Premium
Site‐Directed Mutagenesis of Tyr354 in Geobacillus stearothermophilus Alanine Racemase Identifies a Role in Controlling Substrate Specificity and a Possible Role in the Evolution of Antibiotic Resistance
Author(s) -
Patrick Wayne M.,
Weisner Jan,
Blackburn Jonathan M.
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20020802)3:8<789::aid-cbic789>3.0.co;2-d
Subject(s) - mutagenesis , geobacillus stearothermophilus , saturated mutagenesis , site directed mutagenesis , serine , asparagine , directed mutagenesis , biochemistry , alanine , biology , substrate specificity , directed evolution , alanine scanning , chemistry , mutation , stereochemistry , enzyme , amino acid , mutant , thermophile , gene
Mechanism of alanine racemase specificity resolved: Site‐directed mutagenesis has identified active site residue Tyr354 as a critical determinant of substrate specificity in the Geobacillus stearothermophilus alanine racemase, despite the fact it plays no direct role in catalysis. Mutation to asparagine imparts significant serine racemisation activity, which suggests that this was an important step in the evolution of serine racemases such as VanT, required for vancomycin resistance in Enterococcus gallinarum.