Mechanistic and structural analyses of the roles of active site residues in yeast polyamine oxidase Fms1: Characterization of the N195A and D94N enzymes

Biochemistry

Volumn 51, Issue 43, 2012, Pages 8690-8697

  Adachi, Mariya S ^a   Taylor, Alexander B ^a   Hart, P John ^a,b   Fitzpatrick, Paul F ^a  

^a University of Texas Health Science Center   (United States)

^b SOUTH TEXAS VETERANS HEALTH CARE SYSTEM   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE RESIDUES; AMINE SUBSTRATES; AMINO ACID RESIDUES; BIOSYNTHETIC PATHWAY; FITZPATRICK; PANTOTHENIC ACID; POLYAMINE OXIDASE; POLYAMINES; PROTEIN STRUCTURES; TETRAETHYLENE GLYCOLS; WILD-TYPE ENZYMES;

AMINO ACIDS; CATALYSIS; ENZYMES; HYDROGEN BONDS; MAMMALS; ORGANIC COMPOUNDS; RATE CONSTANTS; YEAST;

SUBSTRATES;

AMINO ACID; FLAVOPROTEIN; PANTOTHENIC ACID; POLYAMINE; POLYAMINE OXIDASE; PROTEIN D94N FMS1; PROTEIN N195A FMS1; QUERCETIN; SPERMINE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; MUTATION; NONHUMAN; OXIDATION; PH; PKA; PRIORITY JOURNAL; PROTEIN STRUCTURE; REDUCTION; SACCHAROMYCES CEREVISIAE; WILD TYPE;

CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; POINT MUTATION; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SPERMINE;

MAMMALIA; SACCHAROMYCES CEREVISIAE;

EID: 84868093877     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3011434     Document Type: Article

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