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Literature summary for 1.3.3.6 extracted from

  • Kong, F.; Liang, Y.; Legeret, B.; Beyly-Adriano, A.; Blangy, S.; Haslam, R.P.; Napier, J.A.; Beisson, F.; Peltier, G.; Li-Beisson, Y.
    Chlamydomonas carries out fatty acid beta-oxidation in ancestral peroxisomes using a bona fide acyl-CoA oxidase (2017), Plant J., 90, 358-371 .
    View publication on PubMed
Search for more literature for 1.3.3.6

Cloned(Commentary)

Cloned (Comment) Organism
gene Cre05.g232002 or CrACX2, screening of a Chlamydomonas insertional mutant library identifies a strain strongly impaired in oil remobilization and defective in Cre05.g232002 (CrACX2), recombinant expression of CrACX2 in Escherichia coli. Overexpression of GFP-tagged enzyme in Chlamydomonas reinhardtii peroxisomes Chlamydomonas reinhardtii

Protein Variants

Protein Variants Comment Organism
additional information screening of a Chlamydomonas reinhardtii insertional mutant library identifies a strain strongly impaired in oil remobilization and defective in Cre05.g232002 (CrACX2), Nb7D4 is disrupted in gene Cre05.g232002. The mutant strain is defective in beta-oxidation of fatty acids and cannot grow on oleic acid. Turnover of fatty acids during diurnal growth is compromised in cracx2 mutant cells. Cellular oil content is increased by 20% in cracx2 mutants during N starvation. Phenotype, overview Chlamydomonas reinhardtii

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome fluorescent protein-tagging points to a peroxisomal location of CrACX2 Chlamydomonas reinhardtii 5777
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acyl-CoA + O2 Chlamydomonas reinhardtii
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 trans-2,3-dehydroacyl-CoA + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Chlamydomonas reinhardtii A8J3M3
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + O2
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 Chlamydomonas reinhardtii trans-2,3-dehydroacyl-CoA + H2O2
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 ?
acyl-CoA + O2 the purified recombinant CrACX2 expressed in Escherichia coli catalyzes the oxidation of fatty acyl-CoAs into trans-2-enoyl-CoA and produces H2O2 Chlamydomonas reinhardtii trans-2,3-dehydroacyl-CoA + H2O2
-
 ?
additional information CrACX2 is more active toward long chain acyl-CoAs (C18:1-, C18:0-, C20:0-, C16:0-CoAs) than to medium chain acyl-CoA (C12:0-CoA) Chlamydomonas reinhardtii ?
-
 ?

Subunits

Subunits Comment Organism
? x * 76000, SDS-PAGE Chlamydomonas reinhardtii

Synonyms

Synonyms Comment Organism
acyl-CoA dehydrogenase UniProt Chlamydomonas reinhardtii
CrACX2
-
 Chlamydomonas reinhardtii
Cre05.g232002 locus name Chlamydomonas reinhardtii

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Chlamydomonas reinhardtii

General Information

General Information Comment Organism
evolution the enzyme is a member of the acyl-CoA oxidase/dehydrogenase superfamily Chlamydomonas reinhardtii
malfunction isolation of a mutant strain strongly impaired in oil remobilization and defective in gene CrACX2, under nitrogen depletion the mutant accumulated 20% more oil than the wild-type. The cracx2 mutant is impaired in fatty acid turnover during day/night cycles. The mutant strain is defective in beta-oxidation of fatty acids and cannot grow on oleic acid. The cracx2 mutant does not over-accumulate acyl-CoAs. Phenotype, overview Chlamydomonas reinhardtii
physiological function CrACX2 is a genuine acyl-CoA oxidase, which is responsible for the first step of the peroxisomal fatty acid beta-oxidation spiral. The enzyme is required for breakdown of fatty acids during lipid remobilization Chlamydomonas reinhardtii