| http://dbpedia.org/ontology/abstract
|
A D-aminoácido desidrogenase (EC 1.4.99.1) … A D-aminoácido desidrogenase (EC 1.4.99.1) é uma enzima bacteriana que catalisa a oxidação de D-aminoácidos nos correspondentes oxiácidos. Contém flavina e ferro não-hemo como cofactores. A enzima possui uma larga especificidade e pode agir na maioria dos D-aminoácidos. D-aminoácido + H2O + aceitador ⇐> a 2-oxiácido + NH3 + aceitador reduzido Esta reacção é distinta da reacção de oxidação catalisada pela que utiliza o oxigénio como substrato secundário. A desidrogenase pode utilizar muitos compostos diferentes como aceitadore sde electrões, com o substrato fisiológico sendo a coenzima Q. substrato fisiológico sendo a coenzima Q.
, D-アルギニンデヒドロゲナーゼ(D-arginine dehydrogenase)ま … D-アルギニンデヒドロゲナーゼ(D-arginine dehydrogenase)またはD-アミノ酸デヒドロゲナーゼ(D-amino-acid dehydrogenase)は、D-アミノ酸をそれぞれ対応するケト酸に酸化するバクテリア酵素である。補因子としてフラビンと非ヘム鉄を含む。この酵素は広範囲の特異性を持ち、ほとんどのD-アミノ酸に作用する。 D-アミノ酸 + H2O + 受容体 2-オキソ酸 + NH3 + 還元型受容体 この反応は、第二基質に酸素を用いるD-アミノ酸オキシダーゼによる酵素反応とは異なり、このデヒドロゲナーゼはいくつかの電子受容体を用いることが可能で、補酵素Qのような生理学的基質を用いる。ゼはいくつかの電子受容体を用いることが可能で、補酵素Qのような生理学的基質を用いる。
, D-amino-acid dehydrogenase (EC 1.4.99.1) i … D-amino-acid dehydrogenase (EC 1.4.99.1) is a bacterial enzyme that catalyses the oxidation of D-amino acids into their corresponding oxoacids. It contains both flavin and nonheme iron as cofactors. The enzyme has a very broad specificity and can act on most D-amino acids. D-amino acid + H2O + acceptor <=> a 2-oxo acid + NH3 + reduced acceptor This reaction is distinct from the oxidation reaction catalysed by D-amino acid oxidase that uses oxygen as a second substrate, as the dehydrogenase can use many different compounds as electron acceptors, with the physiological substrate being coenzyme Q. D-amino acid dehydrogenase is an enzyme that catalyzes NADPH from NADP+ and D- glucose to produce D- amino acids and glucose dehydrogenase. Some but not limited to these amino acids are D-leucine, D-isoleucine, and D-Valine, which are essential amino acids that humans cannot synthesize due to the fact that they are not included in their diet. Moreover, D- amino acids catalyzes the formation of 2-oxo acids to produce D- amino acids in the presence of DCIP which is an electron acceptor. D-amino acids are used as components of pharmaceutical products, such as antibiotics, anticoagulants, and pesticides, because they have been shown to be not only more potent than their L enantiomers, but also more resistant to enzyme degradation. D-amino acid dehydrogenase enzymes have been synthesized via mutagenesis with an ability to produce straight, branched, cyclic aliphatic and aromatic D-amino acids. Solubilized D-amino acid dehydrogenase tends to increase its affinity for D-alanine, D-asparagine, and D--amino-n-butyrate. In E. coli K12 D-amino acid dehydrogenase is most active with D-alanine as its substrate, as this amino acid is the sole source of carbon, nitrogen, and energy. The enzyme works optimally at pH 8.9 and has a Michaelis constant for D-alanine equal to 30 mM. DAD discovered in gram-negative E. coli B membrane can convert L-amino acids into D-amino acids as well. Additionally, D- amino acid dehydrogenase is used in Dye-Linked dehydrogenase (Dye-DHs) which uses artificial dyes such as 2,6-Dichloroindophenol (DCIP) as their electron acceptor rather than using their natural electron acceptors. This can accelerate the reaction between the enzyme and the substrate when the electrons are being transferred. Use