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ID 44050
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Title Alternative
Purification and Characterization of l-Methionine Decarboxylase from Streptomyces sp. 590
Author
Maemura, Tomomi
Uchitomi, Kumiko
Kusaka, Chika
Soda, Kenji
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.
Keywords
L-methionine decarboxylase
pyridoxal 5’-phosohate
Streptomyces
decarboxylation of L-methionine
Note
原著論文
Published Date
2011-02-01
Publication Title
岡山大学農学部学術報告
Publication Title Alternative
Scientific Reports of the Faculty of Agriculture Okayama University
Volume
volume100
Publisher
岡山大学農学部
Publisher Alternative
Faculty of Agriculture, Okayama University
Start Page
3
End Page
7
ISSN
0474-0254 
NCID
AN00033029
Content Type
Departmental Bulletin Paper
language
日本語
File Version
publisher
Refereed
False
Eprints Journal Name
srfa