The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia coli serine hydroxymethyltransferase

FEBS Journal

Volumn 276, Issue 1, 2009, Pages 132-143

  Florio, Rita ^a   Chiaraluce, Roberta ^a   Consalvi, Valerio ^a   Paiardini, Alessandro ^a   Catacchio, Bruno ^a   Bossa, Francesco ^a   Contestabile, Roberto ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

Conserved hydrophobic contacts; Fold type I enzymes; Pyridoxal phosphate; Quaternary structure; Serine hydroxymethyltransferase

Indexed keywords

GLYCINE HYDROXYMETHYLTRANSFERASE; PYRIDOXAL 5 PHOSPHATE;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME STABILITY; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; APOENZYMES; BINDING SITES; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; EVOLUTION, MOLECULAR; GLYCINE HYDROXYMETHYLTRANSFERASE; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PYRIDOXAL PHOSPHATE; RECOMBINANT PROTEINS;

ESCHERICHIA COLI;

EID: 57649153157     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06761.x     Document Type: Article

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