2
84
K. Kirimura et al. / Biochemical and Biophysical Research Communications 394 (2010) 279–284
decarboxylase from Bacillus subtilis ATCC 6051 [9], pyrrole-2-car-
boxylate decarboxylase from Bacillus megaterium PYR2910 [10],
indole-3-carboxylate decarboxylase from Arthrobacter nicotianae
Education, Culture, Sports, Science and Technology (MEXT), Japan
and by Waseda University Grant for Special Research Projects.
FI1612 [11], and
acter WU-0108, Rhizobium sp. MTP-10005, and Agrobacterium
c-resorcylic acid decarboxylase from R. radiob-
Appendix A. Supplementary data
tumefaciens IAM12408 have been previously reported [6–8].
These already-known reversible decarboxylases, except
cylic acid decarboxylase and vanillate/4-hydroxybenzoate decar-
boxylase, were sensitive to O , but Sdc was insensitive to O
Moreover, under both conditions in the presence and absence of
, the decarboxylase and carboxylase activities of Sdc were not
c-resor-
2
2
.
References
O
2
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affected, suggesting that the handling of the recombinant E. coli
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Several genes encoding the nonoxidative aromatic decarboxy-
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[
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In conclusion, we succeeded in the molecular characterization
of a novel reversible and nonoxidative salicylic acid decarboxylase
from T. moniliiforme WU-0401 by purification, characterization and
gene identification of Sdc. A recombinant E. coli expressing sdc con-
verted 40 mM phenol to 10.6 mM salicylic acid with a 27% (mol/
mol) yield at 30 °C for 9 h. Therefore, we consider that the method
described here is a significant model process for selective and eco-
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Acknowledgments
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This study was supported in part by the Global-COE Program
‘Center for Practical Chemical Wisdom” from the Ministry of
‘