Aspartate aminotransferase AspAT

Fig. 8.10 X-ray crystal structure of an aspartate aminotransferase (AspAT) bound to its cofactor pyridoxal 5 -phosphate and aspartate. Directed evolution techniques produced changes in ligand specificity due to substitution of the disparate positions indicated. Coordinates from lART [25].

ASPARTATE AMINOTRANSFERASE (AspAT, ASAT, AST) (SERUM GLUTAMATE-OXALOACETATE TRANSAMINASE, SCOT, GLUTAMATE-OXALOACETATE TRANSAMINASE, GOT)... 

Numerous groups have described the use of d-AAO in a variety of combinations with other agents and in a variety of processes. Cheng and Wu, in the context of a biotransformation of DL-aspartic acid to L-alanine, in which the key reaction works only with L-Asp, removed residual D-Asp with d-AAO and converted the resulting oxaloacetate into L-Asp by including L-aspartate aminotransferase (r-AspAT) in the reaction mixture (Scheme 1). 

Fig. 1.2 Comparison of sequences of aspartate aminotransferases from different species. The residues are numbered according to the sequence of pig cAspAT.13 Possible deletions introduced into the sequences are indicated by hyphens. Residues that are invariant in pig c- and m-AspAT s are boxed, those that are invariant in pig AspAT s and coli AspAT are indicated as bold letters, and those that are directly interacting with substrate or coenzyme are marked as. ...

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