词条 | 3-hydroxypropionate dehydrogenase (NADP+) |
释义 |
| Name = 3-hydroxypropionate dehydrogenase (NADP+) | EC_number = 1.1.1.298 | CAS_number = | IUBMB_EC_number = 1/1/1/298 | GO_code = | image = | width = | caption = }}3-hydroxypropionate dehydrogenase (NADP+) ({{EC number|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. References1. ^{{cite journal | title = Enzymes of a novel autotrophic CO2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle |author1 = Strauss, G. |author2 =Fuchs, G. |journal = Eur. J. Biochem. |year = 1993 |volume = 215 |pages = 633–643 |pmid = 8354269 |doi=10.1111/j.1432-1033.1993.tb18074.x}} {{Alcohol oxidoreductases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}2. ^{{cite journal | title = A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea |author1 = Berg, I. A. |author2 =Kockelkorn, D. |author3 =Buckel, W. |author4 =Fuchs, G. |journal = Science |year = 2007 |volume = 318 |pages = 1782–1786 |pmid = 18079405 |doi=10.1126/science.1149976}} 3. ^{{cite journal | title = Malonyl-coenzyme A reductase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO2 fixation |author1 = Hugler, M. |author2 =Menendez, C. |author3 =Schagger, H. |author4 =Fuchs, G. |journal = J. Bacteriol. |year = 2002 |volume = 184 |pages = 2404–2410 |pmid = 11948153 |issue=9 |pmc=134993 |doi=10.1128/jb.184.9.2404-2410.2002}} External links
1 : EC 1.1.1 |
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