Literature summary for 1.2.1.24 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 .

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Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P51649	-	-

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
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

Synonyms	Comment	Organism
succinic semialdehyde dehydrogenase	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
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
NAD+	-	Homo sapiens

General Information

General Information	Comment	Organism
metabolism	the enzyme is involved in the metabolism of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA)	Homo sapiens
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

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Release 2023.1 (January 2023)