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Literature summary for 1.3.3.6 extracted from

  • Haddouche, R.; Delessert, S.; Sabirova, J.; Neuveglise, C.; Poirier, Y.; Nicaud, J.M.
    Roles of multiple acyl-CoA oxidases in the routing of carbon flow towards beta-oxidation and polyhydroxyalkanoate biosynthesis in Yarrowia lipolytica (2010), FEMS Yeast Res., 10, 917-927.
    View publication on PubMed
Search for more literature for 1.3.3.6

Cloned(Commentary)

Cloned (Comment) Organism
genes POX1-POX6, heterologous co-expression of the different isozymes with polyhydroxyalkanoate synthase (phaC) of Pseudomonas aeruginosa in Yarrowia lipolytica strains, subcloning in Escherichia coli Yarrowia lipolytica

Organism

Organism UniProt Comment Textmining
Yarrowia lipolytica
-
 six acyl-CoA oxidase isoenzymes encoded by genes POX1-POX6
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Yarrowia lipolytica W29 / ATCC 20460
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 six acyl-CoA oxidase isoenzymes encoded by genes POX1-POX6
-

Synonyms

Synonyms Comment Organism
Acyl-CoA oxidase
-
 Yarrowia lipolytica
AOX
-
 Yarrowia lipolytica
Aox3p
-
 Yarrowia lipolytica

General Information

General Information Comment Organism
metabolism the isozymes are involved in the beta-oxidation in peroxisomes. Aox3p function is responsible for 90% and 75% of the total polyhydroxyalkanoate produced from either C9:0 or C13:0 fatty acid, respectively, whereas Aox5p encodes the main Aox involved in the biosynthesis of 70% of polyhydroxyalkanoate from C9:0 fatty acid. Other Aox isozymes, such as Aox1p, Aox2p, Aox4p and Aox6p, play no significant role in PHA biosynthesis, independent of the chain length of the fatty acid used, leaky-hose pipe beta-oxidation cycle model in Yarrowia lipolytica, overview Yarrowia lipolytica