Enzymes of the cyclic GMP metabolism in bovine retina. I. Cloning and expression of the gene for guanylate kinase
Autor: | Ibragim Gaidarov, N.G. Abdulaev, O.N. Suslov |
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Rok vydání: | 1993 |
Předmět: |
DNA
Complementary Guanylate kinase Recombinant Fusion Proteins Molecular Sequence Data Biophysics Gene Expression Sequence Homology Expression Biology Molecular cloning Biochemistry Retina Structural Biology Complementary DNA Genetics Escherichia coli Animals Trypsin Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence Cyclic GMP chemistry.chemical_classification Base Sequence GMP binding cGMP cycle B. taurus Nucleic acid sequence Hydrogen Bonding Cell Biology Molecular biology Amino acid Enzyme chemistry cDNA cloning Cattle Electrophoresis Polyacrylamide Gel Transformation Bacterial Nucleoside-Phosphate Kinase Guanylate Kinases Sequence Analysis Plasmids |
Zdroj: | FEBS letters. 335(1) |
ISSN: | 0014-5793 |
Popis: | Guanylate kinase (EC 2.7.4.8) catalyzing the reaction GMP + ATP = GDP + ADP, was purified to homogeneity from bovine retina. Using oligonucleotides based on the amino acid sequence of this enzyme, the cDNA encoding guanylate kinase (GK) was isolated and its nucleotide sequence was determined. Expression of the GK cDNA in E. coli, and the purification and functional characterization of the expressed enzyme are presented. It is shown that bovine retinal GK, like its yeast counterpart, contains the characteristic glycine-rich motif and all the amino acids involved in GMP binding. Bovine retinal enzyme is extended for several amino acid residues both at the N- and C-termini, compared to the yeast enzyme. |
Databáze: | OpenAIRE |
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