Disruption of Escherichia coli transaldolase into catalytically active monomers: Evidence against half-