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Sequence-specific 1H, 13C and 15N resonance assignments of the rat liver fructose-2,6-bisphosphatase domain. 2003

Klaus Zangger, and Konstantin Pervushin, and Heinz Sterk, and Alex J Lange, and David A Okar

UI MeSH Term Description Entries
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D009587 Nitrogen Isotopes Stable nitrogen atoms that have the same atomic number as the element nitrogen but differ in atomic weight. N-15 is a stable nitrogen isotope. Nitrogen Isotope,Isotope, Nitrogen,Isotopes, Nitrogen
D002247 Carbon Isotopes Stable carbon atoms that have the same atomic number as the element carbon but differ in atomic weight. C-13 is a stable carbon isotope. Carbon Isotope,Isotope, Carbon,Isotopes, Carbon
D003903 Deuterium The stable isotope of hydrogen. It has one neutron and one proton in the nucleus. Deuterons,Hydrogen-2,Hydrogen 2
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus
D019906 Nuclear Magnetic Resonance, Biomolecular NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope. Biomolecular Nuclear Magnetic Resonance,Heteronuclear Nuclear Magnetic Resonance,NMR Spectroscopy, Protein,NMR, Biomolecular,NMR, Heteronuclear,NMR, Multinuclear,Nuclear Magnetic Resonance, Heteronuclear,Protein NMR Spectroscopy,Biomolecular NMR,Heteronuclear NMR,Multinuclear NMR,NMR Spectroscopies, Protein,Protein NMR Spectroscopies,Spectroscopies, Protein NMR,Spectroscopy, Protein NMR
D025481 Phosphofructokinase-2 An allosteric enzyme that regulates glycolysis and gluconeogenesis by catalyzing the transfer of a phosphate group from ATP to fructose-6-phosphate to yield fructose-2,6-bisphosphate, an allosteric effector for the other 6-phosphofructokinase, PHOSPHOFRUCTOKINASE-1. Phosphofructokinase-2 is bifunctional: the dephosphorylated form is a kinase and the phosphorylated form is a phosphatase that breaks down fructose-2,6-bisphosphate to yield fructose-6-phosphate. 6-Phosphofructo-2-kinase,6-Phosphofructo-2-kinase-fructose-2,6-bisphosphatase,Fructose-2,6-bisphosphatase,6-PF-2-K-Fru-2,6-P(2)ase,6-Phosphofructo 2-kinase-fructose 2,6-bisphosphatase,6PF2K,ATP-D-Fructose-6-phosphate 2-phosphotransferase,F Kinase-F-bisphosphatase,Fru-6-P,2-kinase,Fru-kinase-Fru-bisphosphatase,Fructose 2,6-bisphosphatase,Fructose-2,6-bisphosphate 2-phosphatase,Fructose-6-P,2-kinase,Fructose-6-phosphate,2-kinase,Fructose-6-phosphate,2-kinase-fructose-2,6-bisphosphatase,fructose-2,6-diphosphatase,Phosphofructokinase 2

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