Abstract
Abstract The Bambusa oldhamii phenylalanine ammonia-lyase (PAL) proteins, BoPAL1 and BoPAL2, exhibited different substrate specificities toward phenylalanine (Phe) and tyrosine (Tyr). Mutational analysis was conducted to study their substrate selectivity. All expressed wild-type and mutant BoPAL proteins manifested PAL activity; however, Km and kcat values were varied. BoPAL1 F133H and BoPAL2 F134H showed decreased kcat/Km values toward phenylalanine and significantly increased tyrosine ammonia-lyase (TAL) activities. BoPAL1 V197I and BoPAL2 I198 V showed opposite results regarding TAL activity, indicating that the Val or Ile residue prior to the active site, Ala-Ser-Gly, is essential for modulating Phe/Tyr substrate selectivity.
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