Biology:Succinate-semialdehyde dehydrogenase (acylating)
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Succinate-semialdehyde dehydrogenase (acylating) | |||||||||
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Identifiers | |||||||||
EC number | 1.2.1.76 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Succinate-semialdehyde dehydrogenase (acylating) (EC 1.2.1.76, succinyl-coA reductase, coenzyme-A-dependent succinate-semialdehyde dehydrogenase) is an enzyme with systematic name succinate semialdehyde:NADP+ oxidoreductase (CoA-acylating).[1][2][3] This enzyme catalyses the following chemical reaction
- succinate semialdehyde + CoA + NADP+ [math]\displaystyle{ \rightleftharpoons }[/math] succinyl-CoA + NADPH + H+
Catalyses the NADPH-dependent reduction of succinyl-CoA to succinate semialdehyde.
References
- ↑ "Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri". European Journal of Biochemistry 212 (1): 121–7. February 1993. doi:10.1111/j.1432-1033.1993.tb17641.x. PMID 8444151.
- ↑ "Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp". Journal of Bacteriology 188 (24): 8551–9. December 2006. doi:10.1128/JB.00987-06. PMID 17041055. PMC 1698253. http://oceanrep.geomar.de/6268/1/J.%20Bacteriol.-2006-Alber-8551-9.pdf.
- ↑ "A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea". Science 318 (5857): 1782–6. December 2007. doi:10.1126/science.1149976. PMID 18079405.
External links
- Succinate-semialdehyde+dehydrogenase+(acylating) at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/Succinate-semialdehyde dehydrogenase (acylating).
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