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Journal of Biochemistry Advance Access published online on October 5, 2006
Journal of Biochemistry, doi:10.1093/jb/mvj201
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© 2006 The Japanese Biochemical Society.
Received August 6, 2006
Accepted September 25, 2006

Regular Paper

Effects of Nucleotides on the Interaction of Renin with GlcNAc 2-Epimerase (Renin Binding Protein, RnBP)

Saori Takahashi 1 *, Kazuyuki Hori 1, Hironobu Ogasawara 1, Kazuyuki Hiwatashi 1, and Toshihiro Sugiyama 2

1 Akita Research Institute for Food and Brewing, 4-26, Sanuki, Arayamachi, Akita 010-1623, Japan
2 Department of Biochemistry, School of Medicine, Akita University, 1-1-1 Hondo, Akita 010-8543, Japan

* To whom correspondence should be addressed.
Saori Takahashi, E-mail: saori{at}arif.pref.akita.jp


  Abstract

Renin binding protein (RnBP), a cellular renin inhibitor, was identified as an enzyme, GlcNAc 2-epimerase. Recombinant RnBP inhibited porcine renin activity in a dose dependent manner. However, the inhibition was neutralized by nucleotides, such as ATP, dATP, dGTP, dCTP or dTTP. Moreover, ATP inhibited the formation of hetero-complex of renin with RnBP, called high molecular weight (HMW) renin. On the other hand, N-ethylmaleimide (NEM), a SH-alkylating reagent inhibited the GlcNAc 2-epimerase activity concomitant with the decaying of the dimer to the monomer of the enzyme. The inhibition was modulated in the presence of ATP. These results indicate that nucleotides stabilize the dimeric form RnBP (GlcNAc 2-epimerase) and inhibited the formation of the renin-RnBP hetero complex, HMW renin.

Keywords: ATP; binding protein; epimerase; GlcNAc; nucleotides; renin.
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