scholarly journals Understanding human thiol dioxygenase enzymes: structure to function, and biology to pathology

2017 ◽  
Vol 98 (2) ◽  
pp. 52-66 ◽  
Author(s):  
Bibekananda Sarkar ◽  
Mahesh Kulharia ◽  
Anil K. Mantha
Keyword(s):  
2007 ◽  
Vol 129 (48) ◽  
pp. 14846-14847 ◽  
Author(s):  
Swathi Aluri ◽  
Sam P. de Visser

2000 ◽  
Vol 66 (2) ◽  
pp. 678-683 ◽  
Author(s):  
Matthew B. Mesarch ◽  
Cindy H. Nakatsu ◽  
Loring Nies

ABSTRACT Benzene, toluene, xylenes, phenol, naphthalene, and biphenyl are among a group of compounds that have at least one reported pathway for biodegradation involving catechol 2,3-dioxygenase enzymes. Thus, detection of the corresponding catechol 2,3-dioxygenase genes can serve as a basis for identifying and quantifying bacteria that have these catabolic abilities. Primers that can successfully amplify a 238-bp catechol 2,3-dioxygenase gene fragment from eight different bacteria are described. The identities of the amplicons were confirmed by hybridization with a 238-bp catechol 2,3-dioxygenase probe. The detection limit was 102 to 103 gene copies, which was lowered to 100 to 101 gene copies by hybridization. Using the dioxygenase-specific primers, an increase in catechol 2,3-dioxygenase genes was detected in petroleum-amended soils. The dioxygenase genes were enumerated by competitive quantitative PCR with a 163-bp competitor that was amplified using the same primers. Target and competitor sequences had identical amplification kinetics. Potential PCR inhibitors that could coextract with DNA, nonamplifying DNA, soil factors (humics), and soil pollutants (toluene) did not impact enumeration. Therefore, this technique can be used to accurately and reproducibly quantify catechol 2,3-dioxygenase genes in complex environments such as petroleum-contaminated soil. Direct, non-cultivation-based molecular techniques for detecting and enumerating microbial pollutant-biodegrading genes in environmental samples are powerful tools for monitoring bioremediation and developing field evidence in support of natural attenuation.


Marine Drugs ◽  
2018 ◽  
Vol 16 (8) ◽  
pp. 268 ◽  
Author(s):  
Fengjie Li ◽  
Dorte Janussen ◽  
Christian Peifer ◽  
Ignacio Pérez-Victoria ◽  
Deniz Tasdemir

The Antarctic deep-sea sponge Latrunculia (Latrunculia) biformis Kirkpatrick, 1908 (Class Demospongiae Sollas, Order Poecilosclerida Topsent, Latrunculiidae Topsent) was selected for chemical analyses due to its potent anticancer activity. Metabolomic analysis of its crude extract by HRMS/MS-based molecular networking showed the presence of several clusters of pyrroloiminoquinone alkaloids, i.e., discorhabdin and epinardin-type brominated pyridopyrroloquinolines and tsitsikammamines, the non-brominated bis-pyrroloiminoquinones. Molecular networking approach combined with a bioactivity-guided isolation led to the targeted isolation of the known pyrroloiminoquinone tsitsikammamine A (1) and its new analog 16,17-dehydrotsitsikammamine A (2). The chemical structures of the compounds 1 and 2 were elucidated by spectroscopic analysis (one-dimensional (1D) and two-dimensional (2D) NMR, HR-ESIMS). Due to minute amounts, molecular modeling and docking was used to assess potential affinities to potential targets of the isolated compounds, including DNA intercalation, topoisomerase I-II, and indoleamine 2,3-dioxygenase enzymes. Tsitsikammamines represent a small class of pyrroloiminoquinone alkaloids that have only previously been reported from the South African sponge genus Tsitsikamma Samaai & Kelly and an Australian species of the sponge genus Zyzzya de Laubenfels. This is the first report of tsitsikammamines from the genus Latrunculia du Bocage and the successful application of molecular networking in the identification of comprehensive chemical inventory of L. biformis followed by targeted isolation of new molecules. This study highlights the high productivity of secondary metabolites of Latrunculia sponges and may shed new light on their biosynthetic origin and chemotaxonomy.


Author(s):  
M Ahmad ◽  
Q Ali ◽  
MM Hafeez ◽  
A Malik

The field of biotechnology has extraordinary influence on science, law, the administrative condition social insurance, and business throughout the world. As the starting of agriculture, people have been manipulating crops to improve the yield and quantity. Product yields throughout the world are essentially diminished by the activity of herbivorous insects, pathogens, and parasites. Natural environmental stresses make this circumstance significantly worse. Biotechnology can be used to increase the yield of food crops, to improve biotic and abiotic stress tolerance, to modify the traits of the plant (e.g. oil content, percentage of lignin, cell structure), to make the conversion to liquid biofuels more efficient. Various genes have been discovered for biotic and abiotic stress tolerance. The genes discovered for biotic stress are aryloxyalkanoate, dioxygenase, enzymes (aad-1), nitrilase, Cry1Ac, Cry2AB, GTgene, AFP (anti-freezing protein gene) gene, Chitinase II and III gene, and Rps1-k. The genes discovered for abiotic stress are SgNCED1, SgNCED1, USP2, HSP70, BADH, and ALO, PVNCED1, HVA1, LeNCED1. CRISPRs (clustered regularly interspaced short palindromic repeats) are the short DNA sequences present in bacteria and archaeal genomes which are now currently used by researchers to edit the genome. In different plant species (calli, leaf discs) protoplasts have been successfully used to edit their genome through CRISPR/Cas9 system. The aims of the applications are to increase resistance to abiotic or biotic stress, to engineer metabolic pathways, and to increase grain yield. Incorporation of modern biotechnology, with regular traditional practices in a sustainable way, can fulfill the objective of achieving food security for the present and as well as in future.


1998 ◽  
Vol 180 (9) ◽  
pp. 2337-2344 ◽  
Author(s):  
Rebecca E. Parales ◽  
Matthew D. Emig ◽  
Nancy A. Lynch ◽  
David T. Gibson

ABSTRACT Bacterial three-component dioxygenase systems consist of reductase and ferredoxin components which transfer electrons from NAD(P)H to a terminal oxygenase. In most cases, the oxygenase consists of two different subunits (α and β). To assess the contributions of the α and β subunits of the oxygenase to substrate specificity, hybrid dioxygenase enzymes were formed by coexpressing genes from two compatible plasmids in Escherichia coli. The activities of hybrid naphthalene and 2,4-dinitrotoluene dioxygenases containing four different β subunits were tested with four substrates (indole, naphthalene, 2,4-dinitrotoluene, and 2-nitrotoluene). In the active hybrids, replacement of small subunits affected the rate of product formation but had no effect on the substrate range, regiospecificity, or enantiomeric purity of oxidation products with the substrates tested. These studies indicate that the small subunit of the oxygenase is essential for activity but does not play a major role in determining the specificity of these enzymes.


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