in synthesis reactions D-Amino Acid Dehydrogenase has shown itself to be effective in the synthesis of branched-chain amino acids such as D-Leucine, D-Isoleucine, and D-Valine. In the given study, researchers were successfully able to use D-amino acid dehydrogenase to create high amounts of these products from the starting material of 2-oxo acids, in the presence of ammonia. The conditions for this were variable, though the best results appeared at around 65 °C. Amino Acids obtained through these reactions resulted in a high enantioselectivity of >99% and high yields of >99%. Given the nature of this enzyme, it may be possible to use it in order to create non-branched D-amino acids as well as modified D-amino acids. Obtaining D-Amino Acid Dehydrogenase In one study, in order to test the viability of using D-amino dehydrogenase in synthesis reactions, researchers used mutant bacteria to obtain and create different strains of the enzyme. These researchers found that it only required five mutations in order to modify the selective D-Amino Dehydrogenase into working with other D-amino acids. They also found that it retained its highly selective nature, capable of receiving mostly D-enantiomers after mutation, with yields in excess of 95%. A heat-stable variant of D-amino acid dehydrogenase was found in the bacterium Rhodothermus marinus JCM9785. This variant is involved in the catabolism of trans-4-hydroxy-L-proline. From the given studies, in order to obtain D-amino acid dehydrogenase one must first introduce and express it within a given bacterial species, some of which have been previously referenced. It must then be purified under favorable conditions. These are based upon the particular species of D-amino acid dehydrogenase used in a given research experiment. Under incorrect conditions, the protein may denature. For example, it was found that specifically D-alanine dehydrogenases from E. coli and P. aeruginosa would lose most of their activity when subjected to conditions of 37 - 42 °C. After this, it is possible to separate and purify through existing methods. Artificial D-Amino Acid Dehydrogenase Due to the drawbacks of current methods, researchers have begun work on creating an artificial enzyme capable of producing the same D-amino acids as enzymes from naturally occurring sources. By adding five amino acids to a given sample isolated from U. thermosphaericus, they succeeded. By modifying the amino acid sequence, researchers were able to change the specificity of the molecule towards certain reactants and products, showing that it may be possible to use artificial D-amino acid dehydrogenase to screen for certain D-amino acid products. screen for certain D-amino acid products.
, La D-amminoacido deidrogenasi è un enzima … La D-amminoacido deidrogenasi è un enzima appartenente alla classe delle ossidoreduttasi, che catalizza la seguente reazione: un D-amminoacido + H2O + accettore ⇄ un 2-ossoacido + NH3 + accettore ridotto L'enzima è una flavoproteina (FAD). Agisce allo stesso modo sugli altri D-amminoacidi, eccetto D-aspartato e D-glutammato.acidi, eccetto D-aspartato e D-glutammato.
, La D-arginine déshydrogénase, ou D-aminoac … La D-arginine déshydrogénase, ou D-aminoacide déshydrogénase (anciennement EC 1.4.99.1) est une oxydoréductase qui catalyse la réaction : D-arginine + accepteur + H2O 5-guanidino-2-oxopentanoate + NH3 + accepteur réduit (réaction globale) : 1.
* D-arginine + accepteur iminoarginine + accepteur réduit 2.
