Succinate-semialdehyde dehydrogenase: Difference between revisions

Revision as of 16:14, 15 September 2019

Function

Succinate-semialdehyde dehydrogenase (SSD) catalyzes the conversion of succinate semialdehyde, NAD+ and water to succinate, NADH and H+. SSD participates in glutamate and butyrate metabolism^[1].

Disease

SSD deficiency is a disorder of GABA metabolism with symptoms of seizures, delayed development and hypotonia^[2].

Structural highlights

The active site of SSD contains the and the ^[3]. Water molecules are shown as red spheres. .

Structure of succinate-semialdehyde dehydrogenase complex with NADPH and succinate semialdehyde (PDB code 3vz3).

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3D structures of succinate-semialdehyde dehydrogenase3D structures of succinate-semialdehyde dehydrogenase

Updated on 15-September-2019

ReferencesReferences

↑ JAKOBY WB, SCOTT EM. Aldehyde oxidation. III. Succinic semialdehyde dehydrogenase. J Biol Chem. 1959 Apr;234(4):937-40. PMID:13654295
↑ Gordon N. Succinic semialdehyde dehydrogenase deficiency (SSADH) (4-hydroxybutyric aciduria, gamma-hydroxybutyric aciduria). Eur J Paediatr Neurol. 2004;8(5):261-5. PMID:15341910 doi:http://dx.doi.org/10.1016/j.ejpn.2004.06.004
↑ Yuan Z, Yin B, Wei D, Yuan YR. Structural basis for cofactor and substrate selection by cyanobacterium succinic semialdehyde dehydrogenase. J Struct Biol. 2013 May;182(2):125-35. doi: 10.1016/j.jsb.2013.03.001. Epub 2013 , Mar 13. PMID:23500184 doi:10.1016/j.jsb.2013.03.001

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Michal Harel, Alexander Berchansky, Joel L. Sussman

[1] JAKOBY WB, SCOTT EM. Aldehyde oxidation. III. Succinic semialdehyde dehydrogenase. J Biol Chem. 1959 Apr;234(4):937-40. PMID:13654295

[2] Gordon N. Succinic semialdehyde dehydrogenase deficiency (SSADH) (4-hydroxybutyric aciduria, gamma-hydroxybutyric aciduria). Eur J Paediatr Neurol. 2004;8(5):261-5. PMID:15341910 doi:http://dx.doi.org/10.1016/j.ejpn.2004.06.004

[3] Yuan Z, Yin B, Wei D, Yuan YR. Structural basis for cofactor and substrate selection by cyanobacterium succinic semialdehyde dehydrogenase. J Struct Biol. 2013 May;182(2):125-35. doi: 10.1016/j.jsb.2013.03.001. Epub 2013 , Mar 13. PMID:23500184 doi:10.1016/j.jsb.2013.03.001

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 == Structural highlights ==
-The active site of SSD contains the <scene name='59/590825/Cv/4'>substrate succinate semialdehyde</scene> and the <scene name='59/590825/Cv/7'>cofactor NADP</scene><ref>PMID:23500184</ref>. <scene name='59/590825/Cv/9'>Whole binding site</scene>.
+The active site of SSD contains the <scene name='59/590825/Cv/4'>substrate succinate semialdehyde</scene> and the <scene name='59/590825/Cv/11'>cofactor NADP</scene><ref>PMID:23500184</ref>. Water molecules are shown as red spheres. <scene name='59/590825/Cv/12'>Whole binding site</scene>.
 </StructureSection>