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Literature summary for 1.3.8.1 extracted from

  • Saenger, A.K.; Nguyen, T.V.; Vockley, J.; Stankovich, M.T.
    Thermodynamic regulation of human short-chain acyl-CoA dehydrogenase by substrate and product binding (2005), Biochemistry, 44, 16043-16053.
    View publication on PubMed

Application

Application Comment Organism
additional information overall high degree of thermodynamic modulation of wild-type SCAD, substrate binding appears to make a larger contribution than does product to thermodynamic modulation, substrate redox activation leading to a large enzyme midpoint potential shift Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
into Escherichia coli XL1 Blue, mutant expressed from Escherichia coli K19 Homo sapiens

Protein Variants

Protein Variants Comment Organism
E368Q inactivates the reductive and oxidative pathways Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44000
-
SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by gel filtration, to more than 95% purity Homo sapiens

Storage Stability

Storage Stability Organism
-80°C, phosphate buffer, pH 7.6, 20% glycerol Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
butyryl-CoA + electron transfer flavoprotein
-
Homo sapiens crotonyl-CoA + reduced electron transfer flavoprotein
-
?
hexanoyl-CoA + electron transfer flavoprotein
-
Homo sapiens 2-hexenoyl-CoA + reduced acceptor
-
?
octanoyl-CoA + electron transfer flavoprotein
-
Homo sapiens octenoyl-CoA + reduced acceptor
-
?
pentenoyl-CoA + oxidized electron transfer flavoprotein
-
Homo sapiens valeryl-CoA + reduced electron transfer flavoprotein
-
?

Synonyms

Synonyms Comment Organism
SCAD
-
Homo sapiens
short-chain acyl-CoA dehydrogenase
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD
-
Homo sapiens