PMID:11011151
| Citation |
Jhee, KH, Yoshimura, T, Miles, EW, Takeda, S, Miyahara, I, Hirotsu, K, Soda, K, Kawata, Y and Esaki, N (2000) Stereochemistry of the transamination reaction catalyzed by aminodeoxychorismate lyase from Escherichia coli: close relationship between fold type and stereochemistry. J. Biochem. 128:679-86 |
|---|---|
| Abstract |
Aminodeoxychorismate lyase is a pyridoxal 5'-phosphate-dependent enzyme that converts 4-aminodeoxychorismate to pyruvate and p-aminobenzoate, a precursor of folic acid in bacteria. The enzyme exhibits significant sequence similarity to two aminotransferases, D-amino acid aminotransferase and branched-chain L-amino acid aminotransferase. In the present study, we have found that aminodeoxychorismate lyase catalyzes the transamination between D-alanine and pyridoxal phosphate to produce pyruvate and pyridoxamine phosphate. L-Alanine and other D- and L-amino acids tested were inert as substrates of transamination. The pro-R hydrogen of C4' of pyridoxamine phosphate was stereospecifically abstracted during the reverse half transamination from pyridoxamine phosphate to pyruvate. Aminodeoxychorismate lyase is identical to D-amino acid aminotransferase and branched-chain L-amino acid aminotransferase in the stereospecificity of the hydrogen abstraction, and differs from all other pyridoxal enzymes that catalyze pro-S hydrogen transfer. Aminodeoxychorismate lyase is the first example of a lyase that catalyzes pro-R-specific hydrogen abstraction. The result is consistent with recent X-ray crystallographic findings showing that the topological relationships between the cofactor and the catalytic residue for hydrogen abstraction are conserved among aminodeoxychorismate lyase, D-amino acid aminotransferase and branched-chain L-amino acid aminotransferase [Nakai, T., Mizutani, H., Miyahara, I., Hirotsu, K., Takeda, S., Jhee, K.-H., Yoshimura, T., and Esaki, N. (2000) J. Biochem. 128, 29-38]. |
| Links | |
| Keywords |
Alanine/chemistry; Alanine/metabolism; Apoenzymes/chemistry; Apoenzymes/metabolism; Catalysis; Escherichia coli/enzymology; Escherichia coli/genetics; Evolution, Molecular; Hydrogen/metabolism; Kinetics; Molecular Conformation; Oxo-Acid-Lyases/chemistry; Oxo-Acid-Lyases/genetics; Oxo-Acid-Lyases/isolation & purification; Oxo-Acid-Lyases/metabolism; Protein Folding; Pyridoxal Phosphate/chemistry; Pyridoxal Phosphate/metabolism; Pyridoxamine/analogs & derivatives; Pyridoxamine/chemistry; Pyridoxamine/metabolism; Pyruvic Acid/chemistry; Pyruvic Acid/metabolism; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Spectrophotometry; Transaminases/chemistry; Transaminases/genetics; Transaminases/isolation & purification; Transaminases/metabolism; Tryptophan Synthase/metabolism; Tryptophanase/metabolism |
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