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Fig. 1 | AMB Express

Fig. 1

From: Biochemical characteristics and potential application of a thermostable starch branching enzyme from Bacillus licheniformis

Fig. 1

Multiple alignment and homology modeling analysis of bl-GBE a 3D structural model of bl-GBE protein was generated using AlphaFold. Glu352 (a nucleophile), Asp309, and Asp420 (acid/base catalyst) are the three catalytic residues conserved in members of the GH13 family. The position of the 3 domains is shown in different colors; yellow: the N-terminal domain, blue: catalytic domain A, and green: the C-terminal domain, b Sequence alignment of GBEs. Conserved residues are designated with red squares and white lettering, and similar residues are designated with red lettering. GBE amino acid sequences from different sources are aligned. GBEs in black box has been commercialized. The secondary structure is derived from the predicated structure of bl-GBE (AlphaFold). The highly conserved catalytic residues are indicated with red stars. The four highly conservative motifs (CRS) are in the blue triangle

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