* iminoarginine + H2O 5-guanidino-2-oxopentanoate + NH3 (spontané). Cette enzyme possède une très large spécificité par rapport à son substrat : elle agit sur à peu près tous les acides aminés D hormis sur le D-glutamate et le D-aspartate ; elle est inactive sur la glycine, et son activité est maximum sur la D-arginine et la D-lysine. Elle utilise du FAD et du fer non héminique comme cofacteurs. Cette réaction est distincte de celle catalysée par la D-aminoacide oxydase, qui utilise l'oxygène comme second substrat, tandis que la déshydrogénase peut utiliser différents composés comme accepteurs d'électrons, le substrat physiologique étant une coenzyme Q.bstrat physiologique étant une coenzyme Q.
|
| http://dbpedia.org/ontology/wikiPageExternalLink
|
http://enzyme.expasy.org/EC/1.4.99.1 +
, http://www.expasy.org/enzyme/1.4.99.1 +
, http://www.brenda-enzymes.org/php/result_flat.php4%3Fecno=1.4.99.1 +
|
| http://dbpedia.org/ontology/wikiPageID
|
12834891
|
| http://dbpedia.org/ontology/wikiPageLength
|
11580
|
| http://dbpedia.org/ontology/wikiPageRevisionID
|
1114197055
|
| http://dbpedia.org/ontology/wikiPageWikiLink
|
http://dbpedia.org/resource/Iron +
, http://dbpedia.org/resource/Microbial_metabolism +
, http://dbpedia.org/resource/Bacteria +
, http://dbpedia.org/resource/D-amino_acids +
, http://dbpedia.org/resource/Category:EC_1.4 +
, http://dbpedia.org/resource/Electron_transport_chain +
, http://dbpedia.org/resource/Oxygen +
, http://dbpedia.org/resource/Ketoacid +
, http://dbpedia.org/resource/Category:Cellular_respiration +
, http://dbpedia.org/resource/Category:Metabolism +
, http://dbpedia.org/resource/Flavin_group +
, http://dbpedia.org/resource/Oxidative_phosphorylation +
, http://dbpedia.org/resource/Coenzyme_Q +
, http://dbpedia.org/resource/D-amino_acid_oxidase +
|
| http://dbpedia.org/property/wikiPageUsesTemplate
|
http://dbpedia.org/resource/Template:Reflist +
, http://dbpedia.org/resource/Template:Short_description +
, http://dbpedia.org/resource/Template:Electron_transport_chain +
, http://dbpedia.org/resource/Template:CH-NH2_oxidoreductases +
, http://dbpedia.org/resource/Template:Enzymes +
, http://dbpedia.org/resource/Template:Portal +
, http://dbpedia.org/resource/Template:Cellular_respiration +
|
| http://purl.org/dc/terms/subject
|
http://dbpedia.org/resource/Category:Metabolism +
, http://dbpedia.org/resource/Category:EC_1.4 +
, http://dbpedia.org/resource/Category:Cellular_respiration +
|
| http://purl.org/linguistics/gold/hypernym
|
http://dbpedia.org/resource/Enzyme +
|
| http://www.w3.org/ns/prov#wasDerivedFrom
|
http://en.wikipedia.org/wiki/D-amino_acid_dehydrogenase?oldid=1114197055&ns=0 +
|
| http://xmlns.com/foaf/0.1/isPrimaryTopicOf
|
http://en.wikipedia.org/wiki/D-amino_acid_dehydrogenase +
|
| owl:sameAs |
https://global.dbpedia.org/id/4rf2r +
, http://ja.dbpedia.org/resource/D-%E3%82%A2%E3%83%AB%E3%82%AE%E3%83%8B%E3%83%B3%E3%83%87%E3%83%92%E3%83%89%E3%83%AD%E3%82%B2%E3%83%8A%E3%83%BC%E3%82%BC +
, http://sr.dbpedia.org/resource/D-aminokiselina_dehidrogenaza +
, http://dbpedia.org/resource/D-amino_acid_dehydrogenase +
, http://www.wikidata.org/entity/Q692574 +
, http://rdf.freebase.com/ns/m.02x6wps +
, http://sh.dbpedia.org/resource/D-aminokiselina_dehidrogenaza +
, http://it.dbpedia.org/resource/D-amminoacido_deidrogenasi +
, http://pt.dbpedia.org/resource/D-amino%C3%A1cido_desidrogenase +
, http://fr.dbpedia.org/resource/D-Arginine_d%C3%A9shydrog%C3%A9nase +
|
| rdf:type |
http://dbpedia.org/ontology/Protein +
|
| rdfs:comment |
D-amino-acid dehydrogenase (EC 1.4.99.1) i … D-amino-acid dehydrogenase (EC 1.4.99.1) is a bacterial enzyme that catalyses the oxidation of D-amino acids into their corresponding oxoacids. It contains both flavin and nonheme iron as cofactors. The enzyme has a very broad specificity and can act on most D-amino acids. D-amino acid + H2O + acceptor <=> a 2-oxo acid + NH3 + reduced acceptor This reaction is distinct from the oxidation reaction catalysed by D-amino acid oxidase that uses oxygen as a second substrate, as the dehydrogenase can use many different compounds as electron acceptors, with the physiological substrate being coenzyme Q. physiological substrate being coenzyme Q.
