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Literature summary for 1.3.8.1 extracted from

  • Engel, P.C.
    Butyryl-CoA dehydrogenase from Megasphaera elsdenii (1981), Methods Enzymol., 71, 359-366.
No PubMed abstract available

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-butenoyl-CoA + reduced electron transfer flavoprotein Megasphaera elsdenii enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro butanoyl-CoA + electron transfer protein
-
r
2-hexenoyl-CoA + reduced electron transfer flavoprotein Megasphaera elsdenii enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro hexanoyl-CoA + electron transfer protein
-
r
2-pentenoyl-CoA + reduced electron transfer flavoprotein Megasphaera elsdenii enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro pentanoyl-CoA + electron transfer protein
-
r
2-propenoyl-CoA + reduced electron transfer flavoprotein Megasphaera elsdenii enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro propanoyl-CoA + electron transfer protein
-
r

Organism

Organism UniProt Comment Textmining
Megasphaera elsdenii
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-
-

Storage Stability

Storage Stability Organism
short term: 4°C, 0.1 M potassium phosphate buffer, pH 7, 0.02% sodium azide or 0.002% chlorhexidine, long term: frozen in ammonium sulfate Megasphaera elsdenii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-butenoyl-CoA + reduced electron transfer flavoprotein enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro Megasphaera elsdenii butanoyl-CoA + electron transfer protein
-
r
2-hexenoyl-CoA + reduced electron transfer flavoprotein enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro Megasphaera elsdenii hexanoyl-CoA + electron transfer protein
-
r
2-pentenoyl-CoA + reduced electron transfer flavoprotein enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro Megasphaera elsdenii pentanoyl-CoA + electron transfer protein
-
r
2-propenoyl-CoA + reduced electron transfer flavoprotein enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro Megasphaera elsdenii propanoyl-CoA + electron transfer protein
-
r
3-hydroxybutyryl-CoA + acceptor
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Megasphaera elsdenii acetoacetyl-CoA + reduced acceptor
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?
butyryl-CoA + electron acceptor terminal electron acceptor 2,6-dichlorophenol-indophenol Megasphaera elsdenii 2-butenoyl-CoA + reduced acceptor
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?
butyryl-CoA + electron acceptor terminal electron acceptor iodonitrotetrazolium chloride Megasphaera elsdenii 2-butenoyl-CoA + reduced acceptor
-
?
butyryl-CoA + electron acceptor intermediate electron acceptor phenazine methosulfate Megasphaera elsdenii 2-butenoyl-CoA + reduced acceptor
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?
cyclobutanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
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Megasphaera elsdenii cyclo-2-butenecarboxyl-CoA + reduced acceptor
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?
cyclopentanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
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Megasphaera elsdenii cyclo-2-pentenecarboxyl-CoA + reduced acceptor
-
?

Cofactor

Cofactor Comment Organism Structure
FAD tightly bound Megasphaera elsdenii
FAD 1 mol per mol of subunit Megasphaera elsdenii