Inhibition of erythrocyte transglutaminase by GTP

• Published in: Biochimica et biophysica acta Vol. 916; no. 1; pp. 149 - 151
• Main Authors: Bergamini, Carlo M., Signorini, Marco, Poltronieri, Licia
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 05.11.1987; Elsevier; North-Holland
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; Calcium ion activation; Enzyme latency; Enzymes and enzyme inhibitors; Erythrocyte; erythrocyte transglutaminase; Erythrocytes - drug effects; Erythrocytes - enzymology; Fundamental and applied biological sciences. Psychology; GTP; Guanine nucleotide; Guanosine Diphosphate - pharmacology; Guanosine Monophosphate - pharmacology; Guanosine Triphosphate - pharmacology; Humans; Transferases; Transglutaminase inhibition; Transglutaminases - antagonists & inhibitors; Erythrocyte; Transglutaminase inhibition; Guanine nucleotide; Enzyme latency; Calcium ion activation; GTP; Purification; Enzyme; Guanosine diphosphate; Interference; Chelation; Red blood cell; Activation; Cations; Inhibition; Protein-glutamine γ-glutamyltransferase; Latency
• ISSN: 0167-4838; 0006-3002; 1879-2588; 1878-2434
• DOI: 10.1016/0167-4838(87)90222-6

The guanine nucleotides GTP, GDP and GMP inhibit the activity of erythrocyte transglutaminase (protein-glutamine:amine γ-glutamyltransferase, EC 2.3.2.13) in a decreasing order of effectiveness. The inhibition is more apparent at low than at saturating levels of calcium ions and is not due to the chelation of Ca 2+, but to an interference with the process of activation by the cation. This inhibition is likely to contribute to the latency of erythrocyte transglutaminase in physiological conditions.