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Literature summary for 4.2.2.3 extracted from

  • Lamppa, J.W.; Griswold, K.E.
    Alginate lyase exhibits catalysis-independent biofilm dispersion and antibiotic synergy (2013), Antimicrob. Agents Chemother., 57, 137-145.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine alginate lyases are promising therapeutic candidates for treating mucoid Pseudomonas aeruginosa infections. In particular, the enzymes' ability to degrade alginate, a key component of mucoid biofilm matrix, has been the presumed mechanism by which they disrupt biofilms and enhance antibiotic efficacy, but invitro modeling shows that alginate lyase dispersion of Pseudomonas aeruginosa biofilms and enzyme synergy with tobramycin are completely decoupled from catalytic activity Pseudomonas aeruginosa
medicine alginate lyases are promising therapeutic candidates for treating mucoid Pseudomonas aeruginosa infections. In particular, the enzymes' ability to degrade alginate, a key component of mucoid biofilm matrix, has been the presumed mechanism by which they disrupt biofilms and enhance antibiotic efficacy, but invitro modeling shows that alginate lyase dispersion of Pseudomonas aeruginosa biofilms and enzyme synergy with tobramycin are completely decoupled from catalytic activity Sphingomonas sp.

Cloned(Commentary)

Cloned (Comment) Organism
expression of C-terminally His6-tagged A1-III Sphingomonas sp.
expression of C-terminally His6-tagged AlgL Pseudomonas aeruginosa

Protein Variants

Protein Variants Comment Organism
H188A site-directed mutagenesis, the mutation switches the histidine 188 GTG codon to a CGC codon Sphingomonas sp.
Y242F site-directed mutagenesis, the mutation replaces the tyrosine 242 GTA codon with a GAA codon Sphingomonas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information pseudo Michaelis-Menten kinetics of native and recombinant His-tagged enzymes, overview Pseudomonas aeruginosa
additional information
-
additional information pseudo Michaelis-Menten kinetics of native and recombinant His-tagged enzymes, overview Sphingomonas sp.

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q06749 gene algL
-
Sphingomonas sp. Q75WP3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally His6-tagged A1-III by nickel affinity chromatography and dialysis, native enzyme by hydroxyapatite chromatography, ultrafiltration, and gel filtration Sphingomonas sp.
recombinant C-terminally His6-tagged AlgL by nickel affinity chromatography and dialysis, native enzyme by hydroxyapatite chromatography, ultrafiltration, and gel filtration Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrates are medium-viscosity brown seaweed alginate (BSWA) and bacterial (FRD1) alginate substrates from mucoid FRD1 biofilms Pseudomonas aeruginosa ?
-
?
additional information substrates are medium-viscosity brown seaweed alginate (BSWA) and bacterial (FRD1) alginate substrates from mucoid FRD1 biofilms Sphingomonas sp. ?
-
?

Synonyms

Synonyms Comment Organism
A1-III
-
Sphingomonas sp.
alginate lyase
-
Pseudomonas aeruginosa
alginate lyase
-
Sphingomonas sp.
AlgL
-
Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Pseudomonas aeruginosa
37
-
assay at Sphingomonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Pseudomonas aeruginosa
7
-
assay at Sphingomonas sp.

General Information

General Information Comment Organism
metabolism alginate lyase dispersion of Pseudomonas aeruginosa biofilms and enzyme synergy with tobramycin are completely decoupled from catalytic activity, in vitro modeling, overview Pseudomonas aeruginosa
metabolism alginate lyase dispersion of Pseudomonas aeruginosa biofilms and enzyme synergy with tobramycin are completely decoupled from catalytic activity, in vitro modeling, overview Sphingomonas sp.