BIOMAT Database Logo BIOMAT Database Logo

[Presence of NADP-glycohydrolase and NADP-pyrophosphatase activity in the human palatine tonsil and their role in the inactivation of glucose-6-phosphate dehydrogenase]. 1968

E A Pallestrini, and I Lorenzoni

UI MeSH Term Description Entries
D009249 NADP Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed) Coenzyme II,Nicotinamide-Adenine Dinucleotide Phosphate,Triphosphopyridine Nucleotide,NADPH,Dinucleotide Phosphate, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide Phosphate,Nucleotide, Triphosphopyridine,Phosphate, Nicotinamide-Adenine Dinucleotide
D009699 N-Glycosyl Hydrolases A class of enzymes involved in the hydrolysis of the N-glycosidic bond of nitrogen-linked sugars. Glycoside Hydrolases, Nitrogen-linked,Hydrolases, N-Glycosyl,Nucleosidase,Nucleosidases,Nucleoside Hydrolase,Nitrogen-linked Glycoside Hydrolases,Nucleoside Hydrolases,Glycoside Hydrolases, Nitrogen linked,Hydrolase, Nucleoside,Hydrolases, N Glycosyl,Hydrolases, Nitrogen-linked Glycoside,Hydrolases, Nucleoside,N Glycosyl Hydrolases,Nitrogen linked Glycoside Hydrolases
D011755 Pyrophosphatases A group of enzymes within the class EC 3.6.1.- that catalyze the hydrolysis of diphosphate bonds, chiefly in nucleoside di- and triphosphates. They may liberate either a mono- or diphosphate. EC 3.6.1.-. Pyrophosphatase
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
D014066 Palatine Tonsil A round-to-oval mass of lymphoid tissue embedded in the lateral wall of the PHARYNX. There is one on each side of the oropharynx in the fauces between the anterior and posterior pillars of the SOFT PALATE. Tonsil,Tonsil, Palatine,Palatine Tonsils,Tonsils,Tonsils, Palatine

Related Publications

E A Pallestrini, and I Lorenzoni
Effect of NADP-glycohydrolase on glucose-6-phosphate dehydrogenase.
January 1965, Enzymologia biologica et clinica,
E A Pallestrini, and I Lorenzoni
Allosteric role of a structural NADP+ molecule in glucose-6-phosphate dehydrogenase activity.
July 2022, Proceedings of the National Academy of Sciences of the United States of America,
E A Pallestrini, and I Lorenzoni
Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase.
May 2005, Acta crystallographica. Section D, Biological crystallography,
E A Pallestrini, and I Lorenzoni
Regulation of the activity of glucose-6-phosphate dehydrogenase by NADP+ and NADPH.
September 1967, Biochimica et biophysica acta,
E A Pallestrini, and I Lorenzoni
Active molecular unit and NADP content of human glucose 6-phosphate dehydrogenase.
September 1970, Biochemical and biophysical research communications,
E A Pallestrini, and I Lorenzoni
[Succinic dehydrogenase activity of the palatine tonsil].
January 1960, Bollettino delle malattie dell'orecchio, della gola, del naso,
E A Pallestrini, and I Lorenzoni
What is the role of the second "structural" NADP+-binding site in human glucose 6-phosphate dehydrogenase?
August 2008, Protein science : a publication of the Protein Society,
E A Pallestrini, and I Lorenzoni
Proceedings: Human erythrocyte glucose 6-phosphate dehydrogenase. Content of tightly bound NADP.
January 1974, The Italian journal of biochemistry,
E A Pallestrini, and I Lorenzoni
Mechanism of inactivation of glucose-6-phosphate dehydrogenase in human erythrocytes.
October 1959, Nature,
E A Pallestrini, and I Lorenzoni
[The behavior of inorganic pyrophosphatase, triosephosphate dehydrogenase and glucose-6-phosphate dehydrogenase in oxidation of their essential SH groups].
January 1962, Acta biologica et medica Germanica,
Copied contents to your clipboard!