Literature summary for 1.8.3.2 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
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

Protein Variants	Comment	Organism
C130S	site-directed mutagenesis, inactive mutant, no complementation of an enzyme-defect mutant strain, no complementation of an enzyme-defect mutant strain	Saccharomyces cerevisiae
C133S	site-directed mutagenesis, inactive mutant, no complementation of an enzyme-defect mutant strain, no complementation of an enzyme-defect mutant strain	Saccharomyces cerevisiae
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
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
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
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
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

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Reaction

Reaction	Comment	Organism	Reaction ID
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)

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

Subunits

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

Synonyms

Synonyms	Comment	Organism
Erv1p	-	Saccharomyces cerevisiae
sulfhydryl oxidase	-	Saccharomyces cerevisiae

Cofactor

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

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Release 2023.1 (January 2023)