Abstract
Phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) is the first committed enzyme of phenylpropanoid pathway. A PAL gene, designated as BoPAL2, was cloned from a Bambusa oldhamii cDNA library. The open reading frame of BoPAL2 was 2142 bp in size encoding a 713-amino acid polypeptide. BoPAL2 was heterologous expressed in Escherichia coli and Pichia pastoris. The recombinant proteins were exhibited PAL and tyrosine ammonia-lyase activities. The recombinant BoPAL2 had a subunit mass of 80 kDa and existed as a homotetramer. The optimum temperature and pH of BoPAL2 were 50–60 °C and 8.5–9.0, respectively. The K m and k cat values of BoPAL2 expressed in E. coli were 250 μM and 10.12 s −1. The K m and k cat values of BoPAL2 expressed in P. pastoris were 331 μM and 16.04 s −1. The recombinant proteins had similar biochemical properties and kinetic parameters with PALs reported in other plants.
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