Scientific Reports of the Faculty of Agriculture, Okayama University
Published by the Faculty of Agriculture, Okayama University
ONLINE ISSN : 2186-7755

放線菌Streptomyces sp.590由来l-メチオニン脱炭酸酵素の精製および性質検討

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
ISSN
0474-0254 
NCID
AN00033029