ArticleJournal of bacteriology2012
Enzymatic characterization of AMP phosphorylase and ribose-1,5-bisphosphate isomerase functioning in an archaeal AMP metabolic pathway.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 57 citations in OpenAlex.
- Exploring archaeal resources for biomass-derived pentose utilization: pathways, extremozymes, and bioprocessing applications.World journal of microbiology & biotechnology · 2026Review
- A pentose bisphosphate pathway of nucleotide degradation in Promethearchaeum syntrophicum.Science China. Life sciences · 2026Article
- Exploring the Diversity and Metabolic Potential of COMicrobes and environments · 2026Article
- Pentose bisphosphate pathway can act in central metabolism for nucleoside-dependent growth ofApplied and environmental microbiology · 2025Article
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- Bioenergetics evolution: the link between Earth's and Life's history.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- The radical impact of oxygen on prokaryotic evolution-enzyme inhibition first, uninhibited essential biosyntheses second, aerobic respiration third.FEBS letters · 2024Article
- Removal of phosphoglycolate in hyperthermophilic archaea.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A non-carboxylating pentose bisphosphate pathway in halophilic archaea.Communications biology · 2022Article
- Functional differentiation determines the molecular basis of the symbiotic lifestyle of Ca. Nanohaloarchaeota.Microbiome · 2022Article
- Characterization of metagenome-assembled genomes of two endo-archaea ofFrontiers in microbiomes · 2022Article
- Comparative Genomics Provides Insights into the Genetic Diversity and Evolution of the DPANN Superphylum.mSystems · 2021Article
- Thermostable adenosine 5'-monophosphate phosphorylase from Thermococcus kodakarensis forms catalytically active inclusion bodies.Scientific reports · 2021Article
- Elucidation of the Translation Initiation Factor Interaction Network ofFrontiers in microbiology · 2021Article
- Metabolic Diversity and Evolutionary History of the Archaeal Phylum "Applied and environmental microbiology · 2020Article
- Article
- Form III RubisCO-mediated transaldolase variant of the Calvin cycle in a chemolithoautotrophic bacterium.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Prodigal Compound: Return of Ribosyl 1,5-Bisphosphate as an Important Player in Metabolism.Microbiology and molecular biology reviews : MMBR · 2019Review
- Asgard archaea: Diversity, function, and evolutionary implications in a range of microbiomes.AIMS microbiology · 2019Review
- Role of Structural Features in Oligomerization, Active-Site Integrity and Ligand Binding of Ribose-1,5-Bisphosphate Isomerase.Computational and structural biotechnology journal · 2019Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
AMP phosphorylase (AMPpase), ribose-1,5-bisphosphate (R15P) isomerase, and type III ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) have been proposed to constitute a novel pathway involved in AMP metabolism in the Archaea. Here we performed a biochemical examination of AMPpase and R15P isomerase from Thermococcus kodakarensis. R15P isomerase was specific for the α-anomer of R15P and did not recognize other sugar compounds. We observed that activity was extremely low with the substrate R15P alone but was dramatically activated in the presence of AMP. Using AMP-activated R15P isomerase, we reevaluated the substrate specificity of AMPpase. AMPpase exhibited phosphorylase activity toward CMP and UMP in addition to AMP. The [S]-v plot (plot of velocity versus substrate concentration) of the enzyme toward AMP was sigmoidal, with an increase in activity observed at concentrations higher than approximately 3 mM. The behavior of the two enzymes toward AMP indicates that the pathway is intrinsically designed to prevent excess degradation of intracellular AMP. We further examined the formation of 3-phosphoglycerate from AMP, CMP, and UMP in T. kodakarensis cell extracts. 3-Phosphoglycerate generation was observed from AMP alone, and from CMP or UMP in the presence of dAMP, which also activates R15P isomerase. 3-Phosphoglycerate was not formed when 2-carboxyarabinitol 1,5-bisphosphate, a Rubisco inhibitor, was added. The results strongly suggest that these enzymes are actually involved in the conversion of nucleoside monophosphates to 3-phosphoglycerate in T. kodakarensis.
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