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Characterization of Recombinant L-Amino Acid Deaminase of Proteus mirabilis

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Advances in Applied Biotechnology

Part of the book series: Lecture Notes in Electrical Engineering ((LNEE,volume 332))

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Abstract

L-amino acid deaminases catalyze the deamination of L-amino acids. Up until now, two types of L-amino acid deaminase have been identified in Proteus species. To investigate enzymatic characteristics of L-amino acid deaminase from Proteus mirabilis, L-amino acid deaminase encoding gene (pmta) was cloned from P. mirabilis T-1. Prokaryotic expression system was established to express recombinant Pmta. Enzymatic characteristics of the enzymes were analyzed. Results showed that recombinant Pmta exhibited function of second type of L-amino acid deaminase. The Km and Vmax value of Pmta for histidine was 10.57 mmol/L and 202.06 μmol/min/mg, respectively. The optimal temperature and pH of recombinant Pmta was 40 °C and 7.0. The enzymatic characteristics of Pmta were different from those of Pm1 discovered in P. mirabilis KCTC, which was probably due to different amino acid sequences. The Pmta deaminase will be very useful in the preparation of commercially valuable materials including urocanic acid and 3-mercaptopyruvic acid.

An erratum of this chapter can be found under DOI 10.1007/978-3-662-45657-6_66

An erratum to this chapter can be found at http://dx.doi.org/10.1007/978-3-662-45657-6_66

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Acknowledgments

This work was supported by the National High Technology Research and Development Program (No. 2013AA102106), by the Program for Changjiang Scholars and Innovative Research Team in University (No. IRT1166) and by the Tianjin Municipal Education Commission (No. 20120630).

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Authors and Affiliations

  1. College of Biotechnology, Tianjin University of Science and Technology, Tianjin, 300457, China

    Chenglin Zhang, Jia Feng, Xixian Xie, Qingyang Xu & Ning Chen

  2. National and Local United Engineering, Lab of Metabolic Control Fermentation Technology, Tianjin, 300457, China

    Chenglin Zhang, Xixian Xie, Qingyang Xu & Ning Chen

Authors
  1. Chenglin Zhang
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  2. Jia Feng
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  3. Xixian Xie
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  4. Qingyang Xu
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  5. Ning Chen
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Corresponding author

Correspondence to Ning Chen .

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Editors and Affiliations

  1. Tianjin University of Science and Technology, Tianjin, China

    Tong-Cun Zhang

  2. SBI ALApromo, Tokyo, Japan

    Motowo Nakajima

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Zhang, C., Feng, J., Xie, X., Xu, Q., Chen, N. (2015). Characterization of Recombinant L-Amino Acid Deaminase of Proteus mirabilis . In: Zhang, TC., Nakajima, M. (eds) Advances in Applied Biotechnology. Lecture Notes in Electrical Engineering, vol 332. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-45657-6_61

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