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  • enzyme
  • Tyrosinemia, Type III (TYR-III) is an inborn error of metabolism, an inherited condition in which an enzyme, 4-hydroxyphenylpyruvate dioxygenase, in the body is either missing or not working well. (mn.us)
  • 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)
  • Gamma-butyrobetaine dioxygenase belongs to the 2-oxoglutarate (2OG)-dependent dioxygenase superfamily. (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)
  • 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)
  • This enzyme catalyses the following chemical reaction 2-hydroxyethylphosphonate + O2 ⇌ {\displaystyle \rightleftharpoons } hydroxymethylphosphonate + formate 2-hydroxyethylphosphonate dioxygenase contains non-heme-Fe(II). (wikipedia.org)
  • oxidation
  • The dioxygenases (EC 1.13.11) catalyze the oxidation of a substrate without the reduction of one oxygen atom from dioxygen into a water molecule. (wikipedia.org)
  • Gamma-butyrobetaine dioxygenase also catalyses the oxidation of mildronate to form multiple products including malonic acid semialdehyde, dimethylamine, formaldehyde and (1-methylimidazolidin-4-yl)acetic acid, which is proposed to be formed via a Stevens rearrangement mechanism. (wikipedia.org)
  • Aerobic
  • In nearly all aerobic beings, 4- Hydroxyphenylpyruvate dioxygenase is responsible for converting 4- Hydroxyphenylpyruvate into homogentisate. (wikipedia.org)
  • catalytic
  • The mononuclear iron dioxygenases, or non-heme iron-dependent dioxygenases as they are also termed, all utilize a single catalytic iron to incorporate either one or both atoms of dioxygen into a substrate. (wikipedia.org)
  • The catalytic activity of gamma-butyrobetaine dioxygenase can be stimulated with different metal ions, especially potassium ions. (wikipedia.org)
  • Both the apo (PDB id: 3N6W) and the holo (PDB id: 3O2G) structures of gamma-butyrobetaine dioxygenase have been solved, demonstrating an induced fit mechanism may contribute to the catalytic activity of gamma-butyrobetaine dioxygenase. (wikipedia.org)
  • Gamma-butyrobetaine dioxygenase is promiscus in substrate selectivity and it processes a number of modified substrates, including the natural catalytic products L-carnitine and D-carnitine, forming 3-dehydrocarnitine and trimethylaminoacetone. (wikipedia.org)
  • mechanism
  • 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)
  • Other reported gamma-butyrobetaine dioxygenase inhibitors include cyclopropyl-substituted gamma-butyrobetaines and 3-(2,2-dimethylcyclopropyl)propanoic acid, which is a mechanism-based enzyme inhibitor. (wikipedia.org)
  • ascorbate
  • Similar to many other 2OG oxygenases, the activity of gamma-butyrobetaine dioxygenase can be stimulated by reducing agents such as ascorbate and glutathione. (wikipedia.org)
  • suggests
  • A crystal structure of mldronate in complex with gamma-butyrobetaine dioxygenase was published, and it suggests mildronate bind to gamma-butyrobetaine dioxygenase in exactly the same way as gamma-butyrobetaine (PDB id: 3MS5). (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)
  • Gamma-butyrobetaine dioxygenase is an inhibition target for 3-(2,2,2-trimethylhydraziniumyl)propionate (mildronate, also known as THP, MET-88, Meldonium or Quarterine). (wikipedia.org)
  • iron
  • 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)
  • In the 2OG-dependent dioxygenases, ferrous iron (Fe(II)) is also coordinated by a (His)2(Glu/Asp)1 "facial triad" motif. (wikipedia.org)
  • Iron is a cofactor for gamma-butyrobetaine dioxygenase. (wikipedia.org)
  • formation
  • Gamma-butyrobetaine dioxygenase catalyses the formation of L-carnitine from gamma-butyrobetaine, the last step in the L-carnitine biosynthesis pathway. (wikipedia.org)