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Biochemical and biophysical research communications

Human hexokinase: sequences of amino- and carboxyl-terminal halves are homologous.


PMID 3207429

Abstract

cDNA clones encoding human hexokinase have been isolated from an adult kidney library. Analysis of this 917 amino acid protein (Mr = 102,519) indicates that the sequences of the NH2- and COOH-terminal halves, corresponding to the regulatory and catalytic domains, respectively, are homologous; and that eukaryotic hexokinases evolved by duplication of a gene encoding a protein of 450 amino acids. The COOH-terminal half of the protein created by this gene duplication retained the glucose binding site and glucose phosphorylating activity while the substrate binding sites of the NH2-terminal half evolved into a new allosteric effector site.

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H2917 Hexokinase-2 human, 1 mg/mL, buffered aqueous glycerol solution