, La D-amminoacido deidrogenasi è un enzima … La D-amminoacido deidrogenasi è un enzima appartenente alla classe delle ossidoreduttasi, che catalizza la seguente reazione: un D-amminoacido + H2O + accettore ⇄ un 2-ossoacido + NH3 + accettore ridotto L'enzima è una flavoproteina (FAD). Agisce allo stesso modo sugli altri D-amminoacidi, eccetto D-aspartato e D-glutammato.acidi, eccetto D-aspartato e D-glutammato.
, D-アルギニンデヒドロゲナーゼ(D-arginine dehydrogenase)ま … D-アルギニンデヒドロゲナーゼ(D-arginine dehydrogenase)またはD-アミノ酸デヒドロゲナーゼ(D-amino-acid dehydrogenase)は、D-アミノ酸をそれぞれ対応するケト酸に酸化するバクテリア酵素である。補因子としてフラビンと非ヘム鉄を含む。この酵素は広範囲の特異性を持ち、ほとんどのD-アミノ酸に作用する。 D-アミノ酸 + H2O + 受容体 2-オキソ酸 + NH3 + 還元型受容体 この反応は、第二基質に酸素を用いるD-アミノ酸オキシダーゼによる酵素反応とは異なり、このデヒドロゲナーゼはいくつかの電子受容体を用いることが可能で、補酵素Qのような生理学的基質を用いる。ゼはいくつかの電子受容体を用いることが可能で、補酵素Qのような生理学的基質を用いる。
, La D-arginine déshydrogénase, ou D-aminoac … La D-arginine déshydrogénase, ou D-aminoacide déshydrogénase (anciennement EC 1.4.99.1) est une oxydoréductase qui catalyse la réaction : D-arginine + accepteur + H2O 5-guanidino-2-oxopentanoate + NH3 + accepteur réduit (réaction globale) : 1.
* D-arginine + accepteur iminoarginine + accepteur réduit 2.
* iminoarginine + H2O 5-guanidino-2-oxopentanoate + NH3 (spontané).uanidino-2-oxopentanoate + NH3 (spontané).
, A D-aminoácido desidrogenase (EC 1.4.99.1) … A D-aminoácido desidrogenase (EC 1.4.99.1) é uma enzima bacteriana que catalisa a oxidação de D-aminoácidos nos correspondentes oxiácidos. Contém flavina e ferro não-hemo como cofactores. A enzima possui uma larga especificidade e pode agir na maioria dos D-aminoácidos. D-aminoácido + H2O + aceitador ⇐> a 2-oxiácido + NH3 + aceitador reduzido Esta reacção é distinta da reacção de oxidação catalisada pela que utiliza o oxigénio como substrato secundário. A desidrogenase pode utilizar muitos compostos diferentes como aceitadore sde electrões, com o substrato fisiológico sendo a coenzima Q. substrato fisiológico sendo a coenzima Q.
|
| rdfs:label |
D-アルギニンデヒドロゲナーゼ
, D-amminoacido deidrogenasi
, D-amino acid dehydrogenase
, D-aminoácido desidrogenase
, D-Arginine déshydrogénase
|
