In this study, benzoate dioxygenase from Rhodococcus ruber UKMP-5M was catalyzed by oxidating the benzene ring to catechol and other derivatives. The benzoate dioxygenase (benA gene) from Rhodococcus ruber UKMP-5M was then expressed, purified, characterized, The benA gene was amplified (642 bp), and the product was cloned into a pGEM-T vector.The recombinant plasmid pGEMT-benA was digested by d...

The aerobic degradation of aromatic compounds by bacteria is performed by dioxygenases. To show some characteristic patterns of the dioxygenase genotype and its degradation specificities, twenty-nine gram-negative bacterial cultures were obtained from sediment contaminated with phenolic compounds in Wuhan, China. The isolates were phylogenetically diverse and belonged to 10 genera. All 29 gram-...

It is shown that bacteria Bradyrhizobium japonicum 273 were capable of degrading phenol at moderate concentrations either in a free cell culture or by immobilized cells on granulated activated carbon particles. The amount degraded was greater an preparation than culture. application constant electric field during cultivation led to enhanced biodegradation and carbon. highest removal efficiency ...

BACKGROUND Expression of the tryptophan catabolizing enzyme, indoleamine 2,3-dioxygenase, in the mouse placenta has been shown to be critical in preventing immunological rejection of the fetal allograft. To clarify the physiological importance of indoleamine 2,3-dioxygenase in human pregnancy, we have studied how the expression of this enzyme changes during decidualization of human endometrium ...

Our previous studies showed, bacterium Aquamicrobium sp. SK-2 can degrade biphenyl and polychlorinated biphenyls (PCBs). In the present study, proteins involved in degradation was evaluated using various molecular biology methods. The gene bphC strain identified polymerase chain reaction method. Further key enzyme degradation, 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) purified through anion ...

Previously, we pointed out the importance of the kynurenine metabolism in fetuses and neonates. We examined localization and developmental change of indoleamine 2,3-dioxygenase activity in human placenta. The indoleamine 2,3-dioxygenase was found localized in syncytiotrophoblast in the placenta. The indoleamine 2,3-dioxygenase activity was not detected in placenta in the early stage of gestatio...

BACKGROUND The immunoregulatory enzyme indoleamine 2,3-dioxygenase, which catalyzes the conversion of tryptophan into kynurenine, is expressed in a significant subset of patients with acute myeloid leukemia, resulting in the inhibition of T-cell proliferation and the induction of regulatory T cells. Acute myeloid leukemia cells can be differentiated into dendritic cells, which have increased im...

biodegradation of polycyclic aromatic hydrocarbons, toxic compounds widely distributed in the environment by bacteria, is a cheap and safe cleaning up method. the present study attempts to isolate and characterize dioxygenase-producing bacteria which are able to degrade phenanthrene and pyrene from refinery soils. it also aims to assess in vitro biodegradation. to do so, two contaminated soil s...

indolemine 2, 3-dioxygenase (ido) is a cytosolic monomeric hemoprotein enzyme that catalyses tryptophan, the least available essential amino acid in the human body, to n-formylkynurenine, which in turn rapidly degrades to give kynurenine. ido is expressed in different tissues, especially and prominently in some subsets of antigen presenting cells (apcs) of lymphoid organs and also in the placen...

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 ampli...