Results 241 to 250 of about 55,716 (280)
Some of the next articles are maybe not open access.
Cysteine dioxygenase: structure and mechanism
Chemical Communications, 2007AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Joseph, CA, Maroney, MJ
openaire +4 more sources
Essays in Biochemistry, 1999
Catechol dioxygenases are key enzymes in the metabolism of aromatic rings by soil bacteria. Catechol dioxygenases have been found that participate in the metabolism of halogenated aromatic compounds and, in doing so, play a key role in bioremediation of halogenated pollutants.
openaire +2 more sources
Catechol dioxygenases are key enzymes in the metabolism of aromatic rings by soil bacteria. Catechol dioxygenases have been found that participate in the metabolism of halogenated aromatic compounds and, in doing so, play a key role in bioremediation of halogenated pollutants.
openaire +2 more sources
Functionality of biphenyl 2,3-dioxygenase components in naphthalene 1,2-dioxygenase
Applied Microbiology and Biotechnology, 1999Naphthalene 1,2-dioxygenase (Nap dox) and biphenyl 2,3-dioxygenase (Bph dox) are related enzymes that have differentiated during evolution as their specificity has changed. Although their component arrangement is similar, the structure of each component has been modified quite extensively.
Michel Sylvestre, Diane Barriault
openaire +3 more sources
Applied Microbiology and Biotechnology, 2011
This review details recent progresses in the flavonoid biotransformation by bacterial non-heme dioxygenases, biphenyl dioxygenase (BDO), and naphthalene dioxygenase (NDO), which can initially activate biphenyl and naphthalene with insertion of dioxygen in stereospecfic and regiospecific manners.
Hor-Gil Hur +4 more
openaire +3 more sources
This review details recent progresses in the flavonoid biotransformation by bacterial non-heme dioxygenases, biphenyl dioxygenase (BDO), and naphthalene dioxygenase (NDO), which can initially activate biphenyl and naphthalene with insertion of dioxygen in stereospecfic and regiospecific manners.
Hor-Gil Hur +4 more
openaire +3 more sources
Biochemical and Biophysical Research Communications, 2013
Using different maximum-likelihood models of adaptive evolution, signatures of natural selective pressure, operating across the naphthalene family of dioxygenases, were examined. A lineage- and branch-site specific combined analysis revealed that purifying selection pressure dominated the evolutionary history of the enzyme family.
Joydeep Chakraborty +2 more
openaire +3 more sources
Using different maximum-likelihood models of adaptive evolution, signatures of natural selective pressure, operating across the naphthalene family of dioxygenases, were examined. A lineage- and branch-site specific combined analysis revealed that purifying selection pressure dominated the evolutionary history of the enzyme family.
Joydeep Chakraborty +2 more
openaire +3 more sources
4-Hydroxyphenylpyruvate dioxygenase
Archives of Biochemistry and Biophysics, 20054-Hydroxyphenylpyruvate dioxygenase (HPPD) is an Fe(II)-dependent, non-heme oxygenase that catalyzes the conversion of 4-hydroxyphenylpyruvate to homogentisate. This reaction involves decarboxylation, substituent migration and aromatic oxygenation in a single catalytic cycle.
openaire +3 more sources
Production of dyestuffs from indole derivatives by naphthalene dioxygenase and toluene dioxygenase
Letters in Applied Microbiology, 2003To isolate and characterize the phorate [O,O-diethyl-S-(ethylthio)methyl phosphoradiothioate] degrading bacteria from agricultural soil, and their assessment for multifarious biological activities of environmental and agronomic significance.Based on their morphological and biochemical characteristics, the selected isolates PS-1, PS-2 and PS-3 were ...
J Y, Kim +4 more
openaire +3 more sources
Expression of indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase in early concepti
Biochemical Journal, 2001Indoleamine 2,3-dioxygenase (IDO)-initiated tryptophan degradation in the placenta has been implicated in the prevention of the allogeneic fetus rejection [Munn, Zhou, Attwood, Bondarev, Conway, Marshall, Brown, and Mellor (1998) Science 281, 1191-1193].
Yohsuke Minatogawa +5 more
openaire +3 more sources
2012
Abstract The heme dioxygenase enzymes involved in tryptophan oxidation catalyse the first and rate-limiting step in the kynurenine pathway—the O 2 -dependent oxidation of l-tryptophan to N -formylkynurenine. In the past 10 years, there have been substantial new developments, including new structural information, bacterial expression systems for a ...
Efimov, I +5 more
openaire +3 more sources
Abstract The heme dioxygenase enzymes involved in tryptophan oxidation catalyse the first and rate-limiting step in the kynurenine pathway—the O 2 -dependent oxidation of l-tryptophan to N -formylkynurenine. In the past 10 years, there have been substantial new developments, including new structural information, bacterial expression systems for a ...
Efimov, I +5 more
openaire +3 more sources
Structure of the Terminal Oxygenase Component of Angular Dioxygenase, Carbazole 1,9a-Dioxygenase
Journal of Molecular Biology, 2005Carbazole 1,9a-dioxygenase (CARDO) catalyzes the dihydroxylation of carbazole by angular position (C9a) carbon bonding to the imino nitrogen and its adjacent C1 carbon. This reaction is an initial degradation reaction of the carbazole degradation pathway by various bacterial strains. Only a limited number of Rieske non-heme iron oxygenase systems (ROSs)
Zui Fujimoto +12 more
openaire +3 more sources