Fig. 3: Identification of Val79 as a target for enhancing the substrate scope of ThAOS. | Communications Chemistry

Fig. 3: Identification of Val79 as a target for enhancing the substrate scope of ThAOS.

From: Rational engineering of a thermostable α-oxoamine synthase biocatalyst expands the substrate scope and synthetic applicability

Fig. 3

A Interaction between Val79 and the “sidechain” proton of a Gly substrate in an overlay of the crystal structure of the PLP-bound form of ThAOS (PDB: 7POA) with the PLP:Gly external aldimine form of R. capsulatus ALAS (PDB: 2BWP). The V79 sidechain of the opposite monomer is predicted to be in relatively close proximity (3.5 Å) to the C-α of the amino acid. B A sequence and structural alignment of various AOS biocatalysts highlighting the residues equivalent to position V79 of ThAOS. The KBL enzyme from E. coli (PDB: 1FC4) retains the valine residue whereas the AONS enzyme from E. coli and SPT enzyme from S. paucimobilis (PDB: 2JG2) have a serine side chain. An Alb29 enzyme from S. albogriseolus (PDB: 8XHA) has a leucine and the ALAS enzyme from R. capsulatus has a threonine at this equivalent position (PDB: 2BWP). The full alignment is in Fig. S23.

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