Renin inhibits N-acetyl-D-glucosamine 2-epimerase (renin-binding protein)

J Biochem. 2000 Dec;128(6):951-6. doi: 10.1093/oxfordjournals.jbchem.a022846.

Abstract

Renin-binding protein (RnBP) is a highly specific renin inhibitor first isolated from porcine kidney. Our recent studies demonstrated that the human RnBP is the enzyme N-acetyl-D-glucosamine (GlcNAc) 2-epimerase [Takahashi, S. et al. (1999) J. Biochem. 125, 348-353]. We have developed a new assay method for GlcNAc 2-epimerase activity using a system of N-acyl-D-hexosamine oxidase coupled with peroxidase and employed this method to study the effects of renin on GlcNAc 2-epimerase activity. The recombinant human (rh) RnBP existed as a dimer and its GlcNAc 2-epimerase activity was strongly inhibited by the purified renin concomitant with the formation of RnBP-renin heterodimer, so-called high molecular weight (HMW) renin. The renin activity was also inhibited by rhRnBP in a dose-dependent manner. These results indicate that renin is an inhibitor of GlcNAc 2-epimerase, and the renin-RnBP heterodimer HMW renin is an inactive form of both renin and GlcNAc 2-epimerase activities.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbohydrate Epimerases / antagonists & inhibitors*
  • Carbohydrate Epimerases / metabolism
  • Carrier Proteins / antagonists & inhibitors*
  • Carrier Proteins / metabolism
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Renin / physiology*
  • Substrate Specificity

Substances

  • Carrier Proteins
  • Enzyme Inhibitors
  • Renin
  • Carbohydrate Epimerases
  • N-acyl-D-glucosamine 2-epimerase
  • RENBP protein, human