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Literature summary for 1.11.1.12 extracted from

  • Zhang, W.; He, Y.; Yang, Z.; Yu, J.; Chen, Y.; Zhou, C.
    Crystal structure of glutathione-dependent phospholipid peroxidase Hyr1 from the yeast Saccharomyces cerevisiae (2008), Proteins Struct. Funct. Genet., 73, 1058-1062.
    View publication on PubMed
Search for more literature for 1.11.1.12

Cloned(Commentary)

Cloned (Comment) Organism
the open reading frame of Hyr1/YIR037W is cloned into a pET28a-derived vector for expression in Escherichia coli Rosetta DE3 cells Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structure is solved to a resolution of 2.0 A Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
C82S in the presence of thioredixin system, wild-type Hyr1 can consume H2O2 rapidly, while the C82S mutant totally abolish the activity, indicating the important role of Cys82 in Trx2 specificity Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
on a Ni-NTA column, further purified by gel filtration Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information specifically detoxifies phospholipid peroxide Saccharomyces cerevisiae ?
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 ?

Synonyms

Synonyms Comment Organism
glutathione-dependent phospholipid peroxidase
-
 Saccharomyces cerevisiae
GPX3
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 Saccharomyces cerevisiae
Hyr1
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 Saccharomyces cerevisiae
Hyr1/YIR037W
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 Saccharomyces cerevisiae
PHGPX
-
 Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 activity assay Saccharomyces cerevisiae