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Literature summary for 1.5.3.7 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

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
medicine the L-pipecolate pathway for degradation of lysine is the principal one in the brain Homo sapiens

Cloned(Commentary)

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

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
-
-
-

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 ?

pH Optimum

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