Human hexokinase: sequences of amino- and carboxyl-terminal halves are homologous. 1988

S Nishi, and S Seino, and G I Bell
Howard Hughes Medical Institute, Department of Biochemistry, University of Chicago, IL 60637.

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.

UI MeSH Term Description Entries
D007668 Kidney Body organ that filters blood for the secretion of URINE and that regulates ion concentrations. Kidneys
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D002384 Catalysis The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction. Catalyses
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D005947 Glucose A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement. Dextrose,Anhydrous Dextrose,D-Glucose,Glucose Monohydrate,Glucose, (DL)-Isomer,Glucose, (alpha-D)-Isomer,Glucose, (beta-D)-Isomer,D Glucose,Dextrose, Anhydrous,Monohydrate, Glucose
D006593 Hexokinase An enzyme that catalyzes the conversion of ATP and a D-hexose to ADP and a D-hexose 6-phosphate. D-Glucose, D-mannose, D-fructose, sorbitol, and D-glucosamine can act as acceptors; ITP and dATP can act as donors. The liver isoenzyme has sometimes been called glucokinase. (From Enzyme Nomenclature, 1992) EC 2.7.1.1. Hexokinase A,Hexokinase D,Hexokinase II
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000494 Allosteric Regulation The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES. Regulation, Allosteric,Allosteric Regulations,Regulations, Allosteric
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein

Related Publications

S Nishi, and S Seino, and G I Bell
March 1961, Biochimica et biophysica acta,
S Nishi, and S Seino, and G I Bell
March 1965, The Journal of biological chemistry,
S Nishi, and S Seino, and G I Bell
January 1991, The Journal of biological chemistry,
S Nishi, and S Seino, and G I Bell
June 2009, BMB reports,
S Nishi, and S Seino, and G I Bell
June 1999, The Journal of biological chemistry,
S Nishi, and S Seino, and G I Bell
May 1976, FEBS letters,
Copied contents to your clipboard!