Structure-inhibition relationships in the interaction of butyrylcholinesterase with bambuterol, haloxon and their leaving groups (CROSBI ID 739875)
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Podaci o odgovornosti
Šinko, Goran ; Bosak, Anita ; Kovarik, Zrinka ; Simeon-Rudolf, Vera
engleski
Structure-inhibition relationships in the interaction of butyrylcholinesterase with bambuterol, haloxon and their leaving groups
Umjesto sažetka, dio iz uvoda: It was shown earlier that the inhibition by bambuterol (5-[2-(tert-butylamino)-1-hydroxyethyl]-m-phenylene-bis(dimethylcarbamate) hydrochloride) and haloxon (O, O-di-(2-chloroethyl)-O-(3-chloro-4-methylcoumarin-7-yl) phosphate) differentiate horse, human and mouse butyrylcholinesterase (BChE). The sequence alignment together with the three-dimensional BChE structure point out that three residues inside the active site at positions 69, 277 and 285 might be important for the differences in the inhibition of these three BChE species. We extended our study to the conformational analysis of bambuterol and haloxon, and their leaving groups, terbutaline (1-(3, 5-dihydroxyphenyl)-2-tert-butylaminoethanol sulphate) and CHM-coumarin (3-chloro-7-hydroxy-4-methylcoumarin). The relationship between molecular properties of inhibitors and inhibition constants is discussed.
butyrylcholinesterase; inhibition; carbamate; terbutaline; coumarin
Rad je prošireni sažetak (Extended abstract)
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Podaci o prilogu
421-423-x.
2005.
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objavljeno
Podaci o matičnoj publikaciji
Chemico-biological interactions
0009-2797
Podaci o skupu
Nepoznat skup
ostalo
29.02.1904-29.02.2096