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Literature summary for 1.14.99.53 extracted from

  • Sabbadin, F.; Henrissat, B.; Bruce, N.; McQueen-Mason, S.
    Lytic polysaccharide monooxygenases as chitin-specific virulence factors in crayfish plague (2021), Biomolecules, 11, 1180.
    View publication on PubMed
Search for more literature for 1.14.99.53

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Aphanomyces astaci

Crystallization (Commentary)

Crystallization (Comment) Organism
homology modeling reveals the typical central beta-sandwich fold of LPMOs, as well as flexible loops and two stabilizing disulfide bonds. The active site contains the histidine brace, consisting of His1 and His96 coordinating the copper cofactor, and the axial, non-coordinating residue Phe187 Aphanomyces astaci

Metals/Ions

Metals/Ions Comment Organism Structure
copper His1 and His96 coordinate the copper cofactor Aphanomyces astaci

Organism

Organism UniProt Comment Textmining
Aphanomyces astaci
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
mycelium AaAA15A is the most highly expressed AA15-encoding gene in both sporulating and growing mycelia Aphanomyces astaci
-
zoospore low expression level of AA15A Aphanomyces astaci
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-chitin + gallate + O2
-
 Aphanomyces astaci chito-oligosaccharide + C1-aldonic acids + ? + H2O
-
 ?
beta-chitin + gallate + O2
-
 Aphanomyces astaci ? + H2O
-
 ?

Synonyms

Synonyms Comment Organism
AA15 lytic polysaccharide monooxygenase
-
 Aphanomyces astaci
AA15A
-
 Aphanomyces astaci

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
49.3
-
 melting temperature, presence of EDTA Aphanomyces astaci
59.2
-
 melting temperature Aphanomyces astaci