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Title 

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

Authors 

Jin-Oh BaekJeong-Woo SeoOh Suk KwonS I SeongI H KimChul Ho Kim

Publisher 

Wiley-Blackwell

Issue Date 

2011

Citation 

Journal of Basic Microbiology, vol. 51, no. 2, pp. 129-135

Keywords 

Amino acid deaminaseFerric chloridePhenyllactic acidPhenylpyruvic acidProteus mirabilis

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 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.

ISSN 

0233-111X

Link 

http://dx.doi.org/10.1002/jobm.201000086

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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