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Literature summary for 1.5.3.7 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

Application Comment Organism
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

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Substrates and Products (Substrate)

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