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Literature summary for 1.11.1.19 extracted from

  • Saijo, S.; Sato, T.; Tanaka, N.; Ichiyanagi, A.; Sugano, Y.; Shoda, M.
    Precipitation diagram and optimization of crystallization conditions at low ionic strength for deglycosylated dye-decolorizing peroxidase from a basidiomycete (2005), Acta Crystallogr. Sect. F, 61, 729-732.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.11.1.19

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Aspergillus oryzae Thanatephorus cucumeris

Crystallization (Commentary)

Crystallization (Comment) Organism
deglycosylated DyP is crystallized by the sitting drop vapor diffusion method, using 25.3% (w/v) PEG 8000 at 5.5 K (pH 6.2) Thanatephorus cucumeris

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48000
-
 SDS-PAGE Thanatephorus cucumeris

Organism

Organism UniProt Comment Textmining
Thanatephorus cucumeris
-
 strain Dec 1
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
 Thanatephorus cucumeris

Purification (Commentary)

Purification (Comment) Organism
-
 Thanatephorus cucumeris

Storage Stability

Storage Stability Organism
deglycosylated DyP exhibits enzymatic activity and is stable for more than 26 d either in MES buffer at pH 6.0 or in 45% (v/v) methanol Thanatephorus cucumeris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information DyP shows both dye-decolorizing and lignin-degrading activities when H2O2 is added Thanatephorus cucumeris ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 48000, the protein exists as a monomer in solution, gel filtration and dynamic light scattering Thanatephorus cucumeris

Synonyms

Synonyms Comment Organism
dye-decolorizing peroxidase
-
 Thanatephorus cucumeris
DyP
-
 Thanatephorus cucumeris

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2
-
-
 Thanatephorus cucumeris