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Conformation of threo-alpha-cycloglutamic acid and pyridoxal-5'-phosphate aldimine in the active site of aspartate aminotransferase

Tumanian, V.G.; Shliapnikov, S.V.; Severin, E.S.

Molekuliarnaia Biologiia 14(3): 632-639

1980

ISSN/ISBN: 0026-8984
PMID: 7402205
Document Number: 156872
The theoretical conformational analysis of the pyridoxal-5'-phosphate aldimine complex with a substrate analogue--threo-alpha-cycloglutamic acid has been carried out. The calculation method used takes into account the possibility of hydrogen bonding between a carboxyl group of the substrate and the phosphate moiety of the cofactor. The conformational properties and geometrical parameters of the lowest energy structures are discussed. It is shown that of the three conformations permitted for the productive enzyme--substrate complex formations only one is electrostatically favourable.

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