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3-hydroxypropionate dehydrogenase (NADP+)

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3-hydroxypropionate dehydrogenase (NADP+)
Identifiers
EC no.1.1.1.298
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3-hydroxypropionate dehydrogenase (NADP+) (EC 1.1.1.298) is an enzyme with systematic name 3-hydroxypropionate:NADP+ oxidoreductase.[1][2][3] This enzyme catalyses the following chemical reaction

3-hydroxypropionate + NADP+ malonate semialdehyde + NADPH + H+

This enzyme catalyses the reduction of malonate semialdehyde to 3-hydroxypropionate, which is a key step in the 3-hydroxypropionate and the 3-hydroxypropionate/4-hydroxybutyrate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the upstream reaction in the pathway, EC 1.2.1.75. Different from EC 1.1.1.59, 3-hydroxypropionate dehydrogenase (NAD+), by cofactor preference.

References

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  1. ^ Strauss G, Fuchs G (August 1993). "Enzymes of a novel autotrophic CO2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle". European Journal of Biochemistry. 215 (3): 633–43. doi:10.1111/j.1432-1033.1993.tb18074.x. PMID 8354269.
  2. ^ Berg IA, Kockelkorn D, Buckel W, Fuchs G (December 2007). "A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea". Science. 318 (5857): 1782–6. doi:10.1126/science.1149976. PMID 18079405.
  3. ^ Hügler M, Menendez C, Schägger H, Fuchs G (May 2002). "Malonyl-coenzyme A reductase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO(2) fixation". Journal of Bacteriology. 184 (9): 2404–10. doi:10.1128/jb.184.9.2404-2410.2002. PMC 134993. PMID 11948153.
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