Exploring the Active Site of Amine:Pyruvate Aminotransferase on the Basis of the Substrate Structure−Reactivity Relationship:  How the Enzyme Controls Substrate Specificity and Stereoselectivity

Author:

Shin Jong-Shik1,Kim Byung-Gee1

Affiliation:

1. School of Chemical Engineering and Institute for Molecular Biology and Genetics, Seoul National University, Seoul, Korea

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry

Reference14 articles.

1. Enzymatic Reactions in Organic Media

2. Christen, P.; Metzler, D. E.Transaminases; John Wiley & Sons:  New York, 1985.

3. Ueno, H.; Kagamiyama, H.Molecular Aspects of Enzyme Catalysis; Kodansha Ltd.  Tokyo, 1994; pp 87−106. Malashkevich, V. N.; Strokopytov, B. V.; Borisov, V. V.; Dauter, Z.; Wilson, K. S., Torchinsky, Y. M.J. Mol. Biol.1995,247, 111−124. Kuramitsu, S.; Hiromi, K.; Hayashi, H.; Morino, Y.; Kagamiyama, H.Biochemistry1990,29, 5469−5476. Nobe, Y.; Kawaguchi, S.; Ura, H.; Nakai, T.; Hirotsu, K.; Kato, R.; Kuramitsu, S.J. Biol. Chem.1998,273, 29554−29564.

4. The Active Site of Paracoccus denitrificans Aromatic Amino Acid Aminotransferase Has Contrary Properties:  Flexibility and Rigidity,

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