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Literature summary for 1.3.1.9 extracted from

  • Cai, X.; Lorraine Fuller, A.; McDougald, L.R.; Tan, X.; Cai, J.; Wang, F.; Sacchettini, J.C.; Zhu, G.
    Biochemical characterization of enoyl reductase involved in Type II fatty acid synthesis in the intestinal coccidium Eimeria tenella (Phylum Apicomplexa) (2007), FEMS Microbiol. Lett., 272, 238-244.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Eimeria tenella

Inhibitors

Inhibitors Comment Organism Structure
crotonoyl-CoA the addition of short-chain crotonoyl-CoA actually inhibits the oxidation of NADH by recombinant ENR in a dose-dependent manner Eimeria tenella
triclosan
-
Eimeria tenella

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.08832
-
NADH recombinant enzyme, in the absence of enoyl-CoA as scosubstrate, in 0.1 mM Tris-HCl buffer (pH 7.2) Eimeria tenella

Organism

Organism UniProt Comment Textmining
Eimeria tenella A3R4P1
-
-

Purification (Commentary)

Purification (Comment) Organism
amylose-resin-based affinity chromatography Eimeria tenella

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
crotonyl-CoA + NADH + H+
-
Eimeria tenella butyryl-CoA + NAD+
-
?
dodecenoyl-CoA + NADH + H+
-
Eimeria tenella dodecanoyl-CoA + NAD+
-
?
additional information the recombinant ENR expressed in bacteria is only able to oxidize NADH, but unable to transfer the electron to enoyl-CoA, possibly due to the inappropriate folding of ENR expressed in bacteria Eimeria tenella ?
-
?

Synonyms

Synonyms Comment Organism
enoyl reductase the enzyme is involved in Type II fatty acid synthesis Eimeria tenella
ENR
-
Eimeria tenella

Cofactor

Cofactor Comment Organism Structure
NADH
-
Eimeria tenella

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.00145
-
recombinant enzyme, in 0.1 mM Tris-HCl buffer (pH 7.2) Eimeria tenella triclosan