Journal article

ASPARTATE-AMINOTRANSFERASE - INVESTIGATION OF THE ACTIVE-SITES

TL NERO, MG WONG, SW OLIVER, MN ISKANDER, PR ANDREWS

JOURNAL OF MOLECULAR GRAPHICS | BUTTERWORTH-HEINEMANN | Published : 1990

Abstract

An investigation of the crystal structure of cytosolic pig-heart aspartate aminotransferase (AAT, E.C.2.6.1.1) was carried out to determine the structural requirements for ligand recognition by the active site. Structural differences were observed between the two active sites of the AAT dimer. The natural ligand, L-aspartate, was docked into both active sites using various methods. However, due to structural differences, the ligand was able to form all the necessary interactions for initial binding in only one of the active sites. The program GRID (P.J. Goodford, J. Med. Chem. 1985, 28, 849-857) was used to predict favorable binding sites for the functional groups of the aspartate ligand. Th..

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