUmann F, Matem U, Lukacin R (2003) Divergent evolution of flavonoid 2-oxoglutarate-dependent dioxygenases in parsley. FEBS Lett 544 (l-3) 93-98... 

This enzyme [EC 1.14.11.13], also known as gibberellin 2)3-dioxygenase, catalyzes the following reaction gibber-ellin-1 -F 2-oxoglutarate + 02 = 2-/3-hydroxygibberellin-1 + succinate + CO2. The enzyme acts on other gibberel-lins as well. 

Matsuda, J. et al.. Molecular cloning of hyoscyamine 6p-hydroxylase, a 2-oxoglutarate-dependent dioxygenase, from cultured roots of Hyoscyamus niger. J. Biol Chem., 266, 9460, 1991. 

Anzelotti, D. and Ibrahim, R.K., Novel flavonol 2-oxoglutarate dependent dioxygenase affinity purification, characterization, and kinetic properties. Arch. Biochem. Biophys., 382, 161, 2000. 

Roemmelt, S. et al., Formation of novel flavonoids in apple (Malus x domesticd) treated with the 2-oxoglutarate-dependent dioxygenase inhibitor prohexadione-Ca, Phytochemistry, 64, 709, 2003. 

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