Succinate-semialdehyde dehydrogenase: Difference between revisions

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== Function ==
== 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<ref>PMID:13654295</ref>.
'''Succinate-semialdehyde dehydrogenase''' or '''α-ketoglutaric semialdehyde dehydrogenase''' or '''succinyl-CoA reductase''' (SSD) catalyzes the conversion of succinate semialdehyde, NAD+ and water to succinate, NADH and H+.  SSD participates in glutamate and butyrate metabolism<ref>PMID:13654295</ref>. See also [[Aldehyde dehydrogenase]].
 


== Disease ==
== Disease ==
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== Structural highlights ==
== 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>
</StructureSection>
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*Succinate-semialdehyde dehydrogenase
*Succinate-semialdehyde dehydrogenase


**[[2w8n]], [[2w8o]] – hSSD - human <br />
**[[2w8p]] – hSSD (mutant) <br />
**[[4it9]], [[3vz1]] – SySSD - ''Synechococcus''<br />
**[[4it9]], [[3vz1]] – SySSD - ''Synechococcus''<br />
**[[3vz2]] – SySSD (mutant) <br />
**[[3vz2]] – SySSD (mutant) <br />
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**[[5vbf]] – SSD – ''Burkholderia vietnamiensis''<br />
**[[5vbf]] – SSD – ''Burkholderia vietnamiensis''<br />
**[[3rh9]] – SSD – ''Marinobacter aquaeolei''<br />
**[[3rh9]] – SSD – ''Marinobacter aquaeolei''<br />
**[[2w8n]], [[2w8o]] – hSSD - human <br />
**[[2w8p]] – hSSD (mutant) <br />
**[[4ogd]] – SpSSD – ''Streptococcus pyogenes'' <br />
**[[4ogd]] – SpSSD – ''Streptococcus pyogenes'' <br />
**[[5x5t]] – AbSSD – ''Azuspirillum brasilense'' <br />


*Succinate-semialdehyde dehydrogenase complexes
*Succinate-semialdehyde dehydrogenase complexes
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**[[4oht]] – SpSSD + NADPH<br />
**[[4oht]] – SpSSD + NADPH<br />
**[[4ywu]], [[4ywv]] – SySSD + oxobutanoic acid + succinic semialdehyde<br />
**[[4ywu]], [[4ywv]] – SySSD + oxobutanoic acid + succinic semialdehyde<br />
**[[5x5u]] – AbSSD + NAD<br />
**[[8c54]] – SSD + NADH – ''Rhizobium leguminosarum'' – Cryo EM<br />
**[[8cej]] – CkSSD + mesaconyl-c1-CoA – ''Clostridium kluyveri''<br />
**[[8cek]] – CkSSD + NADPH<br />


}}
}}

Latest revision as of 12:49, 6 December 2023


Function

Succinate-semialdehyde dehydrogenase or α-ketoglutaric semialdehyde dehydrogenase or succinyl-CoA reductase (SSD) catalyzes the conversion of succinate semialdehyde, NAD+ and water to succinate, NADH and H+. SSD participates in glutamate and butyrate metabolism[1]. See also Aldehyde dehydrogenase.


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).

Drag the structure with the mouse to rotate

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

Updated on 06-December-2023

ReferencesReferences

  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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman