Summary
Four aromatic amino acid aminotransferases were identified in A. lipoferum ATCC 29708. Each enzyme can in vitro catalyze the transamination of tryptophan, which is the initial reaction in the biosynthesis of IAA via the transamination pathway. Evidence is presented that one of these enzymes is induced in cells that are grown to stationary phase in the presence of tryptophan. This may indicate that this enzyme is the real aminotransferase of the transamination pathway in vivo. A strategy to clone the genes of these enzymes is described.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Hartmann, A., Singh, M. and Klingmüller, W. (1983). Can. J. Microbiol. 29, 916–923
Gelfand, D.H. and Steinberg, R. (1977). J. Bact. 130, 429–440
Lin, E.C.C., Pitt, B.M., Civen, M. and Knox, W.E. (1958). J. Biol. Chem. 233, 668–673
Whitaker, R.J., Gaines, Ch.G. and Jensen, R.A. (1982). J. Biol. Chem. 257, 13550–13556
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1988 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Ruckdäschel, E., Kittell, B.L., Helinski, D.R., Klingmüller, U. (1988). Aromatic Amino Acid Aminotransferases of Azospirillum Lipoferum and Their Possible Involvement in IAA Biosynthesis. In: Klingmüller, W. (eds) Azospirillum IV. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-73072-6_7
Download citation
DOI: https://doi.org/10.1007/978-3-642-73072-6_7
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-73074-0
Online ISBN: 978-3-642-73072-6
eBook Packages: Springer Book Archive