Summary
Lys258 of E. coli aspartate aminotransferase was replaced by Arg by site-directed mutagenesis. The activity of mutant enzyme was 2–3% that of the wild enzyme. A catalytic significance of the positive charge provided by Arg258 was also discussed.
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References
Arnone, A, Christen, P, Jansonius, J.N., & Metzler,D.E. (1985) In: Transaminases (Christen, P. & Metzler, D. E. ) pp. 326–362.
Malcolm,B.A., & Kirsch,J.F. (1985) Biochem. Biophys. Res. Commun. 132, 915–921.
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© 1987 Birkhäuser Verlag Basel
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Kagamiyama, H., Kuramitsu, S., Inoue, Y., Tanase, S., Morino, Y. (1987). Mutation of Lysine 258 to Arginine in the Active Site of Aspartate Aminotransferase. In: Korpela, T.K., Christen, P. (eds) Biochemistry of Vitamin B6 . Birkhäuser Congress Reports. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-9308-4_13
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DOI: https://doi.org/10.1007/978-3-0348-9308-4_13
Publisher Name: Birkhäuser, Basel
Print ISBN: 978-3-0348-9989-5
Online ISBN: 978-3-0348-9308-4
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