PMID: 11926999Apr 3, 2002Paper

Identification of a domain conferring nucleotide binding to the N-acetyl-d-glucosamine 2-epimerase (Renin binding protein)

Journal of Biochemistry
Saori TakahashiKatsumi Mori

Abstract

Renin binding protein (RnBP), a cellular renin inhibitor, has been identified as the enzyme N-acetyl-D-glucosamine (GlcNAc) 2-epimerase. Our recent studies demonstrated that rat GlcNAc 2-epimerase has a ten-times higher affinity for ATP, dATP, and ddATP than the human enzyme [Takahashi, S. et al. (2001) J. Biochem. 130, 815-821]. To identify the domain conferring nucleotide binding to GlcNAc 2-epimerase, we constructed a series of chimeric enzymes successively replacing the three domains of the human enzyme (N-terminal, middle, and C-terminal domains) with the corresponding domains of the rat enzyme. Chimeras were expressed in Escherichia coli JM109 cells under the control of the Taq promoter. The purified chimeric enzymes had GlcNAc 2-epimerase activity and inhibited renin activity in a dose-dependent manner. The recombinant human and rat enzymes required catalytic amounts of ATP with apparent K(m) values of 73 and 5.5 microM, respectively. Chimeric enzymes of HHR, RHH, and RHR (H, human type domain; R, rat type domain) had nearly the same nucleotide specificity as the human GlcNAc 2-epimerase. On the other hand, HRR, HRH, and RRH chimeras had the same nucleotide specificity as the rat enzyme. These results indicate that the m...Continue Reading

Citations

Feb 10, 2009·Bioscience, Biotechnology, and Biochemistry·Takeshi SenouraSusumu Ito
Jul 24, 2014·BMC Genomics·Vincent GrassotJean-Michel Petit
Nov 5, 2011·Biochimie·Agustín Sola-CarvajalÁlvaro Sánchez-Ferrer
Jan 16, 2019·Acta Crystallographica. Section D, Structural Biology·Marie Josée Haglund HalsørInger Lin Uttakleiv Raeder
Oct 7, 2006·Journal of Biochemistry·Saori TakahashiToshihiro Sugiyama

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