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Literature summary for 1.2.1.75 extracted from

  • Son, H.F.; Kim, S.; Seo, H.; Hong, J.; Lee, D.; Jin, K.S.; Park, S.; Kim, K.J.
    Structural insight into bi-functional malonyl-CoA reductase (2020), Environ. Microbiol., 22, 752-765 .
    View publication on PubMed
Search for more literature for 1.2.1.75

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Erythrobacter dokdonensis

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization trials of the full-length MCR fail, thus production of the N-terminal domain (MCRND, Met1-Pro567) and the C-terminal domain (MCRCD, Gly568-Val1230) separately, X-ray diffraction structure determination and analysis at resolutions of 2.20 and 1.80 A, respectively, by a single-wavelength anomalous dispersion (SAD) method Erythrobacter dokdonensis
N-terminal domain, hanging drop vapor diffusion method, using 10% (w/v) PEG3350, 200 mM lithium sulfate, 100 mM Tris-HCl, pH 8.0. C-terminal domain, hanging drop vapor diffusion method, using 1.6 M lithium sulfate and 100 mM HEPES, pH 8.0 Erythrobacter dokdonensis

Protein Variants

Protein Variants Comment Organism
I798A the mutant of the C-terminal domain shows less than 30% activity as compared to the wild type enzyme Erythrobacter dokdonensis
K195A the mutant of the N-terminal domain is almost completely inactive as compared to the wild type enzyme Erythrobacter dokdonensis
K748A the mutant of the C-terminal domain is almost completely inactive as compared to the wild type enzyme Erythrobacter dokdonensis
K802A the mutant of the C-terminal domain shows about 95% activity as compared to the wild type enzyme Erythrobacter dokdonensis
K926A the mutant of the C-terminal domain shows about 90% activity as compared to the wild type enzyme Erythrobacter dokdonensis
L790A inactive Erythrobacter dokdonensis
M662A the mutant of the C-terminal domain is almost completely inactive as compared to the wild type enzyme Erythrobacter dokdonensis
N740A the mutant of the C-terminal domain shows about 15% activity as compared to the wild type enzyme Erythrobacter dokdonensis
N805A the mutant of the C-terminal domain shows less than 60% activity as compared to the wild type enzyme Erythrobacter dokdonensis
R1166A the mutant of the C-terminal domain shows less than 20% activity as compared to the wild type enzyme Erythrobacter dokdonensis
R188A the mutant of the N-terminal domain shows less than 10% activity as compared to the wild type enzyme Erythrobacter dokdonensis
R741A the mutant of the C-terminal domain shows less than 5% activity as compared to the wild type enzyme Erythrobacter dokdonensis
R780A the mutant of the C-terminal domain is almost completely inactive as compared to the wild type enzyme Erythrobacter dokdonensis
R794A the mutant of the C-terminal domain is almost completely inactive as compared to the wild type enzyme Erythrobacter dokdonensis
S726A the mutant of the C-terminal domain is almost completely inactive as compared to the wild type enzyme Erythrobacter dokdonensis
T178A the mutant of the N-terminal domain is almost completely inactive as compared to the wild type enzyme Erythrobacter dokdonensis
Y185A the mutant of the N-terminal domain shows less than 20% activity as compared to the wild type enzyme Erythrobacter dokdonensis
Y191A the mutant of the N-terminal domain shows less than 10% activity as compared to the wild type enzyme Erythrobacter dokdonensis
Y738A the mutant of the C-terminal domain shows about 10% activity as compared to the wild type enzyme Erythrobacter dokdonensis
Y744A the mutant of the C-terminal domain shows less than 5% activity as compared to the wild type enzyme Erythrobacter dokdonensis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ 1 mM used in assay conditions Erythrobacter dokdonensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
265000
-
 gel filtration Erythrobacter dokdonensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
malonate semialdehyde + NADPH + H+ Erythrobacter dokdonensis
-
 3-hydroxypropionic acid + NADP+
-
 ?
malonyl-CoA + NADPH + H+ Erythrobacter dokdonensis
-
 malonate semialdehyde + CoA + NADP+
-
 ?
malonyl-CoA + NADPH + H+ Erythrobacter dokdonensis DSW-74
-
 malonate semialdehyde + CoA + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Erythrobacter dokdonensis
-
-
-
Erythrobacter dokdonensis A0A1A7BFR5 Porphyrobacter dokdonensis
-
Erythrobacter dokdonensis DSW-74 A0A1A7BFR5 Porphyrobacter dokdonensis
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA agarose column chromatography and Sephacryl S-300 gel filtration Erythrobacter dokdonensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
malonate semialdehyde + NADPH + H+
-
 Erythrobacter dokdonensis 3-hydroxypropionic acid + NADP+
-
 ?
malonyl-CoA + NADPH + H+
-
 Erythrobacter dokdonensis malonate semialdehyde + CoA + NADP+
-
 ?
malonyl-CoA + NADPH + H+
-
 Erythrobacter dokdonensis DSW-74 malonate semialdehyde + CoA + NADP+
-
 ?
additional information the bifunctional malonyl-CoA reductase catalyzes the formation of malonate semialdehyde from malonyl-CoA, and the reduction of malonate semialdehyde to 3-hydroxypropionate, cf. EC 1.1.1.298, molecular mechanism of the conversion of malonyl-CoA to 3-HP in the bacterial 3-HP pathway, substrate binding docking simulations, overview Erythrobacter dokdonensis ?
-
-
additional information the bifunctional malonyl-CoA reductase catalyzes the formation of malonate semialdehyde from malonyl-CoA, and the reduction of malonate semialdehyde to 3-hydroxypropionate, cf. EC 1.1.1.298, molecular mechanism of the conversion of malonyl-CoA to 3-HP in the bacterial 3-HP pathway, substrate binding docking simulations, overview Erythrobacter dokdonensis DSW-74 ?
-
-

Subunits

Subunits Comment Organism
homodimer x-ray crystallography Erythrobacter dokdonensis
homodimer subunit structures and interaction analysis Erythrobacter dokdonensis
More olecular architecture of the full-length MCR, modeling, overview Erythrobacter dokdonensis

Synonyms

Synonyms Comment Organism
bi-functional malonyl-CoA reductase
-
 Erythrobacter dokdonensis
malonate semialdehyde reductase
-
 Erythrobacter dokdonensis
malonyl-CoA reductase
-
 Erythrobacter dokdonensis
MCR
-
 Erythrobacter dokdonensis
More see also EC 1.1.1.298 Erythrobacter dokdonensis
MSAR
-
 Erythrobacter dokdonensis

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Erythrobacter dokdonensis
NADPH the NADPH cofactor bound in MCR N-terminal domain is stabilized by hydrogen bonds with the side chains of Arg55, Arg59, Asp84, Asn151, Tyr744 and Lys195, and the main chains of Asn34, Leu35, Gly85, Asn111, Gly113 and Ile224, and by interaction with C-terminal resdiues by hydrogen bonds with the side chains of Ser88, Arg611, Arg612, Asp646, Tyr744 and Lys748, and the main chains of Ser588, Ala589, Ile591, Arg611, Arg612, Val647, Asn673 and Val776, cofactor binding site structure, overview Erythrobacter dokdonensis

General Information

General Information Comment Organism
evolution distribution of bifunctional MCR in bacteria and comparison with archaeal MCR and MSAR, overview Erythrobacter dokdonensis
metabolism enzymes involved in archaeal and bacterial 3-HP pathway and their structures, overview Erythrobacter dokdonensis
additional information Tyr191 is the catalytic residue, active site structure, substrate binding mode, overview. Structure comparison with the archaeal MCR from Sulfurisphaera tokodaii (StMCR) Erythrobacter dokdonensis