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Structure and function of glutamyl-tRNA reductase involved in 5-aminolaevulinic acid formation
J Moser1, W-D Schubert, D W Heinz
1Institute of Microbiology, Technical University Braunschweig, Spielmannstrasse 7, D-38106 Braunschweig, Germany.
Abstract:
In most bacteria, in archaea and in plants, the general precursor of all tetrapyrroles, 5-aminolaevulinic acid, is formed by two enzymes. The initial substrate, glutamyl-tRNA, is reduced by NADPH-dependent glutamyl-tRNA reductase to form glutamate 1-semialdehyde. The aldehyde is subsequently transaminated by glutamate-1-semialdehyde 2,1-aminomutase to yield 5-aminolaevulinic acid. The enzymic mechanism and the solved crystal structure of Methanopyrrus kandleri glutamyl-tRNA reductase are described. A pathway for metabolic channelling of the reactive aldehyde between glutamyl-tRNA reductase and the aminomutase is proposed.