Archaeal type III RuBisCOs function in a pathway for AMP metabolism.
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.
Sato
Takaaki
T
Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.
Atomi
Haruyuki
H
Imanaka
Tadayuki
T
D000249:Adenosine Monophosphate / Q000378:metabolism*; D001105:Archaea / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D019843:Archaeal Proteins / Q000378:metabolism*; D004926:Escherichia coli; D053858:Metabolic Networks and Pathways; D008715:Methionine / Q000378:metabolism; D010428:Pentosephosphates / Q000378:metabolism; D011994:Recombinant Proteins; D012273:Ribulose-Bisphosphate Carboxylase / Q000145:classification / Q000378:metabolism*; D019712:Thermococcus / Q000201:enzymology* / Q000235:genetics; D013939:Thymidine Phosphorylase / Q000235:genetics
D019843:Archaeal Proteins; D010428:Pentosephosphates; D011994:Recombinant Proteins; C050562:ribose-1,5-bisphosphate; D000249:Adenosine Monophosphate; D008715:Methionine; D013939:Thymidine Phosphorylase; D012273:Ribulose-Bisphosphate Carboxylase