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Dual substrate recognition in alanine aminotransferases: Catalytic pocket for dicarboxylic acid substrates.

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posted on 11.07.2014, 02:53 by Esther Peña-Soler, Francisco J. Fernandez, Miguel López-Estepa, Fernando Garces, Andrew J. Richardson, Juan F. Quintana, Kenneth E. Rudd, Miquel Coll, M. Cristina Vega

Schematic representation of the active site of AlaA in complex with acetate (A) and of T. termophilus α-aminoadipate transaminase LysN (PDB 2zyj) (B, orange) and A. thaliana LL-aminopimelate aminotransferase (PDB 3ei5) (B, blue) crystallized in complex with the glutamate external aldimine of PLP (PGU). AlaA residues Tyr15, Arg18 and Tyr129 (shadowed) are equivalent to residues known to stabilize the γ-carboxylate moiety of PGU, including Arg23 in α-aminoadipate transaminase and Tyr37 and Tyr152 in LL-aminopimelate aminotransferase.

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