Expression and characterization of a second L-amino acid deaminase isolated from Proteus mirabilis in Escherichia coli
- Authors
- Baek, Jin-Oh; Seo, Jeong-Woo; Kwon, Ohsuk; Seong, Su-Il; Kim, Ik-Hwan; Kim, Chul Ho
- Issue Date
- 4월-2011
- Publisher
- WILEY-BLACKWELL
- Keywords
- Proteus mirabilis; Amino acid deaminase; Phenylpyruvic acid; Phenyllactic acid; Ferric chloride
- Citation
- JOURNAL OF BASIC MICROBIOLOGY, v.51, no.2, pp.129 - 135
- Indexed
- SCIE
SCOPUS
- Journal Title
- JOURNAL OF BASIC MICROBIOLOGY
- Volume
- 51
- Number
- 2
- Start Page
- 129
- End Page
- 135
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/112747
- DOI
- 10.1002/jobm.201000086
- ISSN
- 0233-111X
- Abstract
- 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 V(max) and K(m) values of Pm1 were 119.7 (mu g phenylpyruvic acid/mg/min) and 31.55 mM phenylalanine, respectively, values lower than those of Pma. The Pm1 deaminase will be very useful industrially in the preparation of commercially valuable materials including urocanic acid and a-oxoglutarate.
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