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  • produce
  • Every person carries in their DNA two copies (one received from each parent) of the gene HGD, which contains the genetic information to produce the enzyme homogentisate 1,2-dioxygenase (HGD) which can normally be found in numerous tissues in the body (liver, kidney, small intestine, colon and prostate). (wikipedia.org)
  • enzymology
  • In enzymology, a cysteamine dioxygenase (EC 1.13.11.19) is an enzyme that catalyzes the chemical reaction 2-aminoethanethiol + O2 ⇌ {\displaystyle \rightleftharpoons } hypotaurine Thus, the two substrates of this enzyme are 2-aminoethanethiol and O2, whereas its product is hypotaurine. (wikipedia.org)
  • In enzymology, a thymine dioxygenase (EC 1.14.11.6) is an enzyme that catalyzes the chemical reaction thymine + 2-oxoglutarate + O2 ⇌ {\displaystyle \rightleftharpoons } 5-hydroxymethyluracil + succinate + CO2 The 3 substrates of this enzyme are thymine, 2-oxoglutarate, and O2, whereas its 3 products are 5-hydroxymethyluracil, succinate, and CO2. (wikipedia.org)
  • superfamily
  • Members of the hemoglobin superfamily efficiently catalyze nitric-oxide dioxygenation, and when paired with native electron donors, function as NO dioxygenases (NODs). (hindawi.com)
  • Most mononculear iron dioxygenases are members of the cupin superfamily in which the overall domain structure is described as a six-stranded β-barrel fold (or jelly roll motif). (wikipedia.org)
  • EC 1.14.11.8) is an enzyme that catalyzes the chemical reaction N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 ⇌ {\displaystyle \rightleftharpoons } 3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2 TMLH is a member of the 2-oxoglutarate (2OG)-dependent dioxygenase superfamily. (wikipedia.org)
  • In addition to numerous flavohemoglobins, many distantly related members of the hemoglobin superfamily including the muscle myoglobin, the non-symbiotic plant hemoglobin and symbiotic plant leghemoglobin, the neuronal neuroglobin, and the mammalian cytoplasmic cytoglobin appear to function as nitric oxide dioxygenases (NODs), although the cellular electron donor(s) for many globins have yet to be defined. (wikipedia.org)
  • Nitric-Oxide Dioxy
  • The net reaction for the reaction catalyzed by nitric oxide dioxygenase is shown below: 2NO + 2O2 + NAD(P)H → 2NO3− + NAD(P)+ + H+ Nitric oxide is a ubiquitous small molecule that is integrated in a wide variety of physiological processes including smooth muscle vasodilation, platelet disaggregation, neurotransmission, and immune response to bacterial infection. (wikipedia.org)
  • A 'nitric oxide dioxygenase' is an enzyme that is capable of carrying out this reaction. (wikipedia.org)
  • Additionally, flavoHbs have been shown to protect bacteria, yeast, and Dictyostelium discoideum against growth inhibition and damage mediated via NO. Nitric oxide dioxygenase was discovered, and first reported in 1998, as an inducible O2-dependent enzymatic activity that protected bacteria against nitric oxide toxicity. (wikipedia.org)
  • Historically, nitric oxide dioxygenase (around 1.8 billion years ago) served to provide the modern day analogue of hemoglobin/myoglobin function for oxygen storage and transport. (wikipedia.org)
  • Protein
  • In benzoate and toluate 1,2-dioxygenase systems, a single protein containing reductase and Rieske-type ferredoxin domains transfers the electrons from NADH to the hydroxylase component. (wikipedia.org)
  • Membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein-1 (MTCBP-1) acts as an eukaryotic aci-reductone dioxygenase (ARD) in the methionine salvage pathway. (ebi.ac.uk)
  • In mammals and humans, 2OG-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. histone and DNA demethylation), as well as sensors of energy metabolism. (wikipedia.org)
  • For example, significant protein structural changes have been observed upon substrate binding for human prolyl hydroxylase isoform 2 (PHD2), a 2OG-dependent dioxygenase that is involved in oxygen sensing, and isopenicillin N synthase (IPNS), a microbial 2OG-dependent dioxygenase. (wikipedia.org)
  • More recently, another protein has been identified as a NO dioxygenase - rhodobacter sphaeroides haem protein (SHP), a novel cytochrome with NO dioxygenase activity. (wikipedia.org)
  • mononuclear
  • Iron-containing dioxygenases can be subdivided into three classes on the basis of how iron is incorporated into the active site: those employing a mononuclear iron center, those containing a Rieske [2Fe-2S] cluster, and those utilizing a heme prosthetic group. (wikipedia.org)
  • Despite this common oxygenation event, the mononuclear iron dioxygenases are diverse in how dioxygen activation is used to promote certain chemical reactions. (wikipedia.org)
  • reaction
  • This enzyme catalyses the following chemical reaction gallate + O2 ⇌ {\displaystyle \rightleftharpoons } (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate Gallate dioxygenase contains non-heme Fe2+. (wikipedia.org)
  • 4-Hydroxyphenylpyruvate dioxygenase (HPPD), also known as α-ketoisocaproate dioxygenase (KIC dioxygenase), is an Fe(II)-containing non-heme oxygenase that catalyzes the second reaction in the catabolism of tyrosine - the conversion of 4-hydroxyphenylpyruvate into homogentisate. (wikipedia.org)
  • This enzyme catalyses the following chemical reaction 2-hydroxyethylphosphonate + O2 ⇌ {\displaystyle \rightleftharpoons } hydroxymethylphosphonate + formate 2-hydroxyethylphosphonate dioxygenase contains non-heme-Fe(II). (wikipedia.org)
  • cupin
  • All 2OG-dependent dioxygenases contain a conserved double-stranded β-helix (DSBH, also known as cupin) fold, which is formed with two β-sheets. (wikipedia.org)
  • hydroxylase
  • Inhibitors that compete against the substrate were also developed, such as peptidyl-based inhibitors that target human prolyl hydroxylase domain 2 (PHD2) and Mildronate, a drug molecule that is commonly used in Russia and Eastern Europe that target gamma-butyrobetaine dioxygenase. (wikipedia.org)
  • Other names in common use include thymine 7-hydroxylase, 5-hydroxy-methyluracil dioxygenase, and 5-hydroxymethyluracil oxygenase. (wikipedia.org)
  • Aerobic
  • In nearly all aerobic beings, 4- Hydroxyphenylpyruvate dioxygenase is responsible for converting 4- Hydroxyphenylpyruvate into homogentisate. (wikipedia.org)
  • mechanism
  • Based on evidence from X-ray crystallography, molecular dynamics calculation and NMR spectroscopy, some 2OG-dependent dioxygenases bind their substrate through an induced fit mechanism. (wikipedia.org)
  • The mechanism of action has still not been entirely deduced, however, the leading theory suggests that the conversion is carried out through a series of redox reactions involving iron centers as shown in the series of half reactions below: Another theory developed more recently (2009) suggests that a NO dioxygenase activity could also proceed through phenolic nitration via a putative heme-peroxynitrite intermediate. (wikipedia.org)
  • known
  • 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (also known as MTCBP-1) ( EC:1.13.11.54 ) is an eukaryotic enzyme that catalyses the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). (ebi.ac.uk)
  • include
  • The inhibitors that were regularly used to target 2OG-dependent dioxygenase include N-oxalylglycine (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 2OG and compete against the binding of 2OG at the enzyme active site Fe(II). (wikipedia.org)