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Structural and Functional Characterization of NadR from Lactococcus lactis.

Artem Stetsenko1, Rajkumar Singh1, Michael Jaehme1

  • 1Groningen Biomolecular Science and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.

Molecules (Basel, Switzerland)
|April 26, 2020
PubMed
Summary

The bifunctional enzyme NadR converts nicotinamide riboside (NR) to nicotinamide adenine dinucleotide (NAD). Structural analysis of Lactococcus lactis NadR revealed an adenine nucleotide

Keywords:
NADNMNNadRnicotinamide ribosidevitamins

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • NadR is a bifunctional enzyme crucial for synthesizing nicotinamide adenine dinucleotide (NAD).
  • Previous structural data from *Haemophilus influenzae* did not fully elucidate NadR's catalytic mechanism.
  • Understanding NadR's mechanism is key to NAD biosynthesis pathways.

Purpose of the Study:

  • To characterize the bifunctional enzyme NadR from *Lactococcus lactis*.
  • To investigate the kinetic properties and structural basis of NadR's catalytic mechanism.
  • To elucidate the role of ATP in the dual enzymatic activities of NadR.

Main Methods:

  • Purification of NadR enzyme from *Lactococcus lactis*.
  • Development of an assay to measure combined enzymatic activities.
  • Kinetic analysis of substrate dependence (NR, NMN, ATP).
  • X-ray crystallography of NadR from *L. lactis* (NadRLl) in complex with substrates and analogs.

Main Results:

  • NadR exhibited hyperbolic dependence on NR and sigmoidal dependence on ATP for NR to NAD conversion.
  • NMN to NAD conversion showed Michaelis-Menten kinetics for NMN but sigmoidal dependence on ATP.
  • Crystal structure of NadRLl revealed an adenine nucleotide binding site between domains, potentially involved in regulation or substrate channeling.

Conclusions:

  • The sigmoidal ATP dependence suggests cooperativity in NadR's bifunctional activity, possibly due to ATP's role in both catalytic steps.
  • The identified nucleotide-binding site offers insights into potential regulatory mechanisms or substrate channeling within NadR.
  • Structural and kinetic data provide a foundation for understanding NadR's role in NAD metabolism.