| Expression and characterization of a second L-amino acid deaminase isolated from Proteus mirabilis in Escherichia coli. | |
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MedLine Citation:
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PMID: 21298676 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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). |
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Authors:
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Jin-Oh Baek; Jeong-Woo Seo; Ohsuk Kwon; Su-Il Seong; Ik-Hwan Kim; Chul Ho Kim |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-2-7 |
Journal Detail:
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Title: Journal of basic microbiology Volume: - ISSN: 1521-4028 ISO Abbreviation: - Publication Date: 2011 Feb |
Date Detail:
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Created Date: 2011-2-7 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8503885 Medline TA: J Basic Microbiol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. |
Affiliation:
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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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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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