Topaquinone (BioDeep_00000032139)

   

human metabolite Endogenous


代谢物信息卡片


(2S)-2-amino-3-(6-hydroxy-3,4-dioxocyclohexa-1,5-dien-1-yl)propanoic acid

化学式: C9H9NO5 (211.0481)
中文名称:
谱图信息: 最多检出来源 Mus musculus(not specific) 3.66%

分子结构信息

SMILES: C(C1=CC(=O)C(=CC1=O)O)[C@@H](C(=O)O)N
InChI: InChI=1S/C9H9NO5/c10-5(9(14)15)1-4-2-7(12)8(13)3-6(4)11/h2-3,5,11H,1,10H2,(H,14,15)/t5-/m0/s1

描述信息

Topaquinone (TPQ), is the quinone of 2,4,5-trihydroxyphenylalanine. TPQ is the cofactor in most copper-containing amine oxidases. It is produced by post-translational modification of a strictly conserved active-site tyrosine residue with the participation of the copper ion at the active site. Once formed, TPQ acts as a switch between the heterolytic transformation of amine substrates to aldehydes, via a pyridoxal phosphate-like Schiff base complex, and one electron chemistry involving reduction of molecular oxygen (PMID: 12686122) [HMDB]
Topaquinone (TPQ), is the quinone of 2,4,5-trihydroxyphenylalanine. TPQ is the cofactor in most copper-containing amine oxidases. It is produced by post-translational modification of a strictly conserved active-site tyrosine residue with the participation of the copper ion at the active site. Once formed, TPQ acts as a switch between the heterolytic transformation of amine substrates to aldehydes, via a pyridoxal phosphate-like Schiff base complex, and one electron chemistry involving reduction of molecular oxygen (PMID: 12686122).

同义名列表

18 个代谢物同义名

(2S)-2-amino-3-(6-hydroxy-3,4-dioxocyclohexa-1,5-dien-1-yl)propanoic acid; alpha-Amino-6-hydroxy-3,4-dioxo-(as)-1,5-cyclohexadiene-1-propanoic acid; (S)-alpha-Amino-6-hydroxy-3,4-dioxo-1,5-cyclohexadiene-1-propanoic acid; alpha-Amino-6-hydroxy-3,4-dioxo-(as)-1,5-cyclohexadiene-1-propanoate; a-Amino-6-hydroxy-3,4-dioxo-(as)-1,5-cyclohexadiene-1-propanoic acid; (S)-alpha-Amino-6-hydroxy-3,4-dioxo-1,5-cyclohexadiene-1-propanoate; (S)-a-Amino-6-hydroxy-3,4-dioxo-1,5-cyclohexadiene-1-propanoic acid; a-Amino-6-hydroxy-3,4-dioxo-(as)-1,5-cyclohexadiene-1-propanoate; (S)-a-Amino-6-hydroxy-3,4-dioxo-1,5-cyclohexadiene-1-propanoate; 6-Hydroxydopa quinone, (6-OH-3,4-dioxo)-tautomer; 2,4,5-Trihydroxyphenylalanine quinone; 6-Hydroxyphenylalanine-3,4-dione; 6-Hydroxydopa quinone; 6-Hydroxydopaquinone; O-Topaquinone; Topa quinone; Topaquinone; TPQ



数据库引用编号

10 个数据库交叉引用编号

分类词条

相关代谢途径

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代谢反应

0 个相关的代谢反应过程信息。

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BioCyc(0)

WikiPathways(0)

Plant Reactome(0)

INOH(0)

PlantCyc(0)

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PharmGKB(0)

1 个相关的物种来源信息

在这里通过桑基图来展示出与当前的这个代谢物在我们的BioDeep知识库中具有相关联信息的其他代谢物。在这里进行关联的信息来源主要有:

