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Literature summary for 1.11.1.16 extracted from

  • Ravichandran, A.; Rao, R.G.; Thammaiah, V.; Gopinath, S.M.; Sridhar, M.
    A versatile peroxidase from Lentinus squarrosulus towards enhanced delignification and in vitro digestibility of crop residues (2019), BioResources, 14, 5132-5149 .
No PubMed abstract available

Application

Application Comment Organism
agriculture use of versatile peroxidase in enhancing the digestibility of straws is substantiated through proximate and in vitro digestibility analysis, use of versatile peroxidase in increasing the in vitro degradation of straws for enhancing feed utilization in ruminants. Usage of commonly available crop residues such as paddy straw, finger millet straw, foxtail millet straw, little millet straw, and barnyard millet straw (milled to 1 to 2 cm length and dried at a constant temperature of 70°C) in biodegradation studies Lentinus squarrosulus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Lentinus squarrosulus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in the heme group Lentinus squarrosulus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 Mn(II) + 2 H+ + H2O2 Lentinus squarrosulus
-
2 Mn(III) + 2 H2O
-
?
2 Mn(II) + 2 H+ + H2O2 Lentinus squarrosulus TAMI004
-
2 Mn(III) + 2 H2O
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2 Lentinus squarrosulus
-
oxidized 2,6-dimethoxyphenol + 2 H2O
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2 Lentinus squarrosulus TAMI004
-
oxidized 2,6-dimethoxyphenol + 2 H2O
-
?
additional information Lentinus squarrosulus versatile peroxidase oxidizes high molecular weight substrates through catalytic tryptophan at the surface resembling lignin peroxidase and Mn2+ to Mn3+ as in manganese peroxidase ?
-
-
additional information Lentinus squarrosulus TAMI004 versatile peroxidase oxidizes high molecular weight substrates through catalytic tryptophan at the surface resembling lignin peroxidase and Mn2+ to Mn3+ as in manganese peroxidase ?
-
-
Reactive Black 5 + 2 H+ + H2O2 Lentinus squarrosulus
-
oxidized Reactive Black 5 + 2 H2O
-
?
Reactive Black 5 + 2 H+ + H2O2 Lentinus squarrosulus TAMI004
-
oxidized Reactive Black 5 + 2 H2O
-
?
veratryl alcohol + H2O2 Lentinus squarrosulus
-
verytryl aldehyde + 2 H2O
-
?
veratryl alcohol + H2O2 Lentinus squarrosulus TAMI004
-
verytryl aldehyde + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Lentinus squarrosulus
-
a wild isolate
-
Lentinus squarrosulus TAMI004
-
a wild isolate
-

Source Tissue

Source Tissue Comment Organism Textmining
mycelium
-
Lentinus squarrosulus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
manganese oxidizing activity is 12 U/ml in submerged and 131 U/ml in solid-state culture Lentinus squarrosulus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 Mn(II) + 2 H+ + H2O2
-
Lentinus squarrosulus 2 Mn(III) + 2 H2O
-
?
2 Mn(II) + 2 H+ + H2O2
-
Lentinus squarrosulus TAMI004 2 Mn(III) + 2 H2O
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
-
Lentinus squarrosulus oxidized 2,6-dimethoxyphenol + 2 H2O
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
-
Lentinus squarrosulus TAMI004 oxidized 2,6-dimethoxyphenol + 2 H2O
-
?
additional information versatile peroxidase oxidizes high molecular weight substrates through catalytic tryptophan at the surface resembling lignin peroxidase and Mn2+ to Mn3+ as in manganese peroxidase Lentinus squarrosulus ?
-
-
additional information versatile peroxidase oxidizes high molecular weight substrates through catalytic tryptophan at the surface resembling lignin peroxidase and Mn2+ to Mn3+ as in manganese peroxidase Lentinus squarrosulus TAMI004 ?
-
-
Reactive Black 5 + 2 H+ + H2O2
-
Lentinus squarrosulus oxidized Reactive Black 5 + 2 H2O
-
?
Reactive Black 5 + 2 H+ + H2O2
-
Lentinus squarrosulus TAMI004 oxidized Reactive Black 5 + 2 H2O
-
?
veratryl alcohol + H2O2
-
Lentinus squarrosulus verytryl aldehyde + 2 H2O
-
?
veratryl alcohol + H2O2
-
Lentinus squarrosulus TAMI004 verytryl aldehyde + 2 H2O
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3
-
manganese peroxidase activity assay at, substrate Mn(II) Lentinus squarrosulus
4.5
-
lignin peroxidase activity assay at, substrate Reactive Black 5 Lentinus squarrosulus

Cofactor

Cofactor Comment Organism Structure
heme
-
Lentinus squarrosulus

General Information

General Information Comment Organism
additional information versatile peroxidase, an extracellular heme protein of the ligninolytic system, is endowed with polyvalent catalytic sites that render this protein with high redox potential Lentinus squarrosulus
physiological function treatment of crops with Lentinus squarrosulus rich in versatile peroxidase show a decrease in neutral detergent fiber, and acid detergent lignin contents, promptig delignification. Screening of wild isolates for a versatile peroxidase having exceptional efficiency for aromatics and manganese oxidation Lentinus squarrosulus