Purification and characterization of monomeric lysine decarboxylase from soybean (Glycine max) axes.
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%.
Kim
H S
HS
Department of Biochemistry, College of Science, Yonsei University, Seoul, Korea.
Kim
B H
BH
Cho
Y D
YD
D002262:Carboxy-Lyases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification*; D004789:Enzyme Activation / Q000187:drug effects; D018525:Germination; D007526:Isoelectric Point; D007700:Kinetics; D008970:Molecular Weight; D063245:Plant Development; D010944:Plants / Q000201:enzymology; D011073:Polyamines / Q000494:pharmacology; D011189:Potassium Chloride / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology; D013025:Glycine max / Q000201:enzymology* / Q000254:growth & development
D011073:Polyamines; D012965:Sodium Chloride; D011189:Potassium Chloride; D002262:Carboxy-Lyases; C021520:lysine decarboxylase