| Literature DB >> 12196141 |
J Moser1, W-D Schubert, D W Heinz, D Jahn.
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.Entities:
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Year: 2002 PMID： 12196141 DOI： 10.1042/bst0300579
Source DB: PubMed Journal: Biochem Soc Trans ISSN： 0300-5127 Impact factor: 5.407