TY - JOUR
T1 - Screening, cloning, expression, and purification of an acidic arylmalonate decarboxylase from Enterobacter cloacae KU1313
AU - Yatake, Yoshito
AU - Miyamoto, Kenji
AU - Ohta, Hiromichi
N1 - Funding Information:
Acknowledgments This research was supported in part by the Ministry of Education, Culture, Sports, Science and Technology, Grant-in-Aid for the Twenty-first Century Center of Excellence Program entitled “Understanding and Control of Life’s Function via Systems Biology (Keio University).” Financial support from Takeda Science Foundation is also greatly acknowledged.
PY - 2008/4
Y1 - 2008/4
N2 - We have already isolated, purified, and characterized arylmalonate decarboxylases (AMDase; EC. 4.1.1.76) from Alcaligenes bronchisepticus KU1201 and Achromobacter sp. KU1311. These are unique enzymes that give optically pure α-arylpropionates from the corresponding α-aryl-α- methylmalonates. Recently, we have further screened novel AMDase producers from soil samples under acidic conditions and succeeded in isolating Enterobacter cloacae KU1313. The gene encoding the enzyme was cloned by polymerase chain reaction and sequenced. The AMDase gene consists of 720 nucleotides, which specifies a 240-amino-acid protein. The recombinant enzyme was purified and shown that the pH-activity profiles were quite different from those of known AMDases.
AB - We have already isolated, purified, and characterized arylmalonate decarboxylases (AMDase; EC. 4.1.1.76) from Alcaligenes bronchisepticus KU1201 and Achromobacter sp. KU1311. These are unique enzymes that give optically pure α-arylpropionates from the corresponding α-aryl-α- methylmalonates. Recently, we have further screened novel AMDase producers from soil samples under acidic conditions and succeeded in isolating Enterobacter cloacae KU1313. The gene encoding the enzyme was cloned by polymerase chain reaction and sequenced. The AMDase gene consists of 720 nucleotides, which specifies a 240-amino-acid protein. The recombinant enzyme was purified and shown that the pH-activity profiles were quite different from those of known AMDases.
KW - AMDase
KW - Arylmalonate decarboxylase
KW - Asymmetric decarboxylation
KW - Enterobacter cloacae
KW - Purification
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U2 - 10.1007/s00253-008-1375-8
DO - 10.1007/s00253-008-1375-8
M3 - Article
C2 - 18283449
AN - SCOPUS:41049104158
SN - 0175-7598
VL - 78
SP - 793
EP - 799
JO - Applied Microbiology and Biotechnology
JF - Applied Microbiology and Biotechnology
IS - 5
ER -