Allosteric Regulation of Type I Hexokinase: A Site-Directed Mutational Study Indicating Location of the Functional Glucose 6-Phosphate Binding Site in the N-Terminal Half of the Enzyme-Reference-Cited by-同舟云学术

Allosteric Regulation of Type I Hexokinase: A Site-Directed Mutational Study Indicating Location of the Functional Glucose 6-Phosphate Binding Site in the N-Terminal Half of the Enzyme

Published:1999-02 Issue:2 Volume:362 Page:203-210
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Sebastian Siby,Wilson John E.,Mulichak Anne,Garavito R.Michael

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference35 articles.

1. Hexokinases

2. Functional Organization of Mammalian Hexokinase II

3. Functional Organization of Mammalian Hexokinases: Both N- and C-Terminal Halves of the Rat Type II Isozyme Possess Catalytic Sites

4. Isolation and characterization of the discrete N- and C-terminal halves of rat brain hexokinase: Retention of full catalytic activity in the isolated C-terminal half

5. Binding of nucleoside triphosphates, inorganic phosphate, and other polyanionic ligands to the N-terminal region of rat brain hexokinase: Relationship to regulation of hexokinase activity by antagonistic interactions between glucose 6-phosphate and inorganic phosphate

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