Arylamine N-acetyltransferase 1 protects against reactive oxygen species during glucose starvation: Role in the regulation of p53 stability. [PDF]
Human arylamine N-acetyltransferase 1 (NAT1) has been associated with cancer cell growth and invasion, but the underlying molecular mechanisms remain unknown.
LiLi Wang +2 more
doaj +2 more sources
Determination of Arylamine N-Acetyltransferase 2 Acetylation Genotype by PCR and Phenotyping Using Dapsone Through High-Pressure Liquid Chromatography Assay: A Gender Wise Study [PDF]
The main aim of the study was to establish the acetylation status of local population of Pakistan by N-acetyltransferase 2 (NAT2) enzyme and to find out the concordance between phenotypic and genotypic methods for the determination of NAT2 acetylation ...
Naheed Akhter +5 more
doaj +2 more sources
Distribution of arylamine N-acetyltransferase 2 (NAT2) genotypes among Omanis [PDF]
Objective: to determine the genotypes of arylamine N-acetyltransferase (NAT2) among 127 unrelated apparently healthy Omanis. Method: Identify the most common known polymorphisms of NAT*2 gene namely, G191A, C282T, C341T, C481T, G590A, A803G and G857A ...
Musbah O. M. Tanira +5 more
doaj +2 more sources
Expression of arylamine N-acetyltransferase 2 activity in immortalized human bronchial epithelial cells. [PDF]
Lung cancer is the leading cause of cancer deaths in the United States with high incidence in tobacco smokers. Arylamine N-acetyltransferase 2 (NAT2) is a xenobiotic enzyme that catalyzes both N- and O-acetylation of carcinogens present in tobacco smoke ...
Wise JTF +4 more
europepmc +3 more sources
Arylamine N-Acetyltransferases in Mycobacteria [PDF]
Polymorphic Human arylamine N-acetyltransferase (NAT2) inactivates the anti-tubercular drug isoniazid by acetyltransfer from acetylCoA. There are active NAT proteins encoded by homologous genes in mycobacteria including M. tuberculosis, M. bovis BCG, M. smegmatis and M. marinum. Crystallographic structures of NATs from M. smegmatis and M.
Sim E +8 more
openaire +4 more sources
Arylamine N-acetyltransferases catalyze the transfer of acetyl groups from the endogenous cofactor acetyl coenzyme A (AcCoA) to arylamine (N-acetylation) and N-hydroxy-arylamine (O-acetylation) acceptors.
David W. Hein +2 more
doaj +1 more source
Pharmacogenetics of the arylamine N-acetyltransferases [PDF]
The arylamine N-acetyltransferases (NATs) are involved in the metabolism of a variety of different compounds that we are exposed to on a daily basis. Many drugs and chemicals found in the environment, such as those in cigarette smoke, car exhaust fumes and in foodstuffs, can be either detoxified by NATs and eliminated from the body or bioactivated to ...
Butcher, N. J. +3 more
openaire +5 more sources
Reaction Engineering and Comparison of Electroenzymatic and Enzymatic ATP Regeneration Systems
An electrochemically coupled ATP regeneration by pyruvate oxidase and acetate kinase for the phosphorylation of mevalonate was established and expanded by a polyphosphate kinase. The reaction was characterized and compared with other ATP regenerating systems in terms of the phosphate donor properties and biocatalytic metrics.
Regine Siedentop +4 more
wiley +1 more source
Abstract Globally, tuberculosis (TB) is the second most lethal infectious disease. However, in sub‐Saharan Africa, TB has the largest disease burden, with drug‐resistant TB increasingly becoming a concern. The social and economic impact of TB should not be overlooked, especially in areas where healthcare systems are overburdened, and resources need to ...
Carola Oelofse +3 more
wiley +1 more source
Bioactivity and health effects of garlic essential oil: A review
This paper reviews the research progress on the composition and bioactivities of garlic essential oil mixtures and the bioactivity of some typical monomeric sulfides in garlic essential oil. The active mechanisms of representative sulfides in garlic essential oil were analyzed, and the applications of garlic essential oil in functional food, food ...
Lei Huang +6 more
wiley +1 more source

