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Literature summary for 1.2.1.12 extracted from

  • Boschi-Muller, S.; Muller, S.; Van Dorsselaer, A.; Bock, A.; Branlant, G.
    Substituting selenocysteine for active site cysteine 149 of phosphorylating glyceraldehyde 3-phosphate dehydrogenase reveals a peroxidase activity (1998), FEBS Lett., 439, 241-245.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C149selenocysteine mutant enzyme has selenoperoxidase activity Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
wild-type enzyme and mutant C149selenocysteine
-

Purification (Commentary)

Purification (Comment) Organism
mutant enzyme C149selenocysteine Geobacillus stearothermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
Geobacillus stearothermophilus 3-phospho-D-glyceroyl phosphate + NADH
-
?
additional information mutant enzyme C149selenocysteine shows selenoperoxidase activity with tert-butyl hydroperoxide and 3-carboxy 4-nitrobenzenethiol. Wild-type enzyme has no peroxidase activity Geobacillus stearothermophilus ?
-
?

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Geobacillus stearothermophilus