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Effects of nucleotides on the interaction of renin with GlcNAc 2-epimerase (renin binding protein, RnBP).

作者信息

Takahashi Saori, Hori Kazuyuki, Ogasawara Hironobu, Hiwatashi Kazuyuki, Sugiyama Toshihiro

机构信息

Akita Research Institute for Food and Brewing, 4-26, Sanuki, Arayamachi, Akita 010-1623.

出版信息

J Biochem. 2006 Nov;140(5):725-30. doi: 10.1093/jb/mvj201. Epub 2006 Oct 5.

DOI:10.1093/jb/mvj201
PMID:17023685
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.

摘要

相似文献

1
Effects of nucleotides on the interaction of renin with GlcNAc 2-epimerase (renin binding protein, RnBP).
J Biochem. 2006 Nov;140(5):725-30. doi: 10.1093/jb/mvj201. Epub 2006 Oct 5.
2
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Identification of a domain conferring nucleotide binding to the N-acetyl-d-glucosamine 2-epimerase (Renin binding protein).
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