Functional Study of Lysine Decarboxylases from Klebsiella pneumoniae in Escherichia coli and Application of Whole Cell Bioconversion for Cadaverine Production.
Klebsiella pneumoniae is a gram-negative, non-motile, rod-shaped, and encapsulated bacterium in the normal flora of the intestines, mouth, skin, and food, and has decarboxylation activity, which results in generation of diamines (cadaverine, agmatine, and putrescine). However, there is no specific information on the exact mechanism of decarboxylation in K. pnuemoniae. Specifically lysine decarboxylases that generate cadaverine with a wide range of applications has not been shown. Therefore, we performed a functional study of lysine decarboxylases. Enzymatic characteristics such as optimal pH, temperature, and substrates were examined by overexpressing and purifying CadA and LdcC. CadA and LdcC from K. pneumoniae had a preference for L-lysine, and an optimal reaction temperature of 37°C and an optimal pH of 7. Although the activity of purified CadA from K. pneumoniae was lower than that of CadA from E. coli, the activity of K. pneumoniae CadA in whole cell bioconversion was comparable to that of E. coli CadA, resulting in 90% lysine conversion to cadaverine with pyridoxal 5'-phosphate L-lysine.
Department of Biological Engineering, College of Engineering, Konkuk University, Seoul 05029, Republic of Korea.
Jung-Ho
JH
Kim
Department of Biological Engineering, College of Engineering, Konkuk University, Seoul 05029, Republic of Korea.
Hyun Joong
HJ
Kim
Department of Biological Engineering, College of Engineering, Konkuk University, Seoul 05029, Republic of Korea.
Yong Hyun
YH
Kim
Department of Biological Engineering, College of Engineering, Konkuk University, Seoul 05029, Republic of Korea.
Jong Min
JM
Jeon
Department of Biological Engineering, College of Engineering, Konkuk University, Seoul 05029, Republic of Korea.
Hun Suk
HS
Song
Department of Biological Engineering, College of Engineering, Konkuk University, Seoul 05029, Republic of Korea.
Junyoung
J
Kim
Department of Biological Engineering, College of Engineering, Konkuk University, Seoul 05029, Republic of Korea.
So-Young
SY
No
Department of Biological and Chemical Engineering, Hongik University, Sejong City 30016, Republic of Korea.
Ji-Hyun
JH
Shin
Department of Environmental Engineering, Ajou University, Suwon 16499, Republic of Korea.
Kwon-Young
KY
Choi
Department of Biological and Chemical Engineering, Hongik University, Sejong City 30016, Republic of Korea.
Kyung Moon
KM
Park
Department of Biological Engineering, College of Engineering, Konkuk University, Seoul 05029, Republic of Korea.
Yung-Hun
YH
Yang
D001426:Bacterial Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism*; D002103:Cadaverine / Q000378:metabolism*; D002262:Carboxy-Lyases / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics*; D007711:Klebsiella pneumoniae / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D002262:Carboxy-Lyases; C021520:lysine decarboxylase; D002103:Cadaverine
Klebsiella pneumoniae; biotransformation; cadaverine; lysine decarboxylase; optimization