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Literature summary for 1.14.99.53 extracted from

  • Askarian, F.; Uchiyama, S.; Masson, H.; Sorensen, H.; Golten, O.; Bunaes, A.; Mekasha, S.; Rohr, A.; Kommedal, E.; Ludviksen, J.; Arntzen, M.; Schmidt, B.; Zurich, R.; van Sorge, N.; Eijsink, V.; Krengel, U.; Mollnes, T.; Lewis, N.; Nizet, V.; Vaaje-Kol, G.
    The lytic polysaccharide monooxygenase CbpD promotes Pseudomonas aeruginosa virulence in systemic infection (2021), Nat. Commun., 12, 1230.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
azurin 1 microM azurin activates 1 microM copper-free CbpD, which otherwise is inactive Pseudomonas aeruginosa
pyocyanin boosts CbpD activity towards beta-chitin, with rapid inactivation abocve 1 M Pseudomonas aeruginosa

Crystallization (Commentary)

Crystallization (Comment) Organism
homology modeling, CbpD is a monomeric tri-modular enzyme with flexible linkers Pseudomonas aeruginosa

Metals/Ions

Metals/Ions Comment Organism Structure
copper
-
 Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9I589
-
-
Pseudomonas aeruginosa DSM 22644 Q9I589
-
-

Synonyms

Synonyms Comment Organism
CbpD
-
 Pseudomonas aeruginosa

General Information

General Information Comment Organism
physiological function deletion of cbpD renders Pseudomonas aeruginosa unable to establish a lethal systemic infection, associated with enhanced bacterial clearance in vivo. CbpD-dependent survival of the wild-type bacterium is not attributable to dampening of pro-inflammatory responses by CbpD ex vivo or in vivo. CbpD attenuates the terminal complement cascade in human serum. Catalytic activity is crucial for virulence function. The lack of the enzyme result in substantial reorganization of the bacterial and host proteomes Pseudomonas aeruginosa