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Literature summary for 1.1.1.298 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 1.1.1.298

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Erythrobacter dokdonensis A0A1A7BFR5 Porphyrobacter dokdonensis
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Erythrobacter dokdonensis DSW-74 A0A1A7BFR5 Porphyrobacter dokdonensis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
malonate semialdehyde + NADPH + H+
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 Erythrobacter dokdonensis 3-hydroxypropanoate + NADP+
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 ?
malonate semialdehyde + NADPH + H+
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 Erythrobacter dokdonensis DSW-74 3-hydroxypropanoate + NADP+
-
 ?
additional information the bifunctional malonyl-CoA reductase catalyzes the formation of malonate semialdehyde from malonyl-CoA, EC 1.2.1.75, and the reduction of malonate semialdehyde to 3-hydroxypropionate, molecular mechanism of the conversion of malonyl-CoA to 3-HP in the bacterial 3-HP pathway, substrate binding docking simulations, overview Erythrobacter dokdonensis ?
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additional information the bifunctional malonyl-CoA reductase catalyzes the formation of malonate semialdehyde from malonyl-CoA, EC 1.2.1.75, and the reduction of malonate semialdehyde to 3-hydroxypropionate, 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 ?
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Subunits

Subunits Comment Organism
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
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 Erythrobacter dokdonensis
malonate semialdehyde reductase
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 Erythrobacter dokdonensis
MCR
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 Erythrobacter dokdonensis
More see also EC 1.2.1.75 Erythrobacter dokdonensis
MSAR
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 Erythrobacter dokdonensis

Cofactor

Cofactor Comment Organism Structure
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