Human MutT homologue 1 (hMTH1) hydrolyzes a variety of oxidized purine nucleoside triphosphates, including 8-oxo-dGTP, 2-oxo-dATP, 2-oxo-ATP and 8-oxo-dATP, to their corresponding nucleoside monophosphates, while Esherichia coli MutT possesses prominent substrate specificity for 8-oxoguanine nucleotides. Three types of crystals were obtained corresponding to the following complexes: selenomethionine-labelled hMTH1 with 8-oxo-dGMP (SeMet hMTH1-8-oxo-dGMP), hMTH1 with 8-oxo-dGMP (hMTH1-8-oxodGMP) and hMTH1 with 2-oxo-dATP (hMTH1-2-oxo-dATP). Crystals of the SeMet hMTH1-8-oxo-dGMP complex belong to space group P4 1 2 1 2, with unitcell parameters a = b = 45.8, c = 153.6 Å , and diffracted to 2.90 Å . Crystals of hMTH1-8-oxo-dGMP and hMTH1-2-oxo-dATP belong to space groups P2 1 and P2 1 2 1 2 1 , with unit-cell parameters a = 34.0, b = 59.0, c = 65.9 Å , = 90.7 and a = 59.2, b = 67.3, c = 80.0 Å , respectively. Their diffraction data were collected at resolutions of 1.95 and 2.22 Å , respectively.
To clarify the degradation pathway of acrinol by light, isolation and identification of acrinol degradation products (ANDP) were attempted. A novel acrinol degradation product, ANDP-8, one of the ANDPs, was isolated by extraction with methanol from cloths dampened with acrinol solution, and purified by column chromatography on Diaion HP-10 and Sephadex LH-20. The structural elucidation of ANDP-8 was examined by infrared, 1 H-NMR, 13 C-NMR and electron impact ionization (EI)-mass spectra studies. From the spectroscopic data, the structure of ANDP-8 was determined to be 2-ethoxyl-6, 9-acridinediamine-5, 8-dione, that was found to be a novel degradation product of acrinol by light. Antimicrobial activities of ANDP-8 against Gram-positive bacteria were 10 to 100-fold higher than those of acrinol. ANDP-8 was also active against yeast and fungi. Nevertheless, acrinol did not show growth inhibition even at a concentration of 100 g/ml.
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