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Literature summary for 2.3.1.42 extracted from

  • Causeret, C.; Bentejac, M.; Albet, S.; Teubner, B.; Bugaut, M.
    Copurification of dihydroxyacetone-phosphate acyl-transferase and other peroxisomal proteins from liver of fenofibrate-treated rats (1997), Biochimie, 79, 423-433.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome membrane-bound Rattus norvegicus 5777
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
amino acid sequence determination Rattus norvegicus
66000
-
gel filtration Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
peroxisomal, partial Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.861
-
pH 7.4, partially purified enzyme Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + dihydroxyacetone phosphate
-
Rattus norvegicus CoA + acyldihydroxyacetone phosphate
-
?

Subunits

Subunits Comment Organism
More immunological, SDS-PAGE and amino acid sequencing analysis of partially purified protein Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
membrane-bound peroxisomal enzyme Rattus norvegicus
7.4
-
optimum with detergent Rattus norvegicus