Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins

Nature Communications

Volumn 5, Issue , 2014, Pages

  Goldfeder, Mor ^a   Kanteev, Margarita ^a   Isaschar Ovdat, Sivan ^a   Adir, Noam ^a   Fishman, Ayelet ^a  

^a TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

CATECHOL OXIDASE; COPPER PROTEIN; HISTIDINE; MONOPHENOL MONOOXYGENASE; PHENOL DERIVATIVE; SULFIDE; WATER; PHENOL; PROTEIN BINDING;

CATALYSIS; ENZYME ACTIVITY; HYDROXYL RADICAL; MUTATION; OXIDATION; PHARMACEUTICAL INDUSTRY; PHENOL; PIGMENT; PROTEIN; SUBSTRATE;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ASSAY; ENZYME SUBSTRATE COMPLEX; HYDROXYLATION; OXIDATION; PROTEIN ANALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; ENZYME SPECIFICITY; ESCHERICHIA COLI; ISOLATION AND PURIFICATION; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN CONFORMATION; X RAY DIFFRACTION;

CRYSTALLIZATION; ESCHERICHIA COLI; HYDROXYLATION; MODELS, MOLECULAR; MONOPHENOL MONOOXYGENASE; OXIDATION-REDUCTION; PHENOL; PROTEIN BINDING; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; X-RAY DIFFRACTION;

EID: 84905233254     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5505     Document Type: Article

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