Activation mechanism of melB tyrosinase from Aspergillus oryzae by acidic treatment

Journal of Biological Inorganic Chemistry

Volumn 18, Issue 1, 2013, Pages 19-26

  Fujieda, Nobutaka ^a   Murata, Michiaki ^a   Yabuta, Shintaro ^a   Ikeda, Takuya ^a   Shimokawa, Chizu ^a   Nakamura, Yukihiro ^b   Hata, Yoji ^b   Itoh, Shinobu ^a  

^a OSAKA UNIVERSITY   (Japan)

^b Gekkeikan Sake Company Ltd   (Japan)

Author keywords

Dioxygen activation; Monooxygenation; Posttranslational modification; Type III copper; Tyrosinase

Indexed keywords

ACID; CATECHOL OXIDASE; FUNGAL ENZYME; LEVODOPA; MELB TYROSINASE; MELO TYROSINASE; MONOPHENOL MONOOXYGENASE; TRYPSIN; UNCLASSIFIED DRUG;

ARTICLE; ASPERGILLUS ORYZAE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; COLORIMETRY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME SUBSTRATE; GEL FILTRATION; HYDROXYLATION; MICHAELIS MENTEN KINETICS; MOLECULAR WEIGHT; NONHUMAN; OXYGEN CONSUMPTION; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; STEADY STATE; SUBSTITUTION REACTION;

ASPERGILLUS ORYZAE; CATALYTIC DOMAIN; ENZYME ACTIVATION; HYDROGEN-ION CONCENTRATION; HYDROXYLATION; MODELS, MOLECULAR; MONOPHENOL MONOOXYGENASE; PHENOLS;

ASPERGILLUS ORYZAE; BASIDIOMYCOTA;

EID: 84872283788     PISSN: 09498257     EISSN: 14321327     Source Type: Journal    
DOI: 10.1007/s00775-012-0945-5     Document Type: Article

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