L-DOPA Dioxygenase Activity on 6-Substituted Dopamine Analogues

p-Hydroxyphenylpyruvate dioxygenase catalyses the transformation of p-hydroxyphenylpyruvate into homogentisate. In plants this enzyme has a crucial role because homogentisate is the aromatic precursor of all prenylquinones. Furthermore this enzyme was recently identified as the molecular target for new families of potent herbicides. In this study we examine precisely the localization of p-hydroxyphenylpyruvate dioxygenase activity within carrot cells. Our results provide evidence that, in cultured carrot cells, p-hydroxyphenylpyruvate dioxygenase is associated with the cytosol. Purification and SDS/PAGE analysis of this enzyme revealed that its activity is associated with a polypeptide of 45–46 kDa. This protein specifically cross-reacts with an antiserum raised against the p-hydroxyphenylpyruvate dioxygenase of Pseudomonas fluorescens. Gel-filtration chromatography indicates that the enzyme behaves as a homodimer. We also report the isolation and nucleotide sequence of a cDNA encoding a carrot p-hydroxyphenylpyruvate dioxygenase. The nucleotide sequence (1684 bp) encodes a protein of 442 amino acid residues with a molecular mass of 48094 Da and shows specific C-terminal regions of similarity with other p-hydroxyphenylpyruvate dioxygenases. This cDNA encodes a functional p-hydroxyphenylpyruvate dioxygenase, as evidenced by expression studies with transformed Escherichia coli cells. Comparison of the N-terminal sequence of the 45–46 kDa polypeptide purified from carrot cells with the deduced peptide sequence of the cDNA confirms that this polypeptide supports p-hydroxyphenylpyruvate dioxygenase activity. Immunodetection studies of the native enzyme in carrot cellular extracts reveal that N-terminal proteolysis occurs during the process of purification. This proteolysis explains the difference in molecular masses between the purified protein and the deduced polypeptide.

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The effects of trace elements, cations, and environmental conditions on protocatechuate 3,4-dioxygenase activity

Scientia Agricola ◽

10.1590/s0103-90162013000200002 ◽

2013 ◽

Vol 70 (2) ◽

pp. 68-73 ◽

Cited By ~ 6

Author(s):

Andréa Scaramal da Silva ◽

Rodrigo Josemar Seminoti Jacques ◽

Robson Andreazza ◽

Fátima Menezes Bento ◽

Flávio Anastácio de Oliveira Camargo

Keyword(s):

Trace Elements ◽

Environmental Conditions ◽

Dioxygenase Activity

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Citalopram decreases tryptophan 2,3-dioxygenase activity and brain 5-HT turnover in swim stressed rats

Pharmacological Reports ◽

10.1016/s1734-1140(12)70851-4 ◽

2012 ◽

Vol 64 (3) ◽

pp. 558-566 ◽

Cited By ~ 24

Author(s):

Iffat Ara ◽

Samina Bano

Keyword(s):

Dioxygenase Activity

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Cyclic analogue of S-benzylisothiourea that suppresses kynurenine production without inhibiting indoleamine 2,3-dioxygenase activity

Bioorganic & Medicinal Chemistry Letters ◽

10.1016/j.bmcl.2018.07.034 ◽

2018 ◽

Vol 28 (17) ◽

pp. 2846-2849

Author(s):

Miwa Fukuda ◽

Tomomi Sasaki ◽

Tomoko Hashimoto ◽

Hiroyuki Miyachi ◽

Minoru Waki ◽

...

