Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.3.8.1 extracted from

  • Mahler, H.R.
    Studies on the fatty acid oxidization system of animal tissues. IV. The prosthetic group of butyryl coenzyme A dehydrogenase (1954), J. Biol. Chem., 206, 13-26.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
CN- activates the enzyme in reaction with ferricytochrome c or ferricyanide as electron acceptors, but not with flavin D or FAd Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
4-chloromercuribenzoate 0.1 mM, 40% inhibition Bos taurus
4-chloromercuribenzoate inhibition is reversible by glutathione Sus scrofa
Hg2+
-
Sus scrofa
additional information no inhibition by CN- Sus scrofa

Metals/Ions

Metals/Ions Comment Organism Structure
copper 2 mol copper /mol FAD, cupric ion can be removed by dialysis against cyanide, copper is not involved in redox reaction Bos taurus
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 Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
120000 220000 gel filtration Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
butanoyl-CoA + oxidized acceptor Sus scrofa
-
crotonyl-CoA + reduced acceptor
-
r

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
butanoyl-CoA + oxidized acceptor
-
Sus scrofa crotonyl-CoA + reduced acceptor
-
r
additional information no activity with octanoyl-CoA and acetyl-CoA Sus scrofa ?
-
?

Synonyms

Synonyms Comment Organism
butyryl CoA dehydrogenase
-
Sus scrofa
butyryl coenzyme A dehydrogenase
-
Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25 38 assay at Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Sus scrofa

Cofactor

Cofactor Comment Organism Structure
FAD about 5 or 6 FAD molecules per enzyme molecule Bos taurus
FAD enzyme-bound, flavin D Sus scrofa
ferricytochrome c
-
Sus scrofa
riboflavin enzyme-bound Sus scrofa