Purification and some properties of aspartate aminotransferase of Amycolatopsis methanolica
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Published:1994-07-01
Issue:7
Volume:40
Page:601-604
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ISSN:0008-4166
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Container-title:Canadian Journal of Microbiology
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language:en
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Short-container-title:Can. J. Microbiol.
Abstract
Aspartate aminotransferase (EC 2.6.1.1) from Amycolatopsis methanolica was purified and characterized. It is a dimeric protein with an overall molecular weight of approximately 90 000 with maximal activity at 70 °C and at pH 8.5. The enzyme was specific for L-aspartate as amino donor and 2-ketoglutarate as amino acceptor: the Km values for L-aspartate and 2-ketoglutarate were 1.27 and 0.38 mM, respectively.Key words: Amycolatopsis methanolica, aspartate aminotransferase, L-aspartate, 2-ketoglutarate.
Publisher
Canadian Science Publishing
Subject
Genetics,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Immunology,Microbiology
Cited by
1 articles.
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