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Literature summary for 1.14.99.54 extracted from

  • Liu, B.; Olson, A.; Wu, M.; Broberg, A.; Sandgren, M.
    Biochemical studies of two lytic polysaccharide monooxygenasesfrom the white-rot fungus Heterobasidion irregulare and their roles in lignocellulose degradation (2017), PLoS ONE, 12, e0189479 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris Heterobasidion irregulare

Organism

Organism UniProt Comment Textmining
Heterobasidion irregulare
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein lack of potential N-glycosylation sites, presence of 37 predicted O-linked glycosylation sites. Molecular mass of recombinant protein is 75 kDa by SDS-PAGE, as compared with 32500 predicted Heterobasidion irregulare

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no substrate: carboxymethylcellulose or short cellooligosaccharides Heterobasidion irregulare ?
-
?
phosphoric acid swollen cellulose + ascorbic acid + O2
-
Heterobasidion irregulare ? + dehydroascorbate + H2O
-
?

Subunits

Subunits Comment Organism
? x * 75000, SDS-PAGE of recombinant protein Heterobasidion irregulare

Synonyms

Synonyms Comment Organism
GH61H
-
Heterobasidion irregulare
Lpmo9H
-
Heterobasidion irregulare