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Science 16 February 2007:
Vol. 315. no. 5814, pp. 1003 - 1006
DOI: 10.1126/science.1135999

Reports

Archaeal Type III RuBisCOs Function in a Pathway for AMP Metabolism

Takaaki Sato, Haruyuki Atomi, Tadayuki Imanaka*

The type III ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO) present in the archaeon Thermococcus kodakaraensis was found to participate in adenosine 5'-monophosphate (AMP) metabolism, a role that is distinct from that of classical RuBisCOs of the Calvin-Benson-Bassham cycle. Genes annotated as thymidine phosphorylase (deoA) and eucaryal translation initiation factor 2B (e2b2) were found to encode AMP phosphorylase and ribose-1,5-bisphosphate isomerase, respectively. These enzymes supplied the RuBisCO substrate, ribulose-1,5-bisphosphate, from AMP and phosphate. Archaea with type III RuBisCOs all harbor both DeoA and the corresponding E2b2 homologs. In this pathway, adenine was released from AMP and the phosphoribose moiety entered central-carbon metabolism.

Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.

* To whom correspondence should be addressed. E-mail: imanaka{at}sbchem.kyoto-u.ac.jp

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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T. J. Santangelo, L. Cubonova, and J. N. Reeve (2008)
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Multiple Rubisco forms in proteobacteria: their functional significance in relation to CO2 acquisition by the CBB cycle.
M. R. Badger and E. J. Bek (2008)
J. Exp. Bot. 59, 1525-1541
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Genome Sequence of Thermofilum pendens Reveals an Exceptional Loss of Biosynthetic Pathways without Genome Reduction.
I. Anderson, J. Rodriguez, D. Susanti, I. Porat, C. Reich, L. E. Ulrich, J. G. Elkins, K. Mavromatis, A. Lykidis, E. Kim, et al. (2008)
J. Bacteriol. 190, 2957-2965
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Polarity in Archaeal Operon Transcription in Thermococcus kodakaraensis.
T. J. Santangelo, L. Cubonova, R. Matsumi, H. Atomi, T. Imanaka, and J. N. Reeve (2008)
J. Bacteriol. 190, 2244-2248
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Function, Structure, and Evolution of the RubisCO-Like Proteins and Their RubisCO Homologs.
F. R. Tabita, T. E. Hanson, H. Li, S. Satagopan, J. Singh, and S. Chan (2007)
Microbiol. Mol. Biol. Rev. 71, 576-599
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Engineering of a Type III Rubisco from a Hyperthermophilic Archaeon in Order To Enhance Catalytic Performance in Mesophilic Host Cells.
S. Yoshida, H. Atomi, and T. Imanaka (2007)
Appl. Envir. Microbiol. 73, 6254-6261
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Science. ISSN 0036-8075 (print), 1095-9203 (online)