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

ABSTRACT: Bacillus licheniformis l-arabinose isomerase (l-AI) is distinguished from other l-AIs by its high degree of substrate specificity for l-arabinose and its high turnover rate. 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 screened residues, was used to study the molecular determinants for the catalytic efficiency of B. licheniformis l-AI. One conserved amino acid, Y333, in the substrate binding pocket of the wild-type B. licheniformis l-AI was identified as an important residue affecting the catalytic efficiency of B. licheniformis l-AI. Further insights into the function of residue Y333 were obtained by replacing it with other aromatic, nonpolar

SUBMITTER: Prabhu P 

PROVIDER: S-EPMC2832401 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature