Literature DB >> 8394709

Localization of the potassium ion activation site in human liver fructose 1,6-bisphosphatase.

G J Xu1, Z B Yu, G F Hu, H T Cao.   

Abstract

Three mouse monoclonal antibodies of human liver fructose 1,6-bisphosphatase are shown to bind to the enzyme at different sites as determined by ELISA. The binding of one of the monoclonal antibodies, L2E1, mimics the effects of K+ ions, including increase in the enzyme activity and enhancement of the sensitivity of the enzyme to AMP inhibition. We tentatively suggest that human liver FruP2ase may have a specific K+ activation site, which at least partially overlaps with the L2E1 binding region. This site has been localized by analyzing the peptide fragments formed by cleavage with cyanogen bromide.

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Year:  1993        PMID: 8394709     DOI: 10.1006/bbrc.1993.1992

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Association and activation of fructose 1,6-bisphosphase during unfolding and refolding: spectroscopic and enzymatic studies.

Authors:  C Yuan; Z Q Xie; F W Zhang; G J Xu
Journal:  J Protein Chem       Date:  2001-01

2.  Inactivation precedes changes in allosteric properties and conformation of D-glyceraldehyde-3-phosphate dehydrogenase and fructose-1,6-bisphosphatase during denaturation by guanidinium chloride.

Authors:  R F Jiang; C L Tsou
Journal:  Biochem J       Date:  1994-10-01       Impact factor: 3.857

  2 in total

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