2023
DOI: 10.1002/pro.4703
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Insight into the role of the Bateman domain at the molecular and physiological levels through engineered IMP dehydrogenases

Abstract: Inosine 5 0 -monophosphate (IMP) dehydrogenase (IMPDH) is an ubiquitous enzyme that catalyzes the NAD + -dependent oxidation of inosine 5 0monophosphate into xanthosine 5 0 -monophosphate. This enzyme is formed of two distinct domains, a core domain where the catalytic reaction occurs, and a less-conserved Bateman domain. Our previous studies gave rise to the classifi-

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Cited by 5 publications
(1 citation statement)
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“…Interestingly, the interchange of the Bateman domain between representatives of both classes leads to the transplantation of the allosteric kinetic regulation or quaternary structure modulation. These recent results demonstrate the key role of the Bateman domain on the IMPDH molecular behaviors and confirm its implication in E. coli physiology ( Gedeon et al, 2023a ).…”
Section: The Multiple Facets Of Allosteric Regulation In Impdhsupporting
confidence: 72%
“…Interestingly, the interchange of the Bateman domain between representatives of both classes leads to the transplantation of the allosteric kinetic regulation or quaternary structure modulation. These recent results demonstrate the key role of the Bateman domain on the IMPDH molecular behaviors and confirm its implication in E. coli physiology ( Gedeon et al, 2023a ).…”
Section: The Multiple Facets Of Allosteric Regulation In Impdhsupporting
confidence: 72%