The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre

European Journal of Biochemistry

Volumn 270, Issue 7, 2003, Pages 1528-1535

  Hofhaus, Götz ^a   Lee, Jeung Eun ^a   Tews, Ivo ^b   Rosenberg, Beate ^a   Lisowsky, Thomas ^a  

^a HEINRICH HEINE UNIVERSITY   (Germany)

^b NONE

Author keywords

Cysteine mutants; Dimer formation; Mitochondrial Erv1p; Redox active CXXC; Sulfhydryl oxidase

Indexed keywords

SULFHYDRYL OXIDASE ERV1P; THIOL OXIDASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CELL FUNCTION; CELL SURVIVAL; DIMERIZATION; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; SACCHAROMYCES CEREVISIAE; YEAST;

BINDING SITES; COLOR; CONSERVED SEQUENCE; CYSTEINE; DIMERIZATION; ENZYME ACTIVATION; FLAVIN-ADENINE DINUCLEOTIDE; GENETIC COMPLEMENTATION TEST; MITOCHONDRIAL PROTEINS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SERINE; SPECTROPHOTOMETRY; STRUCTURE-ACTIVITY RELATIONSHIP;

SACCHAROMYCES CEREVISIAE;

EID: 0037395242     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03519.x     Document Type: Article

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