Human erythrocyte glucose-6-phosphate dehydrogenase. Identification of a reactive lysyl residue labelled with pyridoxal 5'-phosphate. 1988

L Camardella, and C Caruso, and B Rutigliano, and M Romano, and G Di Prisco, and F Descalzi-Cancedda
International Institute of Genetics and Biophysics, Consiglio Nazionale delle Ricerche, Naples, Italy.

Human erythrocyte glucose-6-phosphate dehydrogenase contains a reactive lysyl residue, which can be labelled with pyridoxal 5'-phosphate. The binding of one mole of pyridoxal 5'-phosphate per mole of enzyme subunit produces substantial inactivation. The substrate glucose-6-phosphate prevents the loss of activity, suggesting that the reaction site is close to the substrate-binding site. A tryptic peptide containing the pyridoxal-5'-phosphate-binding lysyl residue has been isolated and characterised. The reactive lysyl residue has been identified in the glucose-6-phosphate dehydrogenase amino acid sequence. Comparison with glucose-6-phosphate dehydrogenase from other sources shows a high homology with a peptide containing a reactive lysyl residue, isolated from the enzyme from Saccharomyces cerevisiae; glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides also contains a region highly homologous with the sequence around the reactive lysyl residue in the human enzyme. The results of this communication provide the first direct evidence for the association of an essential catalytic function with a specific region of the molecule of human erythrocyte glucose-6-phosphate dehydrogenase.

UI MeSH Term Description Entries
D008239 Lysine An essential amino acid. It is often added to animal feed. Enisyl,L-Lysine,Lysine Acetate,Lysine Hydrochloride,Acetate, Lysine,L Lysine
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D011732 Pyridoxal Phosphate This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE). Pyridoxal 5-Phosphate,Pyridoxal-P,Phosphate, Pyridoxal,Pyridoxal 5 Phosphate,Pyridoxal P
D004912 Erythrocytes Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN. Blood Cells, Red,Blood Corpuscles, Red,Red Blood Cells,Red Blood Corpuscles,Blood Cell, Red,Blood Corpuscle, Red,Erythrocyte,Red Blood Cell,Red Blood Corpuscle
D005954 Glucosephosphate Dehydrogenase Glucose-6-Phosphate Dehydrogenase,Dehydrogenase, Glucose-6-Phosphate,Dehydrogenase, Glucosephosphate,Glucose 6 Phosphate Dehydrogenase
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D006868 Hydrolysis The process of cleaving a chemical compound by the addition of a molecule of water.
D000345 Affinity Labels Analogs of those substrates or compounds which bind naturally at the active sites of proteins, enzymes, antibodies, steroids, or physiological receptors. These analogs form a stable covalent bond at the binding site, thereby acting as inhibitors of the proteins or steroids. Affinity Labeling Reagents,Labeling Reagents, Affinity,Labels, Affinity,Reagents, Affinity Labeling
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
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino

Related Publications

L Camardella, and C Caruso, and B Rutigliano, and M Romano, and G Di Prisco, and F Descalzi-Cancedda
December 1981, Biochemical and biophysical research communications,
L Camardella, and C Caruso, and B Rutigliano, and M Romano, and G Di Prisco, and F Descalzi-Cancedda
May 1970, The Journal of biological chemistry,
L Camardella, and C Caruso, and B Rutigliano, and M Romano, and G Di Prisco, and F Descalzi-Cancedda
February 2001, Journal of neurochemistry,
L Camardella, and C Caruso, and B Rutigliano, and M Romano, and G Di Prisco, and F Descalzi-Cancedda
June 1971, European journal of biochemistry,
L Camardella, and C Caruso, and B Rutigliano, and M Romano, and G Di Prisco, and F Descalzi-Cancedda
April 1971, Biochemical and biophysical research communications,
L Camardella, and C Caruso, and B Rutigliano, and M Romano, and G Di Prisco, and F Descalzi-Cancedda
November 1985, Biochemical and biophysical research communications,
L Camardella, and C Caruso, and B Rutigliano, and M Romano, and G Di Prisco, and F Descalzi-Cancedda
December 1989, Biochimica et biophysica acta,
L Camardella, and C Caruso, and B Rutigliano, and M Romano, and G Di Prisco, and F Descalzi-Cancedda
July 1966, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.),
L Camardella, and C Caruso, and B Rutigliano, and M Romano, and G Di Prisco, and F Descalzi-Cancedda
April 1988, Archives of biochemistry and biophysics,
L Camardella, and C Caruso, and B Rutigliano, and M Romano, and G Di Prisco, and F Descalzi-Cancedda
April 1977, Archives of biochemistry and biophysics,
Copied contents to your clipboard!