|
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 |
Activity |
4.1.1.18 |
Family |
4.1.1.18.b |
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 4.1.1.18) 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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