Probing the molecular determinant for the catalytic efficiency of L-arabinose isomerase from Bacillus licheniformis

A systematic strategy that included a sequence alignment-based first screening of residues and a homology model-based second screening, followed by site-directed mutagenesis to alter individual residues was used to study the molecular determinants for the catalytic efficiency of Bacillus licheniformis L-arabinose isomerase (L-AI). The data obtained and molecular dynamics simulations indicated that one of the conserved amino acid, Y333, in the substrate binding pocket of the wild-type B. lichenifromis L-AI is involved in the catalytic efficiency of B. licheniformis L-AL.