Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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A Stereochemical Aspect of Pyridoxal 5' -Phosphate Dependent Enzyme Reactions and Molecular Evolution

  • Jhee, Kwang-Hwan (Laboratory of Biochemistry, and Genetics, NIDDK, National Institute of Health) ;
  • Tohru, Yoshimura (Laboratory of Biofunctional Molecules, Institute for Chemical Research, Kyoto University) ;
  • Yoichi, Kurokawa (Laboratory of Biofunctional Molecules, Institute for Chemical Research, Kyoto University) ;
  • Nobuyoshi, Esaki (Laboratory of Biofunctional Molecules, Institute for Chemical Research, Kyoto University) ;
  • Kenji, Soda (Department of Biotechnology, Faculty of Engineering, Kansai University)
  • Published : 1999.12.01
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Abstract

We have studied the stereospecificities of various pyridoxal 5'-phosphate (PLP) dependent enzymes for the hydrogen transfer between the C-4' of a bound coenzyme and the C-2 of a substrate in the transamination catalyzed by the enzymes. Stereospecificities reflect the structures of enzyme active-sites, in particular the geometrical relationship between the coenzyme-substrate Schiff base and the active site base participating in an $\alpha$-hydrogen abstraction. The PLP enzymes studied so far catalyze only a si-face specific (pro-S) hydrogen transfer. This stereochemical finding suggests that the PLP enzymes have the same topological active-site structures, and that the PLP enzymes have evolved divergently from a common ancestral protein. However, we found that o-amino acid aminotransferase, branched chain L-amino acid aminotransferase, and 4-amino-4-deoxychorismate lyase, which have significant sequence homology with one another, catalyze a re-face specific (pro-R) hydrogen transfer. We also showed that PLP-dependent amino acid racemases, which have no sequence homology with any aminotransferases, catalyze a non-stereospecific hydrogen transfer: the hydrogen transfer occurs on both faces of the planar intermediate. Crystallographical studies have shown that the catalytic base is situated on the re-face of the C-4' of the bound coenzyme in o-amino acid aminotransferase and branched chain L-amino acid aminotransferase, whereas the catalytic base is situated on the si-face in other aminotransferases (such as L-aspartate aminotransferase) catalyzing the si-face hydrogen transfer. Thus, we have clarified the stereospecificities of PLP enzymes in relation with the primary structures and three-dimensional structures of the enzymes. The characteristic stereospecificities of these enzymes for the hydrogen transfer suggest the convergent evolution of PLP enzymes.

Keywords

References

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