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Literature summary extracted from

  • Wanders, R.J.A.; Romeyn, G.J.; Schutgens, R.B.H.; Tager, J.M.
    L-pipecolate oxidase: a distinct peroxisomal enzyme in man (1989), Biochem. Biophys. Res. Commun., 164, 550-555.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.5.3.7 medicine L-pipecolic acid is formed by the catabolism of lysine in humans, and its accumulation is one of the first biochemical abnormalities detected in the Zellweger syndrome Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.5.3.7 peroxisome
-
Homo sapiens 5777
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.3.7 L-pipecolate + O2 Homo sapiens
-
2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2 the product reacts with water to form 2-aminoadipate 6-semialdehyde ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.3.7 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.3.7 liver
-
Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.3.7 L-pipecolate + O2
-
Homo sapiens 2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2 the product reacts with water to form 2-aminoadipate 6-semialdehyde ?