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Literature summary extracted from

  • Luo, Y.S.; Wang, H.J.; Gopalan, K.V.; Srivastava, D.K.; Nicaud, J.M.; Chardot, T.
    Purification and characterization of the recombinant form of acyl CoA oxidase 3 from the yeast Yarrowia lipolytica (2000), Arch. Biochem. Biophys., 384, 1-8.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.3.3.6 phenol low concentration, magnitude of activation depends on the nature of the acyl-CoA substrate Yarrowia lipolytica

Application

EC Number Application Comment Organism
1.3.3.6 biotechnology potential depolluting agent by degradation of oils Yarrowia lipolytica
1.3.3.6 biotechnology several biotechnological applications: production of metabolites, such as citrate, secretion of proteins, degradation of fatty acids Yarrowia lipolytica

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.3.6 expression of His-tagged enzyme in Escherichia coli Yarrowia lipolytica

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.3.6 phenol high concentration, magnitude of inhibition depends on the nature of the acyl-CoA substrate Yarrowia lipolytica

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.3.6 0.002
-
 decanoyl-CoA recombinant enzyme Yarrowia lipolytica
1.3.3.6 0.067
-
 hexanoyl-CoA recombinant enzyme Yarrowia lipolytica

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.3.6 peroxisome
-
 Yarrowia lipolytica 5777
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.3.6 acyl-CoA + O2 Yarrowia lipolytica involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively trans-2,3-dehydroacyl-CoA + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.3.6 Yarrowia lipolytica
-
 isoform AOX3
-
1.3.3.6 Yarrowia lipolytica
-
 i.e. Yarrowia lipolytica
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.3.6 recombinant from Escherichia coli, His-tagged Yarrowia lipolytica

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.3.6 1.95
-
 recombinant enzyme, purified Yarrowia lipolytica

Storage Stability

EC Number Storage Stability Organism
1.3.3.6 -30°C, 35% glycerol (v/v), at least 1 month Yarrowia lipolytica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.3.6 acyl-CoA + O2 medium-chain-length specific Yarrowia lipolytica trans-2,3-dehydroacyl-CoA + H2O2
-
 ?
1.3.3.6 acyl-CoA + O2 involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively Yarrowia lipolytica trans-2,3-dehydroacyl-CoA + H2O2
-
 ?
1.3.3.6 decanoyl-CoA + O2
-
 Yarrowia lipolytica trans-2-decenoyl-CoA + H2O2
-
 ?
1.3.3.6 furylpropionyl-CoA + O2 also oxidizes aromatic/heterocyclic ring-substituted chromogenic substrates Yarrowia lipolytica furylacryloyl-CoA + H2O2
-
 ?
1.3.3.6 hexanoyl-CoA + O2 recombinant enzyme Yarrowia lipolytica (2E)-hex-2-enoyl-CoA + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.3.6 AOX3
-
 Yarrowia lipolytica

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.3.6 28 38 recombinant enzyme Yarrowia lipolytica

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.3.3.6 5 55 recombinant enzyme, at 5°C, 21% activity, at 55°C, 78% activity Yarrowia lipolytica

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.3.6 1.53
-
 decanoyl-CoA recombinant enzyme Yarrowia lipolytica
1.3.3.6 8.59
-
 hexanoyl-CoA recombinant enzyme Yarrowia lipolytica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.3.6 7.4
-
 recombinant enzyme Yarrowia lipolytica