Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.1.19 extracted from

  • Sugano, Y.; Nakano, R.; Sasaki, K.; Shoda, M.
    Efficient heterologous expression in Aspergillus oryzae of a unique dye-decolorizing peroxidase, DyP, of Geotrichum candidum Dec 1 (2000), Appl. Environ. Microbiol., 66, 1754-1758.
    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 strain M-2-3, no exogenous heme is necessary for the expression of DyP Geotrichum candidum

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the oxidation of 2,6-dimethoxyphenol and guaiacol by rDyP occurs without the addition of Mn2+, and no enhancement of activity by the addition of Mn21 is observed Geotrichum candidum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
58000
-
 recombinant enzyme, SDS-PAGE Geotrichum candidum
60000
-
 native enzyme, SDS-PAGE Geotrichum candidum

Organism

Organism UniProt Comment Textmining
Geotrichum candidum
-
 strain Dec 1
-

Purification (Commentary)

Purification (Comment) Organism
quaternary aminoethyl-Toyopearl column chromatography and Mono-Q column chromatography Geotrichum candidum

Source Tissue

Source Tissue Comment Organism Textmining
culture condition:dextrose-grown cell
-
 Geotrichum candidum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
22.4
-
 culture supernatant, at 30°C, pH not specified in the publication Geotrichum candidum
331
-
 after 14.8fold purification, at 30°C, pH not specified in the publication Geotrichum candidum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,6-dimethoxyphenol + H2O2 + H+
-
 Geotrichum candidum ?
-
 ?
guaiacol + H2O2 + H+
-
 Geotrichum candidum ?
-
 ?
additional information veratryl alcohol, Reactive Red 123, Reactive Orange 13, and Reactive Yellow 2 are not decolorized by the recombinant enzyme Geotrichum candidum ?
-
 ?
Reactive Black 5 + H2O2 + H+ weak decolorization, 0.5% activity of the native wild type enzyme compared to Reactive Blue 5 Geotrichum candidum oxidized Reactive Black 5 + H2O
-
 ?
Reactive Blue 19 + H2O2 + H+ 92% activity of the native wild type enzyme compared to Reactive Blue 5 Geotrichum candidum oxidized Reactive Blue 19 + H2O
-
 ?
Reactive Blue 5 + H2O2 + H+ 100% activity Geotrichum candidum oxidized Reactive Blue 5 + H2O
-
 ?
Reactive Red 120 + H2O2 + H+ slight decolorization Geotrichum candidum oxidized Reactive Violet 23 + H2O
-
 ?
Reactive Red 33 + H2O2 + H+ weak decolorization, 2% activity of the native wild type enzyme compared to Reactive Blue 5 Geotrichum candidum oxidized Reactive Red 33 + H2O
-
 ?
Reactive Violet 23 + H2O2 + H+ weak decolorization Geotrichum candidum oxidized Reactive Violet 23 + H2O
-
 ?
Reactive Yellow 2 + H2O2 + H+ 2.6% activity of the native wild type enzyme compared to Reactive Blue 5 Geotrichum candidum oxidized Reactive Yellow 2 + H2O
-
 ?

Synonyms

Synonyms Comment Organism
DyP
-
 Geotrichum candidum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 70 after 2 h heat treatment, the native enzyme shows 97% residual activity at 40°C, 93% residual activity at 50°C, and 79% residual activity at 60°C when measured at 30°C for 1 min. After heating at 30, 40, and 50°C for 120 min, recombinant DyP retains more than 90% of its activity when measured at 30°C for 1 min, but the enzyme gradually becomes inactive after treatment at 60°C (12% residual activity) and is rapidly inactivated at 70°C Geotrichum candidum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3 3.2 recombinant enzyme Geotrichum candidum
3.2
-
 native enzyme Geotrichum candidum

Cofactor

Cofactor Comment Organism Structure
heme DyP is a heme-containing peroxidase Geotrichum candidum