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Journal of Biochemistry Advance Access originally published online on October 5, 2006
Journal of Biochemistry 2006 140(5):725-730; doi:10.1093/jb/mvj201
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© 2006 The Japanese Biochemical Society.

ARTICLE

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

Saori Takahashi1,*, Kazuyuki Hori1, Hironobu Ogasawara1, Kazuyuki Hiwatashi1 and Toshihiro Sugiyama2

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

* To whom correspondence should be addressed. Tel: +81-18-888-2000, Fax: +81-18-888-2008, E-mail: saori{at}arif.pref.akita.jp

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.


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