Dynamic, Ligand-dependent Conformational Change Triggers Reaction of Ribose-1,5-bisphosphate Isomerase from Thermococcus kodakarensis KOD1

Ribose-1,5-bisphosphate isomerase (R15Pi) is a novel enzyme recently identified as a member of an AMP metabolic pathway in archaea. The enzyme converts d-ribose 1,5-bisphosphate into ribulose 1,5-bisphosphate, providing the substrate for archaeal ribulose-1,5-bisphosphate carboxylase/oxygenases. We...

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Hlavní autoři: Nakamura, Akira, Fujihashi, Masahiro, Aono, Riku, Sato, Takaaki, Nishiba, Yosuke, Yoshida, Shosuke, Yano, Ayumu, Atomi, Haruyuki, Imanaka, Tadayuki, Miki, Kunio
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Biochemistry and Molecular Biology 2012
Témata:
Protein Structure and Folding
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3375503/
https://ncbi.nlm.nih.gov/pubmed/22511789
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M112.349423
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