Purification, kinetic studies, and homology model of Escherichia coli fructose-1,6-bisphosphatase-Reference-Cited by-同舟云学术

Purification, kinetic studies, and homology model of Escherichia coli fructose-1,6-bisphosphatase

Published:2002-01 Issue:1 Volume:1594 Page:6-16
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Kelley-Loughnane Nancy,Biolsi Susan A,Gibson Kate M,Lu Guqiang,Hehir Michael J,Phelan Paul,Kantrowitz Evan R

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference37 articles.

1. Inhibition of fructose-1,6-bisphosphatase by fructose 2,6-bisphosphate.

2. J.-Y. Liang, Y. Zhang, S. Huang, H. Ke, W.N. Lipscomb. Activity and allosteric regulation in fructose-1,6-bisphosphatase, in: Proc. 36th Robert A. Welch Found. Conf. Chem. Res. (Regulation of Proteins by Ligands), The Robert A. Welch Foundation, Houston, TX, 1992, pp. 57–99.

3. Comparative amino acid sequence of fructose-1,6-bisphosphatases: identification of a region unique to the light-regulated chloroplast enzyme.

4. Isolation and sequence analysis of the cDNA for pig kidney fructose 1,6-bisphosphatase.

5. Fructose bisphosphatase from Escherichia coli. Purification and characterization

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