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001-es BibID:	BIBFORM085848
Első szerző:	Gyémánt Gyöngyi (vegyész)
Cím:	Subsite mapping of the binding region of α?amylases with a computer program / Gyöngyi Gyémánt, György Hovánszki, Lili Kandra
Dátum:	2002
ISSN:	0014-2956 1432-1033
Megjegyzések:	A computer program has been evaluated for subsite map calculations of depolymerases. The program runs in WINDOWS and uses the experimentally determined bond cleavage frequencies (BCFs) for determination of the number of subsites, the position of the catalytic site and for calculation of subsite binding energies. The apparent free energy values were optimized by minimization of the differences of the measured and calculated BCF data. The program called SUMA (SUbsite Mapping of alpha-Amylases) is freely available for research and educational purposes via the Internet (E-mail: gyemant@tigris.klte.hu). The advantages of this program are demonstrated through alpha-amylases of different origin, e.g. porcine pancreatic alpha-amylase (PPA) studied in our laboratory, in addition to barley and rice alpha-amylases published in the literature. Results confirm the popular ♭five subsite model' for PPA with three glycone and two aglycone binding sites. Calculations for barley alpha-amylase justify the ♭6 + 2 + (1) model' prediction.The binding area of barleya-amylaseis composed ofsixglycone, twoaglyconebinding sites followedbyabarrier subsite at the reducingendof thebinding site.Calculations for rice alpha-amylase represent an entirely new map with a ♭(1) + 2 + 5 model', where ♭(1)' is a barrier subsite at the nonreducing end of the binding site and there are two glycone and five aglycone binding sites. The rice model may be reminiscent of the action of the bacterial maltogenic amylase, that is, suggesting an exo-mechanism for this enzyme.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk subsite mapping alpha-amylase action pattern WINDOWS program
Megjelenés:	European Journal of Biochemistry. - 269 : 21 (2002), p. 5157-5162. -
További szerzők:	Horánszki György Kandra Lili (1943-) (biokémikus)
Pályázati támogatás:	T032005 OTKA FKFP-0426/2000 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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