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Literature summary extracted from

  • Tamazian, G.; Ho Chang, J.; Knyazev, S.; Stepanov, E.; Kim, K.J.; Porozov, Y.
    Modeling conformational redox-switch modulation of human succinic semialdehyde dehydrogenase (2015), Proteins, 83, 2217-2229 .
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.2.1.24 mitochondrial matrix
-
 Homo sapiens 5759
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.24 succinate semialdehyde + NAD+ + H2O Homo sapiens
-
 succinate + NADH + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.24 Homo sapiens P51649
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.24 succinate semialdehyde + NAD+ + H2O
-
 Homo sapiens succinate + NADH + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.24 More human SSADH is active in the reduced state but not in the oxidized state because of disulfide bonding between Cys340 and Cys342 residues. Oxidation induces a large conformational change in the dynamic catalytic loop that consists of 11 residues, including the two cysteines that connect helix alpha8 and strand beta13. As a result, the loop blocks both substrate succinate semialdehyde and cofactor NAD+ binding. Human SSADH activity is regulated by redox-switch modulation, which depends on reversible intra-disulfide binding to the dynamic catalytic loop. Simulations, and protein transformation and configuration modelling to explain the dynamic redox modulation, method optimization, detailed overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.2.1.24 succinic semialdehyde dehydrogenase
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.24 additional information human SSADH is active in the reduced state but not in the oxidized state because of disulfide bonding between Cys340 and Cys342 residues. Oxidation induces a large conformational change in the dynamic catalytic loop that consists of 11 residues, including the two cysteines that connect helix alpha8 and strand beta13. As a result, the loop blocks both substrate succinate semialdehyde and cofactor NAD+ binding Homo sapiens
1.2.1.24 NAD+
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.2.1.24 metabolism the enzyme is involved in the metabolism of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) Homo sapiens
1.2.1.24 additional information human SSADH intrinsic regulatory mechanism, redox-switch modulation, by which large conformational changes are brought about in the catalytic loop through disulfide bonding, enzyme molecular structure, overview Homo sapiens