FAD-binding site and NADP reactivity in human renalase: a new enzyme involved in blood pressure regulation.

  title={FAD-binding site and NADP reactivity in human renalase: a new enzyme involved in blood pressure regulation.},
  author={M. T. Milani and Francesco Ciriello and Sara Baroni and Vittorio Pandini and Giulia Canevari and Martino Bolognesi and Alessandro Aliverti},
  journal={Journal of molecular biology},
  volume={411 2},
Renalase is a recently discovered flavoprotein that regulates blood pressure, regulates sodium and phosphate excretion, and displays cardioprotectant action through a mechanism that is barely understood to date. It has been proposed to act as a catecholamine-degrading enzyme, via either O(2)-dependent or NADH-dependent mechanisms. Here we report the renalase crystal structure at 2.5 Å resolution together with new data on its interaction with nicotinamide dinucleotides. Renalase adopts the p… CONTINUE READING


Publications citing this paper.
Showing 1-10 of 30 extracted citations


Publications referenced by this paper.
Showing 1-10 of 35 references

Regulation of blood pressure and cardiovascular function by renalase.

Kidney international • 2009
View 3 Excerpts
Highly Influenced

Role of renalase in the regulation of blood pressure and the renal dopamine system.

Current opinion in nephrology and hypertension • 2011
View 2 Excerpts

Features and development of Coot

Acta crystallographica. Section D, Biological crystallography • 2010
View 1 Excerpt

Oxidation of amines by flavoproteins.

Archives of biochemistry and biophysics • 2010
View 1 Excerpt

Similar Papers

Loading similar papers…