PMID:20174634

Citation	Langendorf, CG, Key, TL, Fenalti, G, Kan, WT, Buckle, AM, Caradoc-Davies, T, Tuck, KL, Law, RH and Whisstock, JC (2010) The X-ray crystal structure of Escherichia coli succinic semialdehyde dehydrogenase; structural insights into NADP+/enzyme interactions. PLoS ONE 5:e9280
Abstract	In mammals succinic semialdehyde dehydrogenase (SSADH) plays an essential role in the metabolism of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) to succinic acid (SA). Deficiency of SSADH in humans results in elevated levels of GABA and gamma-Hydroxybutyric acid (GHB), which leads to psychomotor retardation, muscular hypotonia, non-progressive ataxia and seizures. In Escherichia coli, two genetically distinct forms of SSADHs had been described that are essential for preventing accumulation of toxic levels of succinic semialdehyde (SSA) in cells.
Links	PubMed PMC2823781 Online version:10.1371/journal.pone.0009280
Keywords	Animals; Binding Sites/genetics; Catalytic Domain; Crystallography, X-Ray; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Kinetics; Models, Molecular; Mutation; NADP/chemistry; NADP/metabolism; Protein Binding; Protein Conformation; Substrate Specificity; Succinate-Semialdehyde Dehydrogenase/chemistry; Succinate-Semialdehyde Dehydrogenase/genetics; Succinate-Semialdehyde Dehydrogenase/metabolism
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