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Literature summary extracted from

  • Wang, W.; Winther, J.R.; Thorpe, C.
    Erv2p: characterization of the redox behavior of a yeast sulfhydryl oxidase (2007), Biochemistry, 46, 3246-3254.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.3.2 truncated version of Erv2p, without the N-terminal 34 residues, cloned into a pET24(a+) plasmid carrying kanamycin resistance. Amplified in DH5alpha Escherichia coli strain. Expressed from the Escherichia coli strain BL21(DE3) or BL21(DE3 star) Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.3.2 Zn2+ upon coordination with Zn2+, full reduction of Erv2p requires 6 electrons. Strongly inhibits Erv2p when assayed using tris(2-carboxyethyl)phosphine as the reducing substrate of the oxidase. Restoration of 1 mM EDTA effects rapid recovery of 80% of the original activity Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.3.2 11.3
-
 dithiothreitol
-
 Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.3.2 membrane
-
 Saccharomyces cerevisiae 16020
-

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.2 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.3.2 gel filtration Saccharomyces cerevisiae

Storage Stability

EC Number Storage Stability Organism
1.8.3.2 -20°C, Tris buffer, pH 7.5, 1 mM EDTA, more than 1 year Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.2 bis-(2-mercaptoethyl)sulfone + O2
-
 Saccharomyces cerevisiae ? + H2O
-
 ?
1.8.3.2 dithiothreitol + O2
-
 Saccharomyces cerevisiae ? + H2O
-
 ?
1.8.3.2 additional information Erv2p is a modest catalyst of disulfide bond formation. None of the monothiols (at 10 mM), including beta-mercaptoethanol, N-acetylcysteamine, reduced glutathione and CoASH, prove detectable substrates of the yeast oxidase at pH 7.5. In contrast, dithiols are significant substrates Saccharomyces cerevisiae ?
-
 ?
1.8.3.2 reduced lysozyme + O2
-
 Saccharomyces cerevisiae ? + H2O
-
 ?
1.8.3.2 RNasered + O2
-
 Saccharomyces cerevisiae ? + H2O
-
 ?
1.8.3.2 thioredoxin + O2
-
 Saccharomyces cerevisiae thioredoxin disulfide + H2O2
-
 ?
1.8.3.2 tris(2-carboxyethyl)-phosphine + O2
-
 Saccharomyces cerevisiae ? + H2O
-
 ?
1.8.3.2 Trx Escherichia coli + O2
-
 Saccharomyces cerevisiae ? + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.3.2 ERv2p
-
 Saccharomyces cerevisiae
1.8.3.2 sulfhydryl oxidase
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.3.2 3.43
-
 dithiothreitol
-
 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.3.2 FAD dithionite and photochemical reductions of Erv2p show full reduction of the flavin cofactor after the addition of 4 electrons with a midpoint potential of -200 mV at pH 7.5. No charge-transfer complex between a proximal thiolate and the oxidized flavin Saccharomyces cerevisiae