Document Detail

Expression and characterization of a second L-amino acid deaminase isolated from Proteus mirabilis in Escherichia coli.
MedLine Citation:
PMID:  21298676     Owner:  NLM     Status:  Publisher    
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 (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. (© 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim).
Jin-Oh Baek; Jeong-Woo Seo; Ohsuk Kwon; Su-Il Seong; Ik-Hwan Kim; Chul Ho Kim
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-2-7
Journal Detail:
Title:  Journal of basic microbiology     Volume:  -     ISSN:  1521-4028     ISO Abbreviation:  -     Publication Date:  2011 Feb 
Date Detail:
Created Date:  2011-2-7     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8503885     Medline TA:  J Basic Microbiol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Microbe-based Fusion Technology Research Center, Jeonbuk Branch Institute, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Jeongeup, Jeonbuk, South Korea; School of Life sciences and Biotechnology, Korea University, Seoul, South Korea.
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