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SYSTEMATIC NAME
IUBMB Comments
3-hydroxypropionate:NADP+ oxidoreductase
Catalyses the reduction of malonate semialdehyde to 3-hydroxypropanoate, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutanoate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively [1,2]. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the upstream reaction in the pathway, EC 1.2.1.75 [3]. Different from EC 1.1.1.59 [3-hydroxypropionate dehydrogenase (NAD+)] by cofactor preference.
bifunctional enzyme which catalyzes the two-step reduction from malonyl-CoA to malonate semialdehyde and from malonate semialdehyde to 3-hydroxypropionate
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
the enzyme is a 3-hydroxyisobutyrate dehydrogenase, 3-HIBADH, EC1.1.1.31, that also utilizes 3-hydroxypropionate as substrate. It catalyzes not only the oxidation of 3-hydroxyisobutyrate but also of L-serine, D-threonine, and other 3-hydroxyacid derivatives. 3-HIBADH may have the similar function to 3-hydroxypropionate dehydrogenase in vivo and be the key enzyme in an autotrophic CO2 fixation pathway, the 3-hydroxypropionate cycle
enzyme is part of an autotrophic 3-hydroxypropionate/4-hydroxybutyrate carbon dioxide assimilation pathway in Metallospaera sedula. In the pathway, CO2 is fixed with acetyl-CoA/propionyl-CoA carboxylase as key carboxylating enzyme. One acetyl-CoA and two bicarbonate molecules are reductively converted via 3-hydroxypropionate to succinyl-CoA
the enzyme is a 3-hydroxyisobutyrate dehydrogenase, 3-HIBADH, EC1.1.1.31, that also utilizes 3-hydroxypropionate as substrate. It catalyzes not only the oxidation of 3-hydroxyisobutyrate but also of L-serine, D-threonine, and other 3-hydroxyacid derivatives. 3-HIBADH may have the similar function to 3-hydroxypropionate dehydrogenase in vivo and be the key enzyme in an autotrophic CO2 fixation pathway, the 3-hydroxypropionate cycle
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
the enzyme is a 3-hydroxyisobutyrate dehydrogenase, 3-HIBADH, EC1.1.1.31, that also utilizes 3-hydroxypropionate as substrate. It catalyzes not only the oxidation of 3-hydroxyisobutyrate but also of L-serine, D-threonine, and other 3-hydroxyacid derivatives
enzyme is part of an autotrophic CO2 fixation pathway in which acetyl-CoA is carboxylated and reductively converted via 3-hydroxypropionate to propionyl-CoA. Propionyl-CoA is carboxylated and converted via succinyl-CoA and CoA transfer to malyl-CoA. Malyl-CoA is cleaved to acetyl-CoA and glyoxylate. Thereby, the first CO, acceptor molecule acetyl-CoA is regenerated, completing the cycle and the net CO, fixation product glyoxylate is released
bifunctional enzyme which catalyzes the two-step reduction from malonyl-CoA to malonate semialdehyde and from malonate semialdehyde to 3-hydroxypropionate
the malonyl-CoA reductase, MCR, from Chloroflexus aurantiacus is bifunctional, it forms malonyl-CoA from malonyl-semialdehyde, EC 1.2.1.75, and subsequently catalyzes the formation of 3-hydroxypropionate, EC 1.1.1.298
the malonyl-CoA reductase, MCR, from Chloroflexus aurantiacus is bifunctional, it forms malonyl-CoA from malonyl-semialdehyde, EC 1.2.1.75, and subsequently catalyzes the formation of 3-hydroxypropionate, EC 1.1.1.298
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
the enzyme is a 3-hydroxyisobutyrate dehydrogenase, 3-HIBADH, EC1.1.1.31, that also utilizes 3-hydroxypropionate as substrate. It catalyzes not only the oxidation of 3-hydroxyisobutyrate but also of L-serine, D-threonine, and other 3-hydroxyacid derivatives
enzyme is part of an autotrophic CO2 fixation pathway in which acetyl-CoA is carboxylated and reductively converted via 3-hydroxypropionate to propionyl-CoA. Propionyl-CoA is carboxylated and converted via succinyl-CoA and CoA transfer to malyl-CoA. Malyl-CoA is cleaved to acetyl-CoA and glyoxylate. Thereby, the first CO, acceptor molecule acetyl-CoA is regenerated, completing the cycle and the net CO, fixation product glyoxylate is released
the malonyl-CoA reductase, MCR, from Chloroflexus aurantiacus is bifunctional, it forms malonyl-CoA from malonyl-semialdehyde, EC 1.2.1.75, and subsequently catalyzes the formation of 3-hydroxypropionate, EC 1.1.1.298
the malonyl-CoA reductase, MCR, from Chloroflexus aurantiacus is bifunctional, it forms malonyl-CoA from malonyl-semialdehyde, EC 1.2.1.75, and subsequently catalyzes the formation of 3-hydroxypropionate, EC 1.1.1.298
no metal ion requirement; no metal ion requirement, no effects by 0.2 mM MnSO4, CuSO4, CaCl2, MgSO4, and FeSO4; up to 0.2 mM, no effect on activity: MnSO4, CuSO4, CaCl2, MgSO4, and FeSO4
native enzyme 100fold by ammonium sulfate fractionation, and hydrophobic interaction and anion exchange chromatography; recombinant enzyme from Escherichia coli strain BL21 96fold by ammonium sulfate fractionation, hydrophobic interaction and anion exchange chromatography, followed by ultrafiltration
gene mcr, functional expression in Escherichia coli under the T5 promoter control leading to production of 3-hydroxypropionate, coexpression with the nicotinamide nucleotide transhydrogenase that converts NADH to NADPH, required by MCR
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the specific activity of this conversion in autotrophically grown cells is 1.8 microM/min * mg protein, whereas in heterotrophically grown cells the specific activity is 0.35 microM/min * mg protein
the specific activity of this conversion in autotrophically grown cells is 1.8 microM/min * mg protein, whereas in heterotrophically grown cells the specific activity is 0.35 microM/min * mg protein
the specific activity of this conversion in autotrophically grown cells is 1.8 microM/min * mg protein, whereas in heterotrophically grown cells the specific activity is 0.35 microM/min * mg protein
Malonic semialdehyde reductase, succinic semialdehyde reductase, and succinyl-coenzyme A reductase from Metallosphaera sedula: Enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in Sulfolobales