| Literature DB >> 20064614 |
Lu-Sheng Hsieh1, Chuan-Shan Yeh, Hung-Chi Pan, Chieh-Yang Cheng, Chien-Chih Yang, Ping-Du Lee.
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 2142bp 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 80kDa and existed as a homotetramer. The optimum temperature and pH of BoPAL2 were 50-60 degrees C and 8.5-9.0, respectively. The K(m) and k(cat) values of BoPAL2 expressed in E. coli were 250microM and 10.12s(-1). The K(m) and k(cat) values of BoPAL2 expressed in P. pastoris were 331microM and 16.04s(-1). The recombinant proteins had similar biochemical properties and kinetic parameters with PALs reported in other plants.Entities:
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Year: 2010 PMID： 20064614 DOI： 10.1016/j.pep.2010.01.009
Source DB: PubMed Journal: Protein Expr Purif ISSN： 1046-5928 Impact factor: 1.650