Structure and function of glutamyl-tRNA reductase involved in 5-aminolaevulinic acid formation.
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.
Institute of Microbiology, Technical University Braunschweig, Spielmannstrasse 7, D-38106 Braunschweig, Germany.
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Moser
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Schubert
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Heinz
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Jahn
D000445:Aldehyde Oxidoreductases / Q000737:chemistry* / Q000378:metabolism*; D000622:Aminolevulinic Acid / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology*; D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D019281:Dimerization; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D011994:Recombinant Proteins; D000622:Aminolevulinic Acid; D000445:Aldehyde Oxidoreductases; C067282:glutamyl tRNA reductase