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1.3.8.1: short-chain acyl-CoA dehydrogenase

This is an abbreviated version!
For detailed information about short-chain acyl-CoA dehydrogenase, go to the full flat file.

Word Map on EC 1.3.8.1

Reaction

a short-chain acyl-CoA
+
electron-transfer flavoprotein
=
a short-chain trans-2,3-dehydroacyl-CoA
+
reduced electron-transfer flavoprotein

Synonyms

3-hydroxyacyl CoA reductase, ACADS, Acfer_0556, Acfer_1477, acyl-CoA dehydrogenase short chain, BCAD, BCD, bcd2, BcdAf, bSCAD, butyryl CoA dehydrogenase, butyryl coenzyme A dehydrogenase, butyryl-CoA dehydrogenase, butyryl-CoA dehydrogenase complex, butyryl-CoA dehydrogenase/Etf complex, CD1054, dehydrogenase, butyryl coenzyme A, EC 1.3.2.1, EC 1.3.99.2, enoyl-coenzyme A reductase, ethylene reductase, HADHSC, non-dissociating bifurcating Etf-Bcd complex, SCAD, ScdA, short chain acyl-CoA dehydrogenase, short-chain 3-hydroxyacyl-CoA dehydrogenase, short-chain acyl CoA dehydrogenase, short-chain acyl-CoA dehydrogenase, short-chain acyl-coenzyme A dehydrogenase, short-chain acylCoA dehydrogenase, unsaturated acyl coenzyme A reductase

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.8 With a flavin as acceptor
                1.3.8.1 short-chain acyl-CoA dehydrogenase

Metals Ions

Metals Ions on EC 1.3.8.1 - short-chain acyl-CoA dehydrogenase

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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
-
2 mol copper /mol FAD, cupric ion can be removed by dialysis against cyanide, copper is not involved in redox reaction
Cu2+
-
10-12 copper ions per enzyme molecule, enzyme-bound copper. The Cu2+ does not play a role in the primary reduction of the flavin-bound enzyme
Iron
-
less than 0.2 g-atom per mol protein