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PMID:3207429

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Citation

Nishi, S, Seino, S and Bell, GI (1988) Human hexokinase: sequences of amino- and carboxyl-terminal halves are homologous. Biochem. Biophys. Res. Commun. 157:937-43

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.

Links

PubMed

Keywords

Allosteric Regulation; Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Catalysis; DNA/genetics; DNA Probes; Glucose/metabolism; Hexokinase/genetics; Humans; Kidney/analysis; Molecular Sequence Data; Phosphorylation; Rats; Sequence Homology, Nucleic Acid

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:HXK1

involved_in

GO:0006096: glycolytic process

ECO:0000304: author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

HUMAN:HXK1

enables

GO:0004396: hexokinase activity

ECO:0000304: author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete


See also

References

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