Identification of cysteine-380 as the essential residue for the human N-acetyl-D-glucosamine 2-epimerase (renin binding protein).

Identification of cysteine-380 as the essential residue for the human N-acetyl-D-glucosamine 2-epimerase (renin binding protein). Research Abstract Details 

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Identification of cysteine-380 as the essential residue for the human N-acetyl-D-glucosamine 2-epimerase (renin binding protein). Abstract Text:

S Takahashi,K Takahashi,T Kaneko,H Ogasawara,S Shindo,K Saito,M Kobayashi,

Renin binding protein (RnBP) is a proteinous renin inhibitor firstly isolated from porcine kidney. Recently, the protein was identified as the enzyme, N-acetyl-D-glucosamine (GlcNAc) 2-epimerase. The GlcNAc 2-epimerase activity of recombinant human RnBP was specifically inhibited by SH-reagents such as N-ethylmaleimide, 5, 5'-dithiobis-2-nitrobenzoate, and iodoacetic acid, indicating that the most probable reactive site is a cysteine residue. To identify the active site residue(s), we have constructed ten cysteine residue mutants (C41S, C66S, C104S, C125S, C210S, C239S, C302S, C380S, C386S, and C390S) for human GlcNAc 2-epimerase and expressed them in Escherichia coli cells. The relative specific activities of C41S, C66S, C125S, C210S, C239S, C302S, C386S, and C390S are nearly the same to that of the wild-type enzyme. The specific activity of the C104S mutant is 26% of that of the wild-type enzyme. The expression of the C380S mutant in E. coli cells was detected on Western blotting, whereas GlcNAc 2-epimerase activity was not detected in the extract. These results indicate that Cys380 is essential for the enzymatic activity of human GlcNAc 2-epimerase.

Identification of cysteine-380 as the essential residue for the human N-acetyl-D-glucosamine 2-epimerase (renin binding protein). Publishing Authors By Initials

S Takahashi,K Takahashi,T Kaneko,H Ogasawara,S Shindo,K Saito,M Kobayashi,

For similar chemical actions and uses: specialty uses of chemicals: laboratory chemicals: indicators and reagents: sulfhydryl reagents research abstracts see: chemical actions and uses: specialty uses of chemicals: laboratory chemicals: indicators and reagents: sulfhydryl reagents research

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Identification of cysteine-380 as the essential residue for the human N-acetyl-D-glucosamine 2-epimerase (renin binding protein). Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 126

Page Numbers: 639-42

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Oct

YEAR: 1999

Identification of cysteine-380 as the essential residue for the human N-acetyl-D-glucosamine 2-epimerase (renin binding protein). Information

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LANGUAGE: eng

NlmUniqueID: 376600

Identification of cysteine-380 as the essential residue for the human N-acetyl-D-glucosamine 2-epimerase (renin binding protein). Keywords Mesh Terms:

KEYWORDS: Sulfhydryl Reagents

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Identification of cysteine-380 as the essential residue for the human N-acetyl-D-glucosamine 2-epimerase (renin binding protein). Information

Substance Name: RENBP protein, human

Registry Number: EC 5.1.3.8

Grant and Affiliation Information for Identification of cysteine-380 as the essential residue for the human N-acetyl-D-glucosamine 2-epimerase (renin binding protein).

AFFILIATION: Department of Bioengineering, Akita Research Institute of Food and Brewing (ARIF), Arayamachi, Akita, 010-1623, Japan. saori@arif.pref. akita.jp

Country: JAPAN

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MEDLINETA: J Biochem

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