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Addendum

N-terminal engineering of glutamyl-tRNA reductase with positive charge arginine to increase 5-aminolevulinic acid biosynthesis

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Pages 424-427 | Received 19 Jul 2016, Accepted 24 Aug 2016, Published online: 18 Oct 2016

Figures & data

Figure 1. The model complex of GluTR and GSA-AT. The V-shaped dimer protein is GluTR while the other dimer is GSA-AT.

Figure 1. The model complex of GluTR and GSA-AT. The V-shaped dimer protein is GluTR while the other dimer is GSA-AT.

Figure 2. The illustration of GluTR variants with insertion of different numbers of lysine residues (A) and arginine residues (B). WT represented the wild-type GluTR.

Figure 2. The illustration of GluTR variants with insertion of different numbers of lysine residues (A) and arginine residues (B). WT represented the wild-type GluTR.

Figure 3. ALA production of the variants with inserting different lysine residues (A) and arginine residues (B).

Figure 3. ALA production of the variants with inserting different lysine residues (A) and arginine residues (B).

Figure 4. Structural analysis of N-terminal domain of GluTR. (A) Wild-type GluTR; (B) the variant GluTR K2 with insertion of 2 lysine residues; (C) the variant GluTR R1 with insertion of one arginine residue. The green dotted lines indicate the hydrogen bonds.

Figure 4. Structural analysis of N-terminal domain of GluTR. (A) Wild-type GluTR; (B) the variant GluTR K2 with insertion of 2 lysine residues; (C) the variant GluTR R1 with insertion of one arginine residue. The green dotted lines indicate the hydrogen bonds.

Figure 5. SDS-PAGE analysis of the GluTR variants with insertion of arginine residues.

Figure 5. SDS-PAGE analysis of the GluTR variants with insertion of arginine residues.

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