| ID | 44050 |
| FullText URL | |
| Title Alternative | Purification and Characterization of l-Methionine Decarboxylase from Streptomyces sp. 590
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| Author |
Maemura, Tomomi
Uchitomi, Kumiko
Kusaka, Chika
Soda, Kenji
Inagaki, Kenji
Kaken ID
researchmap
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| Abstract | L-Methionine decarboxylase [EC 4.1.1.57] catalyzes the decarboxylation of L-methionine and is a pyridoxal 5’-phosohate(PLP)-dependent enzyme. L-Methionine decarboxylase has been purified 630-fold by DEAE-Toyopearl 650M, Phenyl-Toyopearl 650M and Sephacryl S-300 column chromatographies from Streptomyces sp.590. The enzyme has a dimeric structure with identical subunits of Mr 60,000. This enzyme shows optimum activity at pH7.0 and 45°C, and is stable between pH5.7 and pH9.0. L-Methionine decarboxylase has antitumor activity against RERF-LC-AI and HeLa cells. Ten N-terminal amino acid sequence of L-methionine decarboxylase was determined, and the sequence showed no homology with other reported proteins.
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| Keywords | L-methionine decarboxylase
pyridoxal 5’-phosohate
Streptomyces
decarboxylation of L-methionine
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| Note | 原著論文
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| Published Date | 2011-02-01
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| Publication Title |
岡山大学農学部学術報告
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| Publication Title Alternative | Scientific Reports of the Faculty of Agriculture Okayama University
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| Volume | volume100
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| Publisher | 岡山大学農学部
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| Publisher Alternative | Faculty of Agriculture, Okayama University
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| Start Page | 3
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| End Page | 7
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| ISSN | 0474-0254
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| NCID | AN00033029
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| Content Type |
Departmental Bulletin Paper
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| language |
Japanese
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| File Version | publisher
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| Refereed |
False
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| Eprints Journal Name | srfa
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