Keyword(s):

Indoleamine 2,3 Dioxygenase ◽

Dioxygenase Activity

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Resveratrol intake enhances indoleamine-2,3-dioxygenase activity in humans

Pharmacological Reports ◽

10.1016/j.pharep.2016.06.008 ◽

2016 ◽

Vol 68 (5) ◽

pp. 1065-1068 ◽

Cited By ~ 6

Author(s):

Guido A. Gualdoni ◽

Dietmar Fuchs ◽

Gerhard J. Zlabinger ◽

Johanna M. Gostner

Keyword(s):

Indoleamine 2,3 Dioxygenase ◽

Dioxygenase Activity

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Chemical Constituents of Cordyceps cicadae

Natural Product Communications ◽

10.1177/1934578x1501001233 ◽

2015 ◽

Vol 10 (12) ◽

pp. 1934578X1501001 ◽

Cited By ~ 3

Author(s):

Zhi-Bo Chu ◽

Jun Chang ◽

Ying Zhu ◽

Xun Sun

Keyword(s):

Amino Acids ◽

Spectroscopic Analysis ◽

Chemical Constituents ◽

2D Nmr ◽

Cordyceps Cicadae ◽

Nmr Techniques ◽

Dopamine Analogues

One new bifuran derivative (1), together with fourteen known compounds, were isolated from Cordyceps cicadae X. Q. Shing. The known compounds included nine nucleosides, uracil (2), uridine (3), 2′-deoxyuridine (4), 2′-deoxyinosine (5), guanosine (6), 2′-deoxyguanosine (7), thymidine (8), adenosine (9), and 2′-deoxyadenosine (10); three amino acids tryptophan (11), phenylalanine (12), and tyrosine (13); and two dopamine analogues N-acetylnoradrenaline (14) and its dimer, trans–2-(3′,4′-dihydroxyphenyl)-3-acetylamino-7-( N-acetyl-2″-amino-ethylene)-1,4-benzodioxane (15). Their structures were decisively elucidated by spectroscopic analysis, including 1D and 2D NMR techniques.

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Brain and serum concentrations of dopamine analogues after peripheral administration to rats

Naunyn-Schmiedeberg s Archives of Pharmacology ◽

10.1007/bf00505319 ◽

1984 ◽

Vol 326 (3) ◽

pp. 203-209 ◽

Cited By ~ 2

Author(s):

Matthijs G. P. Feenstra ◽

Jan Willem Homan ◽

Roelof Everts ◽

Hans Rollema ◽

Alan S. Horn

Keyword(s):

Serum Concentrations ◽

Dopamine Analogues

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Phage-encoded ten-eleven translocation dioxygenase (TET) is active in C5-cytosine hypermodification in DNA

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.2026742118 ◽

2021 ◽

Vol 118 (26) ◽

pp. e2026742118

Author(s):

Evan J. Burke ◽

Samuel S. Rodda ◽

Sean R. Lund ◽

Zhiyi Sun ◽

Malcolm R. Zeroka ◽

...

Keyword(s):

Phylogenetic Tree ◽

Epigenetic Regulation ◽

Binding Protein ◽

Gene Clusters ◽

Dna Packaging ◽

Methyl Groups ◽

Sequence Specificity ◽

Host Restriction ◽

Tet Enzymes ◽

Dioxygenase Activity

TET/JBP (ten-eleven translocation/base J binding protein) enzymes are iron(II)- and 2-oxo-glutarate–dependent dioxygenases that are found in all kingdoms of life and oxidize 5-methylpyrimidines on the polynucleotide level. Despite their prevalence, few examples have been biochemically characterized. Among those studied are the metazoan TET enzymes that oxidize 5-methylcytosine in DNA to hydroxy, formyl, and carboxy forms and the euglenozoa JBP dioxygenases that oxidize thymine in the first step of base J biosynthesis. Both enzymes have roles in epigenetic regulation. It has been hypothesized that all TET/JBPs have their ancestral origins in bacteriophages, but only eukaryotic orthologs have been described. Here we demonstrate the 5mC-dioxygenase activity of several phage TETs encoded within viral metagenomes. The clustering of these TETs in a phylogenetic tree correlates with the sequence specificity of their genomically cooccurring cytosine C5-methyltransferases, which install the methyl groups upon which TETs operate. The phage TETs favor Gp5mC dinucleotides over the 5mCpG sites targeted by the eukaryotic TETs and are found within gene clusters specifying complex cytosine modifications that may be important for DNA packaging and evasion of host restriction.

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