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Literature summary extracted from

  • Ijlst, L.; de Kromme, I.; Oostheim, W.; Wanders, R.J.A.
    Molecular cloning and expression of human L-pipecolate oxidase (2000), Biochem. Biophys. Res. Commun., 270, 1101-1105.
    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
1.5.3.7 medicine the L-pipecolate pathway for degradation of lysine is the principal one in the brain Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.3.7 expressed as a chimera between maltose-binding protein and L-pipecolic acid oxidase Homo sapiens
1.5.3.7 expressed in Escherichia coli BL21 Homo sapiens

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
-
-
-

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 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.3.7 8.7
-
 assay at Homo sapiens