Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid

Journal of Biological Chemistry

Volumn 276, Issue 17, 2001, Pages 14242-14248

  Lavulo, Lopeti T ^a   Sossong Jr , Thomas M ^b   Brigham Burke, Michael R ^b   Doyle, Michael L ^b,d   Cox, J David ^c   Christianson, David W ^c   Ash, David E ^a  

^a TEMPLE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b GLAXOSMITHKLINE   (United Kingdom)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

^d BRISTOL MYERS SQUIBB   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CENTRIFUGATION; CRYSTALLIZATION; DIFFERENTIAL SCANNING CALORIMETRY; MUTAGENESIS;

SALT LINKS;

ENZYMES;

AMINO ACID; ARGINASE; CARBON 14; LIVER ENZYME; MONOMER; MUTANT PROTEIN; ARGININE; MANGANESE;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DIFFERENTIAL SCANNING CALORIMETRY; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME STRUCTURE; ENZYME SUBUNIT; GENE OVEREXPRESSION; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; RAT; SITE DIRECTED MUTAGENESIS; TEMPERATURE; AMINO ACID SEQUENCE; ANIMAL; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; DIMERIZATION; ELECTRON; ENZYMOLOGY; GEL CHROMATOGRAPHY; GENETICS; KINETICS; LIVER; MOLECULAR GENETICS; MOUSE; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; ULTRACENTRIFUGATION; X RAY CRYSTALLOGRAPHY; XENOPUS;

FRAXINUS;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; ARGINASE; ARGININE; CALORIMETRY, DIFFERENTIAL SCANNING; CATALYSIS; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRONS; KINETICS; LIVER; MANGANESE; MICE; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RATS; TEMPERATURE; ULTRACENTRIFUGATION; XENOPUS;

EID: 0035958024     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M010575200     Document Type: Article

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