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Literature summary for 1.3.3.6 extracted from

  • Zeng, J.; Liu, Y.; Wu, L.; Li, D.
    Mutation of Tyr375 to Lys375 allows medium-chain acyl-CoA dehydrogenase to acquire acyl-CoA oxidase activity (2007), Biochim. Biophys. Acta, 1774, 1628-1634.
    View publication on PubMed
Search for more literature for 1.3.3.6

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.03
-
 hexanoyl-CoA in 50 mM phosphate buffer, pH 7.4, at 30°C Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
 SDS-PAGE Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
nickel metal-affinity resin column chromatography Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hexanoyl-CoA + O2
-
 Rattus norvegicus (2E)-hex-2-enoyl-CoA + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
ACO I
-
 Rattus norvegicus
MCAD Y375K Y375K mutant of medium-chain acyl-CoA dehydrogenase that exhibits acyl-CoA oxidase activity Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.089
-
 hexanoyl-CoA in 50 mM phosphate buffer, pH 7.4, at 30°C Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Rattus norvegicus