succinate-semialdehyde dehydrogenase binding

Definition

Target type: molecularfunction

Binding to succinate-semialdehyde dehydrogenase. [GOC:mah]

Succinate-semialdehyde dehydrogenase (SSADH) is a key enzyme in the gamma-aminobutyric acid (GABA) shunt, a metabolic pathway that plays a crucial role in amino acid metabolism, particularly in the brain. SSADH catalyzes the irreversible oxidation of succinic semialdehyde (SSA) to succinate, a step critical for the detoxification of GABA. This binding process is essential for the enzymatic activity of SSADH, ensuring the efficient conversion of SSA to succinate. The binding interaction between SSADH and SSA involves the active site of the enzyme, where specific amino acid residues interact with the substrate. The precise mechanism of this binding involves the formation of hydrogen bonds and hydrophobic interactions between the enzyme and the substrate, leading to a stable enzyme-substrate complex. This complex facilitates the transfer of electrons from SSA to the enzyme's cofactor, NAD+, resulting in the formation of succinate and NADH. The binding event is highly specific, with SSADH demonstrating a strong preference for SSA over other substrates. Disruptions in the binding process, caused by genetic mutations or environmental factors, can lead to a buildup of SSA in the body, resulting in the neurodevelopmental disorder SSADH deficiency.'
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Proteins (1)

Compounds (16)