Roles of active site residues in LodA, a cysteine tryptophylquinone dependent ε-lysine oxidase-Reference-Cited by-同舟云学术

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Roles of active site residues in LodA, a cysteine tryptophylquinone dependent ε-lysine oxidase

Published:2015-08 Issue: Volume:579 Page:26-32
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Sehanobish Esha,Chacón-Verdú María Dolores,Sanchez-Amat Antonio,Davidson Victor L.

Funder

Burnett School of Biomedical Sciences

National Institute of General Medical Sciences

National Institutes of Health

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference17 articles.

1. A novel type of lysine oxidase: l-lysine-ε-oxidase

2. The Antimicrobial Activity of Marinocine, Synthesized by Marinomonas mediterranea , Is Due to Hydrogen Peroxide Generated by Its Lysine Oxidase Activity

3. Purification and partial characterization of marinocine, a new broad-spectrum antibacterial protein produced by Marinomonas mediterranea

4. Hydrogen Peroxide Linked to Lysine Oxidase Activity Facilitates Biofilm Differentiation and Dispersal in Several Gram-Negative Bacteria

5. LodB is required for the recombinant synthesis of the quinoprotein l-lysine-ε-oxidase from Marinomonas mediterranea

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