Insights into the Mechanistic Pathway of the Pantoea agglomerans Phenylalanine Aminomutase

摘要

The biosynthesis of the hybrid pep-tide-polyketide antibiotic andrimid in Pantoea agglomerans requires the function of a phenylalanine amino-mutase, AdmH (designated PaPAM), which converts (S)-α-phe-nylalanine to (S)-β-phenylala-nine. PaPAM is a member of the class I lyase-like family that includes phenylalanine and tyrosine amino-mutases (PAMs and TAMs, respectively), phenylalanine ammonia lyases (PALs), tyrosine ammonia lyases (TALs), and histidine ammonia lyases (HALs). PALs, TALs, and HALs produce aryl acryl-ates from the corresponding amino-acid substrate by the elimination of ammonia.