Requires Mg2+. Catalyses the reduction of malonyl-CoA to malonate semialdehyde, 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 some thermoacidophilic archaea, respectively [1,2]. The enzyme from Sulfolobus tokodaii has been purified, and found to contain one RNA molecule per two subunits . The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the next reaction in the pathway, EC 1.1.1.298 [3-hydroxypropionate dehydrogenase (NADP+)] .
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Requires Mg2+. Catalyses the reduction of malonyl-CoA to malonate semialdehyde, 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 some thermoacidophilic archaea, respectively [1,2]. The enzyme from Sulfolobus tokodaii has been purified, and found to contain one RNA molecule per two subunits [3]. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the next reaction in the pathway, EC 1.1.1.298 [3-hydroxypropionate dehydrogenase (NADP+)] [4].
enzyme additionally catalyzes the second reduction step of malonate semialdehyde + NADPH + H+ to 3-hydroxypropionate + NADP+. Reverse reaction starting with 3-hydroxypropionate does not require CoA and probably stops at malonate semialdehyde. No substrates are acetyl-CoA, propionyl-CoA, succinyl-CoA, or glyoxylate
structural analysis reveals an unexpected reaction cycle in which NADP+ and CoA successively occupy identical binding sites, proposed reaction mechanism
structural analysis reveals an unexpected reaction cycle in which NADP+ and CoA successively occupy identical binding sites, proposed reaction mechanism
the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
the N-terminal region of MCR (MCR-N, amino acids 1-549) and the C-terminal region of MCR (MCR-C, amino acids 550-1219) are functionally distinct. Malonyl-CoA is reduced into free intermediate malonate semialdehyde with NADPH by the MCR-C fragment, and further reduced to 3-hydroxypropionate by the MCR-N fragment, the initial reduction of malonyl-CoA being rate limiting. The TGXXXG(A)X(1-2)G and YXXXK motifs are important for enzyme activities of both MCR-N and MCR-C fragments, and the enzyme activity increases when MCR is separated into two individual fragments. The MCR-C fragment has higher affinity for malonyl-CoA and 4-times higher Kcat/Km value than MCR
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
malonyl-CoA reductase in the substrate-free state at 2.05 A resolution and in complex with NADP+ at 1.9 A resolution and in complex with CoA at 2.4 A resolution; sitting drop method, 18°C
heterologous expression of the malonyl-CoA dependent pathway genes malonyl-CoA reductase and malonate semialdehyde reductase enables Synechococcus elongatus to synthesize 3-hydroxypropionic acid to a final titer of 665 mg/l
heterologous expression of the malonyl-CoA dependent pathway genes malonyl-CoA reductase and malonate semialdehyde reductase enables Synechococcus elongatus to synthesize 3-hydroxypropionic acid to a final titer of 665 mg/l
the crystallographic data indicate how to construct a bispecific cofactor binding site and to engineer a malonyl-CoA into methylmalonyl-CoA reductase for polyester building block production
the crystallographic data indicate how to construct a bispecific cofactor binding site and to engineer a malonyl-CoA into methylmalonyl-CoA reductase for polyester building block production
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
; recombinant enzyme purified by heat precipitation at 85°C and concentration by ultrafiltration, gel filtration chromatography using a Superdex 200 HR 26/60 gel filtration column and Resource phenyl chromatography using a Resource phenyl column
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
extracts of autotrophically grown cells exhibit an NADPH-dependent succinyl-CoA reductase activity of 200 nM/min*mg of soluble protein, whereas extracts of heterotrophically grown cells exhibit an activity of 10 nM/min*mg of protein
the crystallographic data indicate how to construct a bispecific cofactor binding site and to engineer a malonyl-CoA into methylmalonyl-CoA reductase for polyester building block production
the crystallographic data indicate how to construct a bispecific cofactor binding site and to engineer a malonyl-CoA into methylmalonyl-CoA reductase for polyester building block production
the combination of Escherichia coli BL21(DE3) and pET28a carrying heterogeneous acetyl-CoA carboxylase (Acc) from Corynebacterium glutamicum and codon-optimized malonyl-CoA reductase (MCR) from Chloroflexus aurantiacus is the most efficient host-vector system for 3-hydroxypropionic acid production, and the highest concentration of 3-hydroxypropionic attained in shake flask cultivation reaches 1.80 g/l with induction at 0.25 mM IPTG and 25°C, and supplementation of NaHCO3 and biotin
integration of multiple copies of malonyl-CoA reductase MCR and of phosphorylation-deficient acetyl-CoA carboxylase ACC1 genes into the genome of yeast increases 3-hydroxypropionic acid titer fivefold in comparison with single integration. Optimizing the supply of acetyl-CoA by overexpressing native pyruvate decarboxylase PDC1, aldehyde dehydrogenase ALD6, and acetyl-CoA synthase from Salmonella enterica SEacsL641P engineering the cofactor specificity of the glyceraldehyde-3-phosphate dehydrogenase to increase the intracellular production of NADPH at the expense of NADH improves 3-hydroxypropionic acid production and reduces formation of glycerol as by-product. The final strain produces 9.8 g per L 3-hydroxypropionic acid with a yield of 13% C-mol per C-mol glucose after 100 h in carbon-limited fed-batch cultivation at pH 5
Engineering and systems-level analysis of Saccharomyces cerevisiae for production of 3-hydroxypropionic acid via malonyl-CoA reductase-dependent pathway
HOME
login
history
all enzymes
BRENDA home
History
1.2.1.75 malonyl-CoA reductase (malonate semialdehyde-forming)
more
top
Information
