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

EC NUMBER
COMMENTARY hide
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 hide
ORGANISM
UNIPROT
LITERATURE
malonate semialdehyde + CoA + NADP+ = malonyl-CoA + NADPH + H+
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-hydroxypropanoate cycle
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3-hydroxypropanoate/4-hydroxybutanate cycle
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Carbon fixation pathways in prokaryotes
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glyoxylate assimilation
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Metabolic pathways
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Propanoate metabolism
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CO2 fixation in Crenarchaeota
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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].
CAS REGISTRY NUMBER
COMMENTARY hide
429691-13-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
malonate semialdehyde + coenzyme A + NADP+
malonyl-CoA + NADPH + H+
show the reaction diagram
-
-
-
r
malonyl-CoA + NADPH + H+
malonate semialdehyde + CoA
show the reaction diagram
malonyl-CoA + NADPH + H+
malonate semialdehyde + CoA + NADP+
show the reaction diagram
malonyl-CoA + NADPH + H+
malonate semialdehyde + coenzyme A + NADP+
show the reaction diagram
malonyl-CoA + NADPH + H+
malonate semialdehyde + NADP+ + CoA
show the reaction diagram
-
-
-
-
?
succinate semialdehyde + coenzyme A + NADP+
succinyl-CoA + NADPH + H+
show the reaction diagram
-
-
-
r
succinyl-CoA + NADPH + H+
succinate semialdehyde + coenzyme A + NADP+
show the reaction diagram
at 25% of the rate with malonyl-CoA
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-
r
succinyl-CoA + NADPH + H+
succinic semialdehyde + CoA
show the reaction diagram
additional information
?
-
-
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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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme A
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NADP+
NADPH
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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stimulation in decreasing order: Fe2+, Ca2+, Mg2+
Fe2+
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stimulation in decreasing order: Fe2+, Ca2+, Mg2+
Mn2+
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2fold stimulation at 5 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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0.5 mM, 85% inhibition
iodoacetamide
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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2fold stimulation at 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.1
malonyl-CoA
0.025
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 50
malonyl-CoA
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
iodoacetamide
Sulfolobus tokodaii
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pH 7.8, 65C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6
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pH 7.8, 65C
10
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55C, pH 7.8
44
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pH 7.8, 65C
80
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45C, pH 7.8
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
half-maximal activity
6.5
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half-maximal activity
8
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half-maximal activity
8.5
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half-maximal activity
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
43000
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4 * 43000, SDS-PAGE
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
145000
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2 * 145000, SDS-PAGE
150000
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gel filtration
160000
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gel filtration
300000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
tetramer
additional information
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enzyme in its native state is associated with small RNA
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, 18C
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant enzyme purified by heat precipitation at 85C 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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recombinant protein
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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 in Escherichia coli
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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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under autotrophic conditions, 10fold upregulation
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
synthesis