Kinetic and docking studies of cytosolic/tumor-associated carbonic anhydrase isozymes I, II and IX with some hydroxylic compounds.

A series of hydroxylic compounds (1-10, NK-154 and NK-168) have been assayed for the inhibition of three physiologically relevant carbonic anhydrase isozymes, the cytosolic isozymes I, II and tumor-associated isozyme IX. The investigated compounds showed inhibition constants in the range of 0.068-4003, 0.

Synthesis and biological activity of novel thiourea derivatives as carbonic anhydrase inhibitors.

A new series of chiral thiourea derivatives (5a-5c) and thiourea containing benzimidazole moieties (9b-9e) were synthesized from different amino acids (l-valine, l-isoleucine, l-methionine, l-phenylalanine, and d-phenylglycine). The compounds were characterized and tested against the two most studied members of the pH regulatory enzyme family, carbonic anhydrase (CA, EC 4.2.

trans-Diaqua{5,5'-[(E,E)-pyridine-2,6-diylbis(methylidynenitrilo)]bis[pyrimidine-2,4(1H,3H)-dione]}zinc(II) nitrate hexafluorophosphate trihydrate.

The title compound, [Zn(C(15)H(11)N(7)O(4))(H(2)O)(2)](NO(3))(PF(6)).3H(2)O, contains a mononuclear zinc(II) complex. The Zn(2+) centre is seven-coordinated in a slightly distorted pentagonal-bipyramidal geometry, with the two water O atoms located in the apical positions, and the pyridine N atom, the two imine N atoms and two carbonyl O atoms of the uracil groups located in the equatorial plane.