Abstract
L-Glutamate-1-semialdehyde was synthesized by catalytic hydrogenation of N-carbobenzoxy-L-glutamyl-1-chloride-5-benzyl ester. Soluble protein extracts of chloroplasts isolated from greening barley leaves enzymically converted L-glutamate-1-semialdehyde to δ-aminolevulinate. The enzyme was partially purified by gel filtration on a Biogel column excluding proteins larger than 500,000 daltons. The enzyme had a broad pH optimum around 8.0 and required no specific cofactors for activity. Aminooxyacetate (20mM), cycloserine (20mM), ρ-chloromercuribenzoate (0.1mM), glyoxylate (20mM) and pyridoxal phosphate (5mM) inhibited δ-aminolevulinate formation from L-glutamate-1-semialdehyde. However, β- hydroxyglutamate (1mM) a potent inhibitor of L-glutamate-U-14C conversion to δ-aminolevulinate, had no effect on L-glutamate-1-semialdehyde aminotransferase. The aminotransferase activity was eluted from the Biogel column together with the enzyme activity that converted L-glutamate-U-14C into δ-aminolevulinate. Soluble proteins prepared from etiolated plastids and mature chloroplasts of barley had a low specific activity of L-glutamate-1-semialdehyde aminotransferase compared to soluble proteins from greening plastids. It is proposed that L-glutamate-1-semialdehyde aminotransferase catalyses a part reaction in the conversion of L-glutamate to δ-aminolevulinate in greening barley plastids.
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Gamini Kannangara, C., Gough, S.P. Biosynthesis of Δ-aminolevulinate in greening barley leaves: Glutamate 1-semialdehyde aminotransferase. Carlsberg Res. Commun. 43, 185–194 (1978). https://doi.org/10.1007/BF02914241
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DOI: https://doi.org/10.1007/BF02914241