Mutation of a strictly conserved, active-site residue alters substrate specificity and cofactor biogenesis in a copper amine oxidase

Biochemistry

Volumn 38, Issue 12, 1999, Pages 3683-3693

  Hevel, Joan M ^a,b   Mills, Stephen A ^a   Klinman, Judith P ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF HAWAII   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

6 HYDROXYDOPA; AMINE OXIDASE (FLAVIN CONTAINING); COPPER; QUINONE DERIVATIVE; TYROSINE;

AMINO ACID SUBSTITUTION; AMINO ACID SYNTHESIS; ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME MECHANISM; ENZYME SPECIFICITY; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; REACTION ANALYSIS;

AMINE OXIDASE (COPPER-CONTAINING); BINDING SITES; CATALYSIS; CONSERVED SEQUENCE; DIHYDROXYPHENYLALANINE; HYDROGEN-ION CONCENTRATION; KINETICS; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PICHIA; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SCHIFF BASES; SUBSTRATE SPECIFICITY;

FELIS CATUS;

EID: 0033596951     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982199m     Document Type: Article

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