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. 2001 Dec 3;20(23):6583–6590. doi: 10.1093/emboj/20.23.6583

graphic file with name cde664f1.jpg

Fig. 1. Pathway of tRNA-dependent formation of 5-aminolevulinic acid (ALA) and structure of the substrate-like inhibitor glutamycin. (A) Glutamyl-tRNA reductase (GluTR) reduces tRNA-bound glutamate to glutamate-1-semialdehyde (GSA). Glutamate-1-semialdehyde aminomutase (GSAM) transaminates GSA to ALA. (B) The inhibitor glutamycin is an analog of the 3′-terminal nucleotide of acylated tRNAGlu.