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| {{enzyme
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| | Name = succinate-semialdehyde dehydrogenase
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| | EC_number = 1.2.1.24
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| | CAS_number = 9028-95-9
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| | IUBMB_EC_number = 1/2/1/24
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| | GO_code = 0004777
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| In [[enzymology]], a '''succinate-semialdehyde dehydrogenase''' ({{EC number|1.2.1.24}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
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| :succinate semialdehyde + NAD<sup>+</sup> + H<sub>2</sub>O <math>\rightleftharpoons</math> succinate + NADH + 2 H<sup>+</sup>
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| The 3 [[substrate (biochemistry)|substrates]] of this enzyme are [[succinate semialdehyde]], [[nicotinamide adenine dinucleotide|NAD<sup>+</sup>]], and [[water|H<sub>2</sub>O]], whereas its 3 [[product (chemistry)|products]] are [[succinate]], [[nicotinamide adenine dinucleotide|NADH]], and [[hydrogen ion|H<sup>+</sup>]].
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| This enzyme belongs to the family of [[oxidoreductase]]s, 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.
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| Succinate-semialdehyde dehydrogenase is found in organisms ranging across the tree of life from bacteria to humans. It is important in the degradation of [[gamma-Aminobutyric acid|γ-aminobutyric acid]] in humans, and deficiency of the enzyme causes serious health effects ([[succinic semialdehyde dehydrogenase deficiency]]).
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| In bacteria, the enzyme is also involved in [[gamma-Aminobutyric acid|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]].<ref name="pmid16347070">{{cite journal | author = Sims GK, Sommers LE, Konopka A | title = Degradation of Pyridine by Micrococcus luteus Isolated from Soil | journal = Appl. Environ. Microbiol. | volume = 51 | issue = 5 | pages = 963–8 |date=May 1986 | pmid = 16347070 | pmc = 238995 | doi = | url = }}</ref>
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| ==References==
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| == Further reading ==
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| {{refbegin}}
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| * {{cite journal | author = ALBERS RW, KOVAL GJ | date = 1961 | title = Succinic semialdehyde dehydrogenase: purification and properties of the enzyme from monkey brain | journal = Biochim. Biophys. Acta. | volume = 52 | pages = 29–35 | pmid = 13860092 | doi = 10.1016/0006-3002(61)90900-3 }}
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| {{refend}}
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| {{1.2-enzyme-stub}}
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| [[Category:EC 1.2.1]] | |
| [[Category:NADH-dependent enzymes]]
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| [[Category:Enzymes of unknown structure]]
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