Simultaneous multiple alignment of available sequences of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase revealed several segments of conserved residues in the 2-kinase domain. The sequence of the kinase domain was also compared with proteins of known three-dimensional structure. No similarity was found between the kinase domain of 6-phosphofructo-2-kinase and 6-phosphofructo-1-kinase. This questions the modelling of the 2-kinase domain on bacterial 6-phosphofructo-1-kinase that has previously been proposed [Bazan, Fletterick and Pilkis (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 9642Ő9646]. However, sequence similarities were found between the 2-kinase domain and several nucleotide-binding proteins, the most similar being adenylate kinase. A structural model of the 2-kinase domain based on adenylate kinase is proposed. It accommodates all the results of site-directed mutagenesis studies carried out to date on residues in the 2-kinase domain. It also allows residues potentially involved in catalysis and/or substrate binding to be predicted.
Skip Nav Destination
Article navigation
February 1997
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
Research Article|
February 01 1997
Modelling the 2-kinase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase on adenylate kinase
Luc BERTRAND;
Luc BERTRAND
*Facultés Universitaires Notre-Dame de la Paix, Department of Biology, Rue de Bruxelles, 61, B-5000 Namur, Belgium
†Hormone and Metabolic Research Unit, University of Louvain Medical School, and International Institute of Cellular and Molecular Pathology, Avenue Hippocrate, 75, B-1200 Brussels, Belgium
Search for other works by this author on:
Didier VERTOMMEN;
Didier VERTOMMEN
†Hormone and Metabolic Research Unit, University of Louvain Medical School, and International Institute of Cellular and Molecular Pathology, Avenue Hippocrate, 75, B-1200 Brussels, Belgium
Search for other works by this author on:
Eric DEPIEREUX;
Eric DEPIEREUX
*Facultés Universitaires Notre-Dame de la Paix, Department of Biology, Rue de Bruxelles, 61, B-5000 Namur, Belgium
Search for other works by this author on:
Louis HUE;
Louis HUE
†Hormone and Metabolic Research Unit, University of Louvain Medical School, and International Institute of Cellular and Molecular Pathology, Avenue Hippocrate, 75, B-1200 Brussels, Belgium
Search for other works by this author on:
Mark H. RIDER;
Mark H. RIDER
‡
†Hormone and Metabolic Research Unit, University of Louvain Medical School, and International Institute of Cellular and Molecular Pathology, Avenue Hippocrate, 75, B-1200 Brussels, Belgium
‡To whom correspondence should be addressed.
Search for other works by this author on:
Ernest FEYTMANS
Ernest FEYTMANS
*Facultés Universitaires Notre-Dame de la Paix, Department of Biology, Rue de Bruxelles, 61, B-5000 Namur, Belgium
Search for other works by this author on:
Publisher: Portland Press Ltd
Received:
July 16 1996
Revision Received:
September 26 1996
Accepted:
September 26 1996
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 1997
1997
Biochem J (1997) 321 (3): 615–621.
Article history
Received:
July 16 1996
Revision Received:
September 26 1996
Accepted:
September 26 1996
Connected Content
A correction has been published:
Modelling the 2-kinase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase on adenylate kinase
Citation
Luc BERTRAND, Didier VERTOMMEN, Eric DEPIEREUX, Louis HUE, Mark H. RIDER, Ernest FEYTMANS; Modelling the 2-kinase domain of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase on adenylate kinase. Biochem J 1 February 1997; 321 (3): 615–621. doi: https://doi.org/10.1042/bj3210615
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Captcha Validation Error. Please try again.