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Literature summary for 1.11.1.12 extracted from

  • Chen, H.; Lin, C.; Ken, C.; Wen, L.; Lin, C.
    Putative phospholipid hydroperoxide glutathione peroxidase from Antrodia camphorata (2009), Food Chem., 115, 476-482.
    View publication on PubMed
Search for more literature for 1.11.1.12

Cloned(Commentary)

Cloned (Comment) Organism
into the vector pYEX-S1 for transformation into Saccharomyces cerevisiae cells Taiwanofungus camphoratus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
18000
-
 His6-tagged fusion protein, determined by SDS-PAGE Taiwanofungus camphoratus

Organism

Organism UniProt Comment Textmining
Taiwanofungus camphoratus B8K1J5
-
-

Purification (Commentary)

Purification (Comment) Organism
by Ni2+-nitrilotriacetic acid Sepharose Taiwanofungus camphoratus

Source Tissue

Source Tissue Comment Organism Textmining
fruit body
-
 Taiwanofungus camphoratus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PHGPx is an antioxidant enzyme that can reduce peroxidized phospholipids produced in cell membranes Taiwanofungus camphoratus ?
-
 ?

Subunits

Subunits Comment Organism
monomer
-
 Taiwanofungus camphoratus

Synonyms

Synonyms Comment Organism
AC-PHGPx
-
 Taiwanofungus camphoratus
phospholipid hydroperoxide glutathione peroxidase
-
 Taiwanofungus camphoratus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
23
-
 activity assay at room temperature, ferrithiocyanate assay Taiwanofungus camphoratus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
 Taiwanofungus camphoratus

Cofactor

Cofactor Comment Organism Structure
glutathione
-
 Taiwanofungus camphoratus