  • PubMed: 来源于PubMed文献库中的文献信息,我们通过自然语言数据挖掘得到的在同一篇文献中被同时提及的相关代谢物列表,这个列表按照代谢物同时出现的文献数量降序排序,取前10个代谢物作为相关研究中关联性很高的代谢物集合展示在桑基图中。
  • NCBI Taxonomy: 通过文献数据挖掘,得到的代谢物物种来源信息关联。这个关联信息同样按照出现的次数降序排序,取前10个代谢物作为高关联度的代谢物集合展示在桑吉图上。
  • Chemical Taxonomy: 在物质分类上处于同一个分类集合中的其他代谢物
  • Chemical Reaction: 在化学反应过程中,存在为当前代谢物相关联的生化反应过程中的反应底物或者反应产物的关联代谢物信息。

点击图上的相关代谢物的名称,可以跳转到相关代谢物的信息页面。

亚细胞结构定位 关联基因列表


文献列表

  • Heli Elovaara, Heidi Kidron, Vimal Parkash, Yvonne Nymalm, Eva Bligt, Pauli Ollikka, David J Smith, Marjo Pihlavisto, Marko Salmi, Sirpa Jalkanen, Tiina A Salminen. Identification of two imidazole binding sites and key residues for substrate specificity in human primary amine oxidase AOC3. Biochemistry. 2011 Jun; 50(24):5507-20. doi: 10.1021/bi200117z. [PMID: 21585208]
  • Hossein Heli, Mojtaba Amani, Ali Akbar Moosavi-Movahedi, Ali Jabbari, Giovanni Floris, Anna Mura. Electroactive centers in Euphorbia latex and lentil seedling amine oxidases. Bioscience, biotechnology, and biochemistry. 2008 Jan; 72(1):29-36. doi: 10.1271/bbb.70299. [PMID: 18175931]
  • Anna Mura, Roberto Anedda, Francesca Pintus, Mariano Casu, Alessandra Padiglia, Giovanni Floris, Rosaria Medda. An important lysine residue in copper/quinone-containing amine oxidases. The FEBS journal. 2007 May; 274(10):2585-95. doi: 10.1111/j.1742-4658.2007.05793.x. [PMID: 17433047]
  • Anna Mura, Alessandra Padiglia, Rosaria Medda, Francesca Pintus, Alessandro Finazzi Agrò, Giovanni Floris. Properties of copper-free pig kidney amine oxidase: role of topa quinone. FEBS letters. 2006 Aug; 580(18):4317-24. doi: 10.1016/j.febslet.2006.06.089. [PMID: 16842785]
  • Zbynĕk Lamplot, Marek Sebela, Petr Frycák, Silvia Longu, Alessandra Padiglia, Rosaria Medda, Giovanni Floris, Pavel Pec. Reactions of plant copper/topaquinone amine oxidases with N6-aminoalkyl derivatives of adenine. Journal of enzyme inhibition and medicinal chemistry. 2005 Apr; 20(2):143-51. doi: 10.1080/14756360400021866. [PMID: 15968819]
  • Alessandra Padiglia, Giovanni Floris, Silvia Longu, M Eugenia Schininà, Jens Z Pedersen, Alessandro Finazzi Agrò, Francesco De Angelis, Rosaria Medda. Inhibition of lentil copper/TPQ amine oxidase by the mechanism-based inhibitor derived from tyramine. Biological chemistry. 2004 Mar; 385(3-4):323-9. doi: 10.1515/bc.2004.028. [PMID: 15134347]
  • Bradley O Elmore, John A Bollinger, David M Dooley. Human kidney diamine oxidase: heterologous expression, purification, and characterization. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 2002 Jun; 7(6):565-79. doi: 10.1007/s00775-001-0331-1. [PMID: 12072962]
  • Q Su, J P Klinman. Probing the mechanism of proton coupled electron transfer to dioxygen: the oxidative half-reaction of bovine serum amine oxidase. Biochemistry. 1998 Sep; 37(36):12513-25. doi: 10.1021/bi981103l. [PMID: 9730824]
  • N Nakamura, P Moënne-Loccoz, K Tanizawa, M Mure, S Suzuki, J P Klinman, J Sanders-Loehr. Topaquinone-dependent amine oxidases: identification of reaction intermediates by Raman spectroscopy. Biochemistry. 1997 Sep; 36(38):11479-86. doi: 10.1021/bi9708139. [PMID: 9298968]
  • E Agostinelli, G De Matteis, A Sinibaldi, B Mondovì, L Morpurgo. Reactions of the oxidized organic cofactor in copper-depleted bovine serum amine oxidase. The Biochemical journal. 1997 Jun; 324 ( Pt 2)(?):497-501. doi: 10.1042/bj3240497. [PMID: 9182709]
  • V Kumar, D M Dooley, H C Freeman, J M Guss, I Harvey, M A McGuirl, M C Wilce, V M Zubak. Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 A resolution. Structure (London, England : 1993). 1996 Aug; 4(8):943-55. doi: 10.1016/s0969-2126(96)00101-3. [PMID: 8805580]
  • V Steinebach, G A De Jong, S S Wijmenga, S De Vries, J A Duine. The copper-topaquinone-phenylhydrazine-adduct geometry in Escherichia coli amine oxidase derivatized with phenylhydrazines substituted with 19F-NMR relaxation measurements. European journal of biochemistry. 1996 Jun; 238(3):683-9. doi: 10.1111/j.1432-1033.1996.0683w.x. [PMID: 8706668]
  • V Steinebach, B W Groen, S S Wijmenga, W M Niessen, J A Jongejan, J A Duine. Identification of topaquinone, as illustrated for pig kidney diamine oxidase and Escherichia coli amine oxidase. Analytical biochemistry. 1995 Sep; 230(1):159-66. doi: 10.1006/abio.1995.1451. [PMID: 8585612]
  • G Alton, T H Taher, R J Beever, M M Palcic. Stereochemistry of benzylamine oxidation by copper amine oxidases. Archives of biochemistry and biophysics. 1995 Jan; 316(1):353-61. doi: 10.1006/abbi.1995.1047. [PMID: 7840636]
  • S M Janes, J P Klinman. Isolation of 2,4,5-trihydroxyphenylalanine quinone (topa quinone) from copper amine oxidases. Methods in enzymology. 1995; 258(?):20-34. doi: 10.1016/0076-6879(95)58034-4. [PMID: 8524151]
  • M M Palcic, S M Janes. Spectrophotometric detection of topa quinone. Methods in enzymology. 1995; 258(?):34-8. doi: 10.1016/0076-6879(95)58035-2. [PMID: 8524159]
  • M A McGuirl, C D McCahon, K A McKeown, D M Dooley. Purification and characterization of pea seedling amine oxidase for crystallization studies. Plant physiology. 1994 Nov; 106(3):1205-11. doi: 10.1104/pp.106.3.1205. [PMID: 7824646]
  • S M Janes, M M Palcic, C H Scaman, A J Smith, D E Brown, D M Dooley, M Mure, J P Klinman. Identification of topaquinone and its consensus sequence in copper amine oxidases. Biochemistry. 1992 Dec; 31(48):12147-54. doi: 10.1021/bi00163a025. [PMID: 1457410]
  • D Mu, S M Janes, A J Smith, D E Brown, D M Dooley, J P Klinman. Tyrosine codon corresponds to topa quinone at the active site of copper amine oxidases. The Journal of biological chemistry. 1992 Apr; 267(12):7979-82. doi: 10.1016/s0021-9258(18)42395-2. [PMID: 1569055]
  • D E Brown, M A McGuirl, D M Dooley, S M Janes, D Mu, J P Klinman. The organic functional group in copper-containing amine oxidases. Resonance Raman spectra are consistent with the presence of topa quinone (6-hydroxydopa quinone) in the active site. The Journal of biological chemistry. 1991 Mar; 266(7):4049-51. doi: . [PMID: 1900285]