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Literature summary for 1.10.3.2 extracted from

  • Yatsu, J.; Asano, T.
    Cuticle laccase of the silkworm, Bombyx mori: purification, gene identification and presence of its inactive precursor in the cuticle (2009), Insect Biochem. Mol. Biol., 39, 254-262.
    View publication on PubMed
Search for more literature for 1.10.3.2

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ multi-copper enzyme Bombyx mori

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
 2 * 70000, SDS-PAGE Bombyx mori
84280
-
 2 * 84280, mature enzyme, calculated from amino acid sequence Bombyx mori
154000
-
 gel filtration Bombyx mori

Organic Solvent Stability

Organic Solvent Comment Organism
additional information 1% (v/v) Triton X-100 and 8 M urea have little or no influence on the strength of cuticle laccase activity Bombyx mori

Organism

Organism UniProt Comment Textmining
Bombyx mori
-
 Kinsyu x Showa
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, Q-Sepharose column chromatography, HiTrap Q column chromatography, Mono Q column chromatography, and Superdex-200 gel filtration Bombyx mori

Source Tissue

Source Tissue Comment Organism Textmining
cuticle pupal cuticle Bombyx mori
-
epidermis
-
 Bombyx mori
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dopamine + O2
-
 Bombyx mori ?
-
 ?
methyl hydroquinone + O2
-
 Bombyx mori ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 70000, SDS-PAGE Bombyx mori
homodimer 2 * 84280, mature enzyme, calculated from amino acid sequence Bombyx mori

Synonyms

Synonyms Comment Organism
benzenediol:O2 oxidoreductase
-
 Bombyx mori
Lac2
-
 Bombyx mori
laccase2
-
 Bombyx mori

Expression

Organism Comment Expression
Bombyx mori laccase2 is highly expressed in the epidermis prior to ecdysis up