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Examining electrostatic preorganization in monoamine oxidases A and B by structural comparison and pKa calculations (CROSBI ID 206348)

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Repič, Matej ; Purg, Miha ; Vianello, Robert ; Mavri, Janez Examining electrostatic preorganization in monoamine oxidases A and B by structural comparison and pKa calculations // The journal of physical chemistry. B, Condensed matter, materials, surfaces, interfaces & biophysical, 118 (2014), 16; 4326-4332. doi: 10.1021/jp500795p

Podaci o odgovornosti

Repič, Matej ; Purg, Miha ; Vianello, Robert ; Mavri, Janez

engleski

Examining electrostatic preorganization in monoamine oxidases A and B by structural comparison and pKa calculations

Monoamine oxidases (MAO) A and B are important flavoenzymes involved in the metabolism of amine neurotransmitters. Orru et al. ( J. Neural Transm. 2013, 120, 847−851) recently presented experimental results that have challenged the prevailing assumption that MAO A and MAO B employ an identical catalytic mechanism. We compared the spatial configuration of ionizable groups in both isozymes and estimated the time-averaged electrostatic potential by calculating the pKa values of five active site residues. Superimposition of both experimental structures shows very close overlap and the RMSD in placements of ionizable groups within 16 Å of the reaction center is only 0.847 Å. This similarity is also reflected in the calculated pKa values, where the largest difference between the MAO A and MAO B pKa values was found for residues Tyr188 in MAO B and the corresponding Tyr197 in MAO A assuming 1.23 units. The pKa values for the other four studied residues differ by less than 0.75 units. The results show that the electrostatic preorganizations in both active sites are very similar, supporting the idea that both enzymes work by the same mechanism.

monoamine oxidase

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Podaci o izdanju

118 (16)

2014.

4326-4332

objavljeno

1520-6106

10.1021/jp500795p

Povezanost rada

Kemija

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