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B6db references: 98297252

type Journal Article
authors Kim, H. S.; Kim, B. H.; Cho, Y. D.
title Purification and characterization of monomeric lysine decarboxylase from soybean (Glycine max) axes
journal Arch Biochem Biophys
sel unselected
ui 98297252
year (1998)
volume 354
number 1
pages 40-6.
keywords Carboxy-Lyases/antagonists & inhibitors/*chemistry/*isolation & purification
abstract Lysine decarboxylase (EC was purified 364-fold from 2-day-old soybean (Glycine max) axes. The enzyme was a monomeric protein having a molecular mass of 95,000 Da and an isoelectric point of 4.0. The K(m) for L-lysine was 1.17 mM. The optimal temperature and pH of the enzyme were 37 degrees C and 7.5, respectively. Storage of the enzyme at temperature ranging from 0 to 4 degrees C caused a 50% loss of the activity in 24 h. The enzyme was competitively inhibited by Cl- with a Ki value of 1.46 mM. However, the activity of the purified enzyme was not inhibited by F-, Br-, I-, H2PO4-, HPO4(2-), or SO4(2-). Cadaverine at 1 mM inhibited the enzyme activity by 35%.
last changed 2014/07/11 10:49

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