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In enzymology, a succinate-semialdehyde dehydrogenase (SSADH) (EC 1.2.1.24) is an enzyme that catalyzes the chemical reaction

succinate semialdehyde + NAD⁺ + H₂O ⇌ succinate + NADH + 2 H⁺

The 3 substrates of this enzyme are succinate semialdehyde, NAD⁺, and H₂O, whereas its 3 products are succinate, NADH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is succinate-semialdehyde:NAD+ oxidoreductase. Other names in common use include succinate semialdehyde dehydrogenase, succinic semialdehyde dehydrogenase, succinyl semialdehyde dehydrogenase, and succinate semialdehyde:NAD+ oxidoreductase. This enzyme participates in glutamate and butyrate metabolism.

Succinate-semialdehyde dehydrogenase is found in organisms ranging across the tree of life from bacteria to humans. It is important in the degradation of γ-aminobutyric acid in humans, and deficiency of the enzyme causes serious health effects (succinic semialdehyde dehydrogenase deficiency).

In bacteria, the enzyme is also involved in γ-aminobutyric acid degradation, but can be recruited to facilitate other functions, such as converting succinate-semialdehyde formed during fission of the pyridine ring to succinic acid for entry into the Krebs Cycle.^[1]

References

^ Sims GK, Sommers LE, Konopka A (May 1986). "Degradation of Pyridine by Micrococcus luteus Isolated from Soil". Appl. Environ. Microbiol. 51 (5): 963–8. PMC 238995 . PMID 16347070.

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English Journal

Hypoxia and GABA shunt activation in the pathogenesis of Alzheimer's disease.

Salminen A1, Jouhten P2, Sarajärvi T3, Haapasalo A4, Hiltunen M5.
Neurochemistry international.Neurochem Int.2015 Nov 23. pii: S0197-0186(15)30068-1. doi: 10.1016/j.neuint.2015.11.005. [Epub ahead of print]
We have previously observed that the conversion of mild cognitive impairment to definitive Alzheimer's disease (AD) is associated with a significant increase in the serum level of 2,4-dihydroxybutyrate (2,4-DHBA). The metabolic generation of 2,4-DHBA is linked to the activation of the γ-aminobutyri
PMID 26617286

E1 of α-ketoglutarate dehydrogenase defends Mycobacterium tuberculosis against glutamate anaplerosis and nitroxidative stress.

Maksymiuk C1, Balakrishnan A1, Bryk R1, Rhee KY2, Nathan CF3.
Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2015 Oct 27;112(43):E5834-43. doi: 10.1073/pnas.1510932112. Epub 2015 Oct 1.
Enzymes of central carbon metabolism (CCM) in Mycobacterium tuberculosis (Mtb) make an important contribution to the pathogen's virulence. Evidence is emerging that some of these enzymes are not simply playing the metabolic roles for which they are annotated, but can protect the pathogen via additio
PMID 26430237

Engineering the intracellular metabolism of Escherichia coli to produce gamma-aminobutyric acid by co-localization of GABA shunt enzymes.

Pham VD1, Somasundaram S1, Lee SH2, Park SJ3, Hong SH4.
Biotechnology letters.Biotechnol Lett.2015 Oct 17. [Epub ahead of print]
OBJECTIVES: To direct the carbon flux from Krebs cycle into the gamma-aminobutyric acid (GABA) shunt pathway for the production of GABA by protein scaffold introduction in Escherichia coli.RESULTS: Escherichia coli was engineered to produce GABA from glucose by the co-localization of enzymes succina
PMID 26476527

Japanese Journal

Archaeal Aldehyde Dehydrogenase ST0064 from Sulfolobus tokodaii, a Paralog of Non-Phosphorylating Glyceraldehyde-3-phosphate Dehydrogenase, Is a Succinate Semialdehyde Dehydrogenase

Bioscience, biotechnology, and biochemistry 77(6), 1344-1348, 2013-06-23
NAID 10031184711

Accumulation of gamma-aminobutyrate (GABA) caused by heat-drying and expression of related genes in immature vegetable soybean (edamame)

Breeding science 63(2), 205-210, 2013-06-01
NAID 10031173712

Suppression of γ-Aminobutyric Acid (GABA) Transaminases Induces Prominent GABA Accumulation, Dwarfism and Infertility in the Tomato (Solanum lycopersicum L. )

Plant and cell physiology 54(5), 793-807, 2013-05-01
NAID 10031177056

「コハク酸セミアルデヒドデヒドロゲナーゼ」

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PMC	articles
PubMed	articles
NCBI	proteins

succinate-semialdehyde dehydrogenase
	Succinate semialdehyde dehydrogenase dodekamer, Human
Identifiers
EC number	1.2.1.24
CAS number	9028-95-9
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
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PMC	articles
PubMed	articles
NCBI	proteins

　　[★]

英: succinate-semialdehyde dehydrogenase
関: コハク酸セミアルデヒド脱水素酵素

「succinate」

　　[★] コハク酸、コハク酸塩、コハク酸エステル, succinic acid

「dehydrogenase」

　　[★] 脱水素酵素デヒドロゲナーゼ

「dehydrogenases」