GTP diphosphatase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: GTP + H2O = GMP + H+ + diphosphate. [GOC:dgf, PMID:22531138, RHEA:29391]

GTP diphosphatase activity is a catalytic activity that hydrolyzes guanosine triphosphate (GTP) to guanosine diphosphate (GDP) and inorganic phosphate (Pi). This reaction is essential for many cellular processes, including signal transduction, protein synthesis, and cytoskeletal dynamics. GTP diphosphatases, also known as GTPase activating proteins (GAPs), are a diverse group of enzymes that play critical roles in regulating the activity of GTP-binding proteins (G proteins). G proteins act as molecular switches, cycling between an active GTP-bound state and an inactive GDP-bound state. GAPs accelerate the hydrolysis of GTP by G proteins, promoting their inactivation. This regulation is crucial for ensuring proper signaling and preventing uncontrolled activation of G protein-mediated pathways. GTP diphosphatases are found in all domains of life and exhibit a wide range of substrate specificities. Some GAPs act on specific G proteins, while others are more promiscuous, regulating multiple G proteins within a pathway. The catalytic mechanism of GTP diphosphatase activity involves the binding of GTP and a water molecule to the active site of the enzyme. The enzyme then facilitates the transfer of a phosphate group from GTP to water, resulting in the formation of GDP and Pi. This reaction is typically highly specific for GTP and requires the presence of a magnesium ion for optimal activity. GTP diphosphatases play a vital role in maintaining cellular homeostasis and are involved in a wide range of physiological processes, including cell growth, development, and immune response. Dysregulation of GTP diphosphatase activity can lead to various pathological conditions, such as cancer and neurodegenerative diseases.'
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Proteins (1)

Compounds (8)