Relationship of stopped flow to steady state parameters in the dimeric copper amine oxidase from Hansenula polymorpha and the role of zinc in inhibiting activity at alternate copper-containing subunits

Biochemistry

Volumn 45, Issue 14, 2006, Pages 4683-4694

  Takahashi, Kenichi ^a,b   Klinman, Judith P ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b KURUME UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; DIMERS; FLOW OF FLUIDS; SUBSTRATES; YEAST; ZINC;

COPPER CONTENT; ELECTRON TRANSFER; ENZYME PREPARATION; HOMODIMER;

ENZYMES;

AMINE OXIDASE (FLAVIN CONTAINING); COPPER; COPPER AMINE OXIDASE; ISOTOPE; METHYLAMINE; OXYGEN; UNCLASSIFIED DRUG; ZINC;

ARTICLE; CALCULATION; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME INHIBITION; HANSENULA POLYMORPHA; KINETICS; NONHUMAN; OXIDATION; OXYGEN AFFINITY; PRIORITY JOURNAL; REACTION ANALYSIS; REDUCTION; SACCHAROMYCES CEREVISIAE; STEADY STATE;

AMINE OXIDASE (COPPER-CONTAINING); COPPER; DIHYDROXYPHENYLALANINE; KINETICS; MODELS, CHEMICAL; OXIDATION-REDUCTION; PICHIA; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SPECTROPHOTOMETRY; ZINC;

PICHIA ANGUSTA; SACCHAROMYCES CEREVISIAE;

EID: 33645688672     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0521893     Document Type: Article

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