L-Lysine 6-Oxidase, M. mediterranea | P1500

LodA is a novel enzyme (EC 1.4.3.20) that catalyzes the chemical reaction:L-lysine + O2 + H2O↔ 6-amino-2-oxohexanoate + NH3 + H2O2. It has antibacterial activity against a wide spectrum of Gram-positive and Gram-negative bacteria including nosocomial isolates of S.aureus and Pseudomonas sp. The antimicrobial activity is due to hydrogen peroxide generated by its lysine oxidase activity. It also has autotoxic activity. Involved in biofilm differentiation; responsible for cell death within microcolonies during biofilm development which is linked to the generation of a phenotypically diverse dispersal population and thus may play a role in colonization. The lysine oxidase is used in the enzymatic assay of L-lysine.

P1500 | L-Lysine 6-Oxidase, M. mediterranea DataSheet

Biomolecule/Target :

Synonyms: L-lysine-epsilon-oxidase, LodA, marinocine

Alternates names: L-lysine-epsilon-oxidase, LodA, marinocine

Taglines:

NCBI Gene ID #:

NCBI Gene Symbol: lodA

Gene Source: Marinomonas mediterranea

Accession #: F2JXJ3

Recombinant: False

Source: Marinomonas mediterranea

Purity by SDS-PAGE: >95%

Assay:

Purity:

Assay #2:

Endotoxin Level:

Activity (Specifications/test method): Specific activity is >2 U/mg. The specific activity of Lysine oxidase was measured in the presence of substrate, L-lysine. Rate of H2O2 production was detected by increase in absorbance.

Biological activity:

Results:

Binding Capacity:

Unit Definition: One unit of L-Lysine oxidase is the amount of enzyme that converts L-lysine to 6-amino-2-oxohexanoate and generates 1.0 umol of H2O2 per minute at pH 7.4 at 25 °C.

Molecular Weight: 80.88 kDa

Concentration:

Appearance: Lyophilized powder

Physical form description: Lyophilized

Reconstitution Instructions: Reconstitute in sterile deionized water.

Amino acid sequence:

Handling: Centrifuge the vial prior to opening.

Usage: For Research Use Only! Not to be used in humans