ArticlePloS one2010
The X-ray crystal structure of Escherichia coli succinic semialdehyde dehydrogenase; structural insights into NADP+/enzyme interactions.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 58 citations in OpenAlex.
- A crucial active site network of titratable residues guides catalysis and NADProtein science : a publication of the Protein Society · 2025Article
- Gene replacement therapies for inherited disorders of neurotransmission: Current progress in succinic semialdehyde dehydrogenase deficiency.Journal of inherited metabolic disease · 2024Review
- Biochemical and structural elucidation of the L-carnitine degradation pathway of the human pathogenFrontiers in microbiology · 2024Article
- Molecular basis of sulfolactate synthesis by sulfolactaldehyde dehydrogenase fromChemical science · 2023Article
- Adaptive laboratory evolution accelerated glutarate production by Corynebacterium glutamicum.Microbial cell factories · 2021Article
- Succinic Semialdehyde Dehydrogenase Deficiency: In Vitro and In Silico Characterization of a Novel Pathogenic Missense Variant and Analysis of the Mutational Spectrum ofInternational journal of molecular sciences · 2020Article
- Insights into the κ/ι-carrageenan metabolism pathway of some marineCommunications biology · 2019Article
- Structure and biochemistry of phenylacetaldehyde dehydrogenase from the Pseudomonas putida S12 styrene catabolic pathway.Archives of biochemistry and biophysics · 2017Article
- NADP-Dependent Aldehyde Dehydrogenase from ArchaeonArchaea (Vancouver, B.C.) · 2016Article
- Reduction of mitochondrial protein mitoNEET [2Fe-2S] clusters by human glutathione reductase.Free radical biology & medicine · 2015Article
- Kinetic and structural characterization for cofactor preference of succinic semialdehyde dehydrogenase from Streptococcus pyogenes.Molecules and cells · 2014Article
- Structure and function of phosphonoacetaldehyde dehydrogenase: the missing link in phosphonoacetate formation.Chemistry & biology · 2014Article
- Structural basis for a cofactor-dependent oxidation protection and catalysis of cyanobacterial succinic semialdehyde dehydrogenase.The Journal of biological chemistry · 2013Article
- Crystallization and preliminary X-ray crystallographic studies of succinic semialdehyde dehydrogenase from Streptococcus pyogenes.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Succinic semialdehyde dehydrogenase: biochemical-molecular-clinical disease mechanisms, redox regulation, and functional significance.Antioxidants & redox signaling · 2011Review
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIn 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. METHODOLOGY/PRINCIPAL
findingsHere we structurally characterise SSADH encoded by the E coli gabD gene by X-ray crystallographic studies and compare these data with the structure of human SSADH. In the E. coli SSADH structure, electron density for the complete NADP+ cofactor in the binding sites is clearly evident; these data in particular revealing how the nicotinamide ring of the cofactor is positioned in each active site. CONCLUSIONS/SIGNIFICANCE: Our structural data suggest that a deletion of three amino acids in E. coli SSADH permits this enzyme to use NADP+, whereas in contrast the human enzyme utilises NAD+. Furthermore, the structure of E. coli SSADH gives additional insight into human mutations that result in disease.
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