Biosynthesis of 5-Aminolevulinic Acid View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2009

AUTHORS

Dieter Jahn , Dirk W. Heinz

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. More... »

PAGES

29-42

Book

TITLE

Tetrapyrroles

ISBN

978-0-387-78517-2
978-0-387-78518-9

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-0-387-78518-9_2

DOI

http://dx.doi.org/10.1007/978-0-387-78518-9_2

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1044053118


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62 schema:description 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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