aMolecular Bioprocess Research Center, Jeonbuk Branch Institute, KRIBB, Daejeon 580-185, Korea;bSchool of Life sciences and Biotechnology, Korea University, Seoul 136-701, Korea;cR & D center, Biotopia Co., Ltd., Gyeonggi 456-853, Korea
Abstract:
We expressed an L-amino acid deaminase (Pma) from Proteus mirabilis (P. mirabilis) in Escherichia coli and characterized the kinetics of phenylpyruvic acid production. P. mirabilis Pma was well expressed in E. coli in an active state and was found to be associated with membranes. The association of Pma with cellular membranes is likely to be necessary for its enzymatic activity.