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Literature summary extracted from

  • Dodt, G.; Kim, D.; Reimann, S.; McCabe, K.; Gould, S.J.; Mihalik, S.J.
    The human L-pipecolic acid oxidase is similar to bacterial monomeric sarcosine oxidases rather than D-amino acid oxidases (2000), Cell Biochem. Biophys., 32, 313-316.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.5.3.7 medicine L-pipecolic oxidase activity is deficient in patients with peroxisome biogenesis disorders Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

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 kidney
-
 Homo sapiens
-
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 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.3.7 FAD covalently bound Homo sapiens