L-pipecolate oxidase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: L-pipecolate + O2 = 2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2 + H+. Delta1-piperideine-6-carboxylate is also known as 2,3,4,5-tetrahydropyridine-2-carboxylate. [EC:1.5.3.7, RHEA:11992]

L-pipecolate oxidase activity is a catalytic activity that involves the oxidation of L-pipecolate, a cyclic amino acid, to $\\delta$-aminovalerate. This reaction is crucial for the degradation of lysine in certain organisms, particularly in bacteria. The enzyme responsible for this activity, L-pipecolate oxidase, belongs to the flavin-containing monooxygenase (FMO) family and utilizes molecular oxygen as an electron acceptor. The reaction mechanism involves the following steps:

1. L-pipecolate binds to the enzyme's active site.
2. The enzyme's flavin cofactor, typically FAD, is reduced by L-pipecolate.
3. Molecular oxygen is activated and incorporated into the enzyme-substrate complex.
4. The activated oxygen atom is transferred to L-pipecolate, resulting in the formation of $\\delta$-aminovalerate and a reduced flavin cofactor.
5. The reduced flavin cofactor is reoxidized by molecular oxygen, completing the catalytic cycle.

This enzymatic reaction is essential for the metabolism of lysine in several organisms, including bacteria and plants. In bacteria, it is involved in the degradation of lysine, which can serve as a carbon and nitrogen source. In plants, it contributes to the synthesis of the amino acid proline, which plays a role in osmoregulation and stress response.'
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Proteins (2)

Compounds (1)