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Biosynthesis of 5-Aminolevulinic Acid

  • Chapter
Tetrapyrroles

Part of the book series: Molecular Biology Intelligence Unit ((MBIU))

Abstract

5-Aminolevulinic acid (ALA) is the general precursor of all known tetrapyrroles. Currently, two different biosynthetic routes for ALA formation are known. Humans, animals, fungi and the α-group of the proteobacteria employ the one-step-condensation of succinyl-coenzyme A and glycine catalyzed by pyridoxal 5′-phosphate-dependent ALA synthase. In plants, algae, archaea and all other bacteria ALA is formed by two enzymes. The initial substrate glutamyl-tRNA is synthesized by glutamyl-tRNA synthetase and supplied both to protein and to tetrapyrrole biosynthesis. During the first committed step of ALA synthesis a NADPH-dependent glutamyl-tRNA reductase reduces glutamyl-tRNA to form glutamate-1-semialdehyde. The aldehyde is subsequendy transaminated by glutamate-1-semialdehyde-2,1-aminomutase to yield ALA. Evidence for metabolic channeling of the reactive aldehyde between glutamyl-tRNA reductase and the aminomutase is outlined based on the structures of both enzymes. The enzymatic mechanisms deduced from biochemical investigations and recently solved crystal structures are described for all participating enzymes.

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Authors and Affiliations

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

    Dieter Jahn

  2. Department of Structural Biology, German Research Center for Biotechnology, Braunschweig, Germany

    Dirk W. Heinz

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  1. Dieter Jahn
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  2. Dirk W. Heinz
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Correspondence to Dieter Jahn .

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Jahn, D., Heinz, D.W. (2009). Biosynthesis of 5-Aminolevulinic Acid. In: Tetrapyrroles. Molecular Biology Intelligence Unit. Springer, New York, NY. https://doi.org/10.1007/978-0-387-78518-9_2

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