Succinate-semialdehyde dehydrogenase

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succinate-semialdehyde dehydrogenase
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Succinate semialdehyde dehydrogenase dodekamer, Human
Identifiers
EC number1.2.1.24
CAS number9028-95-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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[edit]

  1. ^ 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.

Further reading[edit]

  • ALBERS RW, KOVAL GJ (1961). "Succinic semialdehyde dehydrogenase: purification and properties of the enzyme from monkey brain". Biochim. Biophys. Acta. 52: 29&ndash, 35. doi:10.1016/0006-3002(61)90900-3. PMID 13860092.