Ostreococcus tauri ADP-glucose pyrophosphorylase reveals alternative paths for the evolution of subunit roles

Journal of Biological Chemistry

Volumn 284, Issue 49, 2009, Pages 34092-34102

  Kuhn, Misty L ^a   Falaschetti, Christine A ^a   Ballicora, Miguel A ^a  

^a LOYOLA UNIVERSITY CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3-PHOSPHOGLYCERATE; ADPGLUCOSE PYROPHOSPHORYLASE; ALLOSTERIC PROPERTIES; ALTERNATIVE PATH; CATALYTIC EFFICIENCIES; GREEN PLANTS; HETEROLOGOUS GENES; IN-PLANTS; NON-CATALYTIC; OSTREOCOCCUS TAURI; POTATO TUBERS; REDOX REGULATION; SOLUBLE EXPRESSION; STARCH SYNTHESIS; SUBFUNCTIONALIZATION; SUBUNIT GENES; UNICELLULAR ALGA;

CATALYSIS; GENE EXPRESSION; GLUCOSE; SUBSTRATES; SUGAR (SUCROSE); SYNTHESIS (CHEMICAL);

ENZYMES;

ADENOSINE TRIPHOSPHATE; GLUCOSE 1 PHOSPHATE ADENYLYLTRANSFERASE; GLYCERALDEHYDE 3 PHOSPHATE; MAGNESIUM ION; PHOSPHOGLYCERATE KINASE;

ALGA; ALLOSTERISM; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME STRUCTURE; ENZYME SUBUNIT; GENE EXPRESSION; MOLECULAR EVOLUTION; NONHUMAN; OSTREOCOCCUS TAURI; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN PURIFICATION; REGULATORY MECHANISM;

ALGAE; ALLOSTERIC SITE; CATALYSIS; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE; GLYCERIC ACIDS; KINETICS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PHOTOSYNTHESIS; PHYLOGENY; PROTEIN STRUCTURE, TERTIARY;

ALGAE; EUKARYOTA; OSTREOCOCCUS TAURI; SOLANUM TUBEROSUM; VIRIDIPLANTAE;

EID: 71749106140     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.037614     Document Type: Article

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