Expression and characterization of a second L-amino acid deaminase isolated from Proteus mirabilis in Escherichia coli = Proteus mirabilis 유래 amino acid deaminase 효소의 특성 규명
Cited 34 time in
- Expression and characterization of a second L-amino acid deaminase isolated from Proteus mirabilis in Escherichia coli = Proteus mirabilis 유래 amino acid deaminase 효소의 특성 규명
- Jin-Oh Baek; Jeong-Woo Seo; Oh Suk Kwon; S I Seong; I H Kim; Chul Ho Kim
- Bibliographic Citation
- Journal of Basic Microbiology, vol. 51, no. 2, pp. 129-135
- Publication Year
- L-amino acid deaminases catalyze the deamination of natural L-amino acids. Two types of L-amino acid deaminase have been identified in Proteus species. One exhibits high levels of activity toward a wide range of aliphatic and aromatic L-amino acids, typically L-phenylalanine, whereas the other acts on a relatively narrow range of basic L-amino acids, typically L-histidine. In this study, we cloned, expressed, and characterized a second amino acid deaminase, termed Pm1, from P. mirabilis KCTC 2566. Homology alignment of the deduced amino acid sequence of Pm1 demonstrated that the greatest similarity (96%) was with the L-amino acid deaminase (LAD) of P. vulgaris, and that homology with Pma was relatively low (72%). Also, similar to LAD, Pm1 was most active on L-histidine, indicating that Pm1 belongs to the second type of amino acid deaminase. In agreement with this conclusion, the Vmax and Km values of Pm1 were 119.7 (μg phenylpyruvic acid/mg/min) and 31.55 mM phenylalanine, respectively, values lower than those of Pma. The Pml deaminase will be very useful industrially in the preparation of commercially valuable materials including urocanic acid and α -oxoglutarate.
- Amino acid deaminase; Ferric chloride; Phenyllactic acid; Phenylpyruvic acid; Proteus mirabilis
- Appears in Collections:
- Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
- Files in This Item:
Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.