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Literature summary extracted from

  • Hofhaus, G.; Lee, J.E.; Tews, I.; Rosenberg, B.; Lisowsky, T.
    The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre (2003), Eur. J. Biochem., 270, 1528-1535.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.3.2 expression in Escherichia coli strains DH5alpha and BL21(DE3) of wild-type enzyme and a His-tagged truncated enzyme form comprising the 15 kDa C-terminus, expression of full-length point mutants Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.8.3.2 C130S site-directed mutagenesis, inactive mutant, no complementation of an enzyme-defect mutant strain, no complementation of an enzyme-defect mutant strain Saccharomyces cerevisiae
1.8.3.2 C133S site-directed mutagenesis, inactive mutant, no complementation of an enzyme-defect mutant strain, no complementation of an enzyme-defect mutant strain Saccharomyces cerevisiae
1.8.3.2 C159S site-directed mutagenesis, about 70% reduced activity in vitro compared to the wild-type enzyme, complementation of an enzyme-defect mutant strain Saccharomyces cerevisiae
1.8.3.2 C176S site-directed mutagenesis, about 60% reduced activity in vitro compared to the wild-type enzyme, complementation of an enzyme-defect mutant strain Saccharomyces cerevisiae
1.8.3.2 C30S site-directed mutagenesis, about 70% reduced activity in vitro compared to the wild-type enzyme, complementation of an enzyme-defect mutant strain Saccharomyces cerevisiae
1.8.3.2 C33S site-directed mutagenesis, about 50% reduced activity in vitro compared to the wild-type enzyme, no complementation of an enzyme-defect mutant strain Saccharomyces cerevisiae
1.8.3.2 additional information construction of a His-tagged truncated enzyme form comprising the 15 kDa C-terminus, the mutant shows in vitro activity similar to the wild-type enzyme, dimerization behaviour of the mutant enzymes, overview Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.3.2 mitochondrial intermembrane space
-
 Saccharomyces cerevisiae 5758
-
1.8.3.2 mitochondrion intermembrane space Saccharomyces cerevisiae 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.3.2 R-SH + O2 Saccharomyces cerevisiae
-
 R-S-S-R + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.2 Saccharomyces cerevisiae Q12284 several strains, overview
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.3.2 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 the N-terminal cysteine pair of the enzyme is essential for in vivo activity and interacts with the primary redox centre Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.2 R-SH + O2
-
 Saccharomyces cerevisiae R-S-S-R + H2O2
-
 ?
1.8.3.2 R-SH + O2 3 cysteine pairs are required for optimal enzyme function Saccharomyces cerevisiae R-S-S-R + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.3.2 dimer Cys30 and Cys33 are involved in dimer formation Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
1.8.3.2 Erv1p
-
 Saccharomyces cerevisiae
1.8.3.2 sulfhydryl oxidase
-
 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.3.2 FAD dependent on, N-terminal cysteine pair contributes to the correct arrangement of the FAD-binding fold Saccharomyces cerevisiae