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Literature summary for 1.3.1.124 extracted from

  • Alphey, M.S.; Yu, W.; Byres, E.; Li, D.; Hunter, W.N.
    Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase: enzyme-ligand interactions in a distinctive short-chain reductase active site (2005), J. Biol. Chem., 280, 3068-3077.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), expression of selenomethionine enzyme in Escherichia coli strain B834(DE3) Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type and selenomethionine enzyme, 0.001 ml of protein and of reservoir solution, the latter containing 16% PEG 4000 w/v, 0.18 M ammonium sulfate, 80 mM sodium acetate, pH 4.6, 20% glycerol, addition of 30% ethylene glycol and 4 mM NADP+ for the binary complex of enzyme with NADP+, and 120 mM substrate for the ternary complex of enzyme with NADP+ and substrate trans-trans-2,4-dienoyl-CoA, X-ray diffraction structure determination and analysis at 2.1 A and 1.75 A resolution, respectively Homo sapiens

Protein Variants

Protein Variants Comment Organism
E310A site-directed mutagenesis, effects on reaction mechanism Homo sapiens
E310Q site-directed mutagenesis, effects on reaction mechanism Homo sapiens
K214A site-directed mutagenesis, effects on reaction mechanism Homo sapiens
N148A site-directed mutagenesis, effects on reaction mechanism Homo sapiens
S210A site-directed mutagenesis, effects on reaction mechanism Homo sapiens
T197A site-directed mutagenesis, effects on reaction mechanism Homo sapiens
Y199A site-directed mutagenesis, effects on reaction mechanism Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens enzyme is the key enzyme of beta-oxidation of unsaturated fatty acid in mitochondria and to a lesser extent in peroxisomes, three accessory proteins are involved in the pathway ?
-
?
trans-trans-2,4-hexadienoyl-CoA + NADPH Homo sapiens
-
trans-3-hexenoyl-CoA + NADP+
-
r

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, to homogeneity Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
a (2E)-2-enoyl-CoA + NADP+ = a (2E,4E)-2,4-dienoyl-CoA + NADPH + H+ reaction mechanism, enzyme-ligand interactions in a distinctive short-chain reductase active site, catalytic site structure, stabilization of the dienolate reaction intermediate by Tyr199 and Asn148, and NADP+, overview Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme is the key enzyme of beta-oxidation of unsaturated fatty acid in mitochondria and to a lesser extent in peroxisomes, three accessory proteins are involved in the pathway Homo sapiens ?
-
?
trans-trans-2,4-hexadienoyl-CoA + NADPH
-
Homo sapiens trans-3-hexenoyl-CoA + NADP+
-
r
trans-trans-2,4-hexadienoyl-CoA + NADPH substrate binding mechanism and structure Homo sapiens trans-3-hexenoyl-CoA + NADP+
-
r

Subunits

Subunits Comment Organism
tetramer crystal structure Homo sapiens

Synonyms

Synonyms Comment Organism
2,4-dienoyl-CoA reductase
-
Homo sapiens
DECR
-
Homo sapiens
More enzyme belongs to the short-chain dehydrogenase/reductase family with a distinctive catalytic center Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADP+ binding mechanism and structure Homo sapiens
NADPH binding mechanism and structure Homo sapiens