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Transfer RNA-Dependent Aminolevulinic Acid Formation: Structure and Function Of Glutamyl-tRNA Synthetase, Reductase and Glutamate-1-Semialdehyde-2,1-Aminomutase

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Chlorophylls and Bacteriochlorophylls

Part of the book series: Advances in Photosynthesis and Respiration ((AIPH,volume 25))

Abstract

In plants, green algae, archaea and in most bacteria the common precursor of all tetrapyrroles, 5-aminolevulinic acid, is formed by three enzymes. The initial substrate glutamate is converted to glutamyl-tRNA by glutamyltRNA synthetase for use in both protein and tetrapyrrole biosynthesis. During the first committed step an NADPH-dependent glutamyl-tRNA reductase reduces glutamyl-tRNA to form glutamate-1-semialdehyde, which is subsequently transaminated by glutamate-1-semialdehyde-2,1-aminomutase to yield 5-aminolevulinic acid. The enzymatic mechanisms deduced from biochemical investigations and recently solved crystal structures are described for all three enzymes. A potential pathway for metabolic channeling of the reactive aldehyde between glutamyl-tRNA reductase and the aminomutase is outlined.

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Authors and Affiliations

  1. Department of Structural Biology, German Research Center for Biotechnology, Mascheroder Weg 1, D-38104, Braunschweig, Germany

    Wolf-Dieter Schubert & Dirk W. Heinz

  2. Institute of Microbiology, Technical University Braunschweig, Spielmannstrasse 7, D-38106, Braunschweig, Germany

    Dieter Jahn & Jürgen Moser

Authors
  1. Dieter Jahn
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  2. Jürgen Moser
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  3. Wolf-Dieter Schubert
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  4. Dirk W. Heinz
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Editors and Affiliations

  1. Humboldt University, Berlin, Germany

    Bernhard Grimm

  2. CSIRO Plant Industry, Canberra, Australia

    Robert J. Porra

  3. Ludwig-Maximilians-Universität München, Germany

    Wolfhart Rüdiger

  4. Ludwig-Maximilians-Universität München, Germany

    Hugo Scheer

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Jahn, D., Moser, J., Schubert, WD., Heinz, D.W. (2006). Transfer RNA-Dependent Aminolevulinic Acid Formation: Structure and Function Of Glutamyl-tRNA Synthetase, Reductase and Glutamate-1-Semialdehyde-2,1-Aminomutase. In: Grimm, B., Porra, R.J., Rüdiger, W., Scheer, H. (eds) Chlorophylls and Bacteriochlorophylls. Advances in Photosynthesis and Respiration, vol 25. Springer, Dordrecht. https://doi.org/10.1007/1-4020-4516-6_12

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