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Enzyme Nomenclature
Information on EC 1.2.1.75 - malonyl-CoA reductase (malonate semialdehyde-forming)
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
1.2.1.75
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RECOMMENDED NAME
GeneOntology No.
malonyl-CoA reductase (malonate semialdehyde-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
malonate semialdehyde + CoA + NADP+ = malonyl-CoA + NADPH + H+
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-
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malonate semialdehyde + CoA + NADP+ = malonyl-CoA + NADPH + H+
the protein acts as rigid template to press CoA and NADP into similar S-shaped, superimposable forms
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malonate semialdehyde + CoA + NADP+ = malonyl-CoA + NADPH + H+
the protein acts as rigid template to press CoA and NADP into similar S-shaped, superimposable forms
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
malonate semialdehyde:NADP+ oxidoreductase (malonate semialdehyde-forming)
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].
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CAS REGISTRY NUMBER
COMMENTARY
429691-13-4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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the enzyme participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea
physiological function
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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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
malonate semialdehyde + coenzyme A + NADP+
malonyl-CoA + NADPH + H+
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-
-
r
malonyl-CoA + NADPH + H+
malonate semialdehyde + NADP+ + CoA
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-
-
-
?
succinate semialdehyde + coenzyme A + NADP+
succinyl-CoA + NADPH + H+
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-
-
r
succinyl-CoA + NADPH + H+
succinate semialdehyde + coenzyme A + NADP+
at 25% of the rate with malonyl-CoA
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r
additional information
?
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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
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malonyl-CoA + NADPH + H+
malonate semialdehyde + CoA
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-
-
?
malonyl-CoA + NADPH + H+
malonate semialdehyde + CoA + NADP+
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-
-
-
?
malonyl-CoA + NADPH + H+
malonate semialdehyde + CoA + NADP+
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structural analysis reveals an unexpected reaction cycle in which NADP+ and CoA successively occupy identical binding sites, proposed reaction mechanism
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?
malonyl-CoA + NADPH + H+
malonate semialdehyde + CoA + NADP+
structural analysis reveals an unexpected reaction cycle in which NADP+ and CoA successively occupy identical binding sites, proposed reaction mechanism
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-
?
malonyl-CoA + NADPH + H+
malonate semialdehyde + coenzyme A + NADP+
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-
-
-
?
malonyl-CoA + NADPH + H+
malonate semialdehyde + coenzyme A + NADP+
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-
-
r
succinyl-CoA + NADPH + H+
succinic semialdehyde + CoA
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-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39000
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or dimer, 4 * 39000, calculated, 4 * 45000, SDS-PAGE, enzyme contains bound RNA; or tetramer, 2 * 39000, calculated, 2 * 45000, SDS-PAGE, enzyme contains bound RNA
45000
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or dimer, 4 * 39000, calculated, 4 * 45000, SDS-PAGE, enzyme contains bound RNA; or tetramer, 2 * 39000, calculated, 2 * 45000, SDS-PAGE, enzyme contains bound RNA
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
tetramer
additional information
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enzyme in its native state is associated with small RNA
dimer
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or tetramer, 2 * 39000, calculated, 2 * 45000, SDS-PAGE, enzyme contains bound RNA
tetramer
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or dimer, 4 * 39000, calculated, 4 * 45000, SDS-PAGE, enzyme contains bound RNA
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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
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Escherichia coli Rosetta 2 cells transformed with pTrc99A-Mcr plasmid harbouring mcr gene from Sulfolobus tokodaii
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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
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in heterotropically grown cells, activity is downregulated to 40 nmol per min and mg
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
additional information
synthesis
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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
synthesis
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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
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additional information
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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
additional information
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
synthesis
biotechnology
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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
biotechnology
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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
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synthesis
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MCR is of biotechnological interest for the synthesis of polyester building blocks
synthesis
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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
synthesis
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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
synthesis
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MCR is of biotechnological interest for the synthesis of polyester building blocks
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.75)
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