Oxidant dependent oxidation of copper bound catecholate: Catecholase versus catechol dioxygenase activity

Polyhedron ◽  
2015 ◽  
Vol 102 ◽  
pp. 185-192 ◽  
Author(s):  
Dóra Lakk-Bogáth ◽  
Róbert Csonka ◽  
Noémi Lorencz ◽  
Michel Giorgi ◽  
Gábor Speier ◽  
...  
Keyword(s):  
Catechol Dioxygenase ◽  
Dioxygenase Activity

To be structurally well-defined or not to be, that is not the question for iron(III)–poly(4-Vinylpyridine-co-acrylamide) to exhibit catechol dioxygenase activity!

2018 ◽  
Vol 106 ◽  
pp. 87-91
Author(s):  
Christopher J. Corcoran ◽  
Christian C. Tang ◽  
Vasiliki Lykourinou ◽  
Andrew C. Terentis ◽  
Alexander Angerhofer ◽  
...  
Keyword(s):  
Catechol Dioxygenase ◽  
Dioxygenase Activity

Catalytic Fate of Two Copper Complexes towards Phenoxazinone Synthase and Catechol Dioxygenase Activity

2017 ◽  
Vol 2 (34) ◽  
pp. 11040-11047 ◽  
Author(s):  
Mamoni Garai ◽  
Dhananjay Dey ◽  
Hare Ram Yadav ◽  
Angshuman Roy Choudhury ◽  
Milan Maji ◽  
...  
Keyword(s):  
Copper Complexes ◽  
Catechol Dioxygenase ◽  
Phenoxazinone Synthase ◽  
Dioxygenase Activity

Catalytic aspects of a nickel(II)–bipyridine complex towards phosphatase and catechol dioxygenase activity

Polyhedron ◽  
2017 ◽  
Vol 129 ◽  
pp. 114-122 ◽  
Author(s):  
Mamoni Garai ◽  
Dhananjay Dey ◽  
Hare Ram Yadav ◽  
Angshuman Roy Choudhury ◽  
Niranjan Kole ◽  
...  
Keyword(s):  
Catechol Dioxygenase ◽  
Dioxygenase Activity

Bioinspired Copper(I) Complexes that Exhibit Monooxygenase and Catechol Dioxygenase Activity

2014 ◽  
Vol 21 (3) ◽  
pp. 1198-1207 ◽  
Author(s):  
Aline Arnold ◽  
Ramona Metzinger ◽  
Christian Limberg
Keyword(s):  
Catechol Dioxygenase ◽  
Dioxygenase Activity

A new iron(III) complex of glycine derivative of amine-chloro substituted phenol ligand: Synthesis, characterization and catechol dioxygenase activity

2012 ◽  
Vol 1029 ◽  
pp. 60-67 ◽  
Author(s):  
Iraj Saberikia ◽  
Elham Safaei ◽  
Mohammad Hossein Kowsari ◽  
Yong-Ill Lee ◽  
Patricia Cotic ◽  
...  
Keyword(s):  
Catechol Dioxygenase ◽  
Glycine Derivative ◽  
Ligand Synthesis ◽  
Dioxygenase Activity

scholarly journals Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the corresponding cDNA

1997 ◽  
Vol 325 (3) ◽  
pp. 761-769 ◽  
Author(s):  
Isabelle GARCIA ◽  
Matthew RODGERS ◽  
Catherine LENNE ◽  
Anne ROLLAND ◽  
Alain SAILLAND ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Gel Filtration ◽  
Peptide Sequence ◽  
Amino Acid Residues ◽  
Carrot Cells ◽  
Expression Studies ◽  
Sds Page ◽  
Molecular Masses ◽  
The Difference ◽  
Dioxygenase Activity

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.

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

2013 ◽  
Vol 70 (2) ◽  
pp. 68-73 ◽  
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

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

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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