TY - JOUR
T1 - Occurrence of agmatine pathway for putrescine synthesis in Selenomonas ruminatium
AU - Liao, Shaofu
AU - Poonpairoj, Phuntip
AU - Ko, Kyong Cheol
AU - Takatuska, Yumiko
AU - Yamaguchi, Yoshihiro
AU - Abe, Naoki
AU - Kaneko, Jun
AU - Kamio, Yoshiyuki
N1 - Funding Information:
This work was supported in part by the Foundation of the Noda Institute for Scientific Research. S. Liao and K-C. Ko were supported by pre-doctoral fellowship from Yoneyama Foundation and Waroh Suzuki Foundation respectively. P. Poonpairoi was the recipient of a fellowship from the Ministry of Education, Cultures, Sports, Science and Technology of Japan. Y. Takatsuka and Y. Yamaguchi were the recipients of postdoctoral fellowships from the Japan Society for Promotion of Science.
PY - 2008
Y1 - 2008
N2 - Selenomonas ruminantium synthesizes cadaverine and putrescine from L-lysine and L-ornithine as the essential constituents of its peptidoglycan by a constitutive lysine/ornithine decarboxylase (LDC/ODC). S. ruminantium grew normally in the presence of the specific inhibitor for LDC/ODC, DL-α-difluoromethylornithine, when arginine was supplied in the medium. In this study, we discovered the presence of arginine decarboxylase (ADC), the key enzyme in agmatine pathway for putrescine synthesis, in S. ruminantium. We purified and characterized ADC and cloned its gene (adc) from S. ruminantium chromosomal DNA. ADC showed more than 60% identity with those of LDC/ODC/ADCs from Gram-positive bacteria, but no similarity to that from Gram-negative bacteria. In this study, we also cloned the aguA and aguB genes, encoding agmatine deiminase (AguA) and N-carbamoyl-putrescine amidohydrolase (AguB), both of which are involved in conversion from agmatine into putrescine. AguA and AguB were expressed in S. ruminantium. Hence, we concluded that S. ruminantium has both ornithine and agmatine pathways for the synthesis of putrescine.
AB - Selenomonas ruminantium synthesizes cadaverine and putrescine from L-lysine and L-ornithine as the essential constituents of its peptidoglycan by a constitutive lysine/ornithine decarboxylase (LDC/ODC). S. ruminantium grew normally in the presence of the specific inhibitor for LDC/ODC, DL-α-difluoromethylornithine, when arginine was supplied in the medium. In this study, we discovered the presence of arginine decarboxylase (ADC), the key enzyme in agmatine pathway for putrescine synthesis, in S. ruminantium. We purified and characterized ADC and cloned its gene (adc) from S. ruminantium chromosomal DNA. ADC showed more than 60% identity with those of LDC/ODC/ADCs from Gram-positive bacteria, but no similarity to that from Gram-negative bacteria. In this study, we also cloned the aguA and aguB genes, encoding agmatine deiminase (AguA) and N-carbamoyl-putrescine amidohydrolase (AguB), both of which are involved in conversion from agmatine into putrescine. AguA and AguB were expressed in S. ruminantium. Hence, we concluded that S. ruminantium has both ornithine and agmatine pathways for the synthesis of putrescine.
KW - Agmatine deiminase
KW - Agmatine pathway for putrescine synthesis
KW - Arginine decarboxylase
KW - N-carbamoyl-putrescine amidohydrolase
KW - Selenomonas ruminantium
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U2 - 10.1271/bbb.70550
DO - 10.1271/bbb.70550
M3 - Article
C2 - 18256468
AN - SCOPUS:40449112983
SN - 0916-8451
VL - 72
SP - 445
EP - 455
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 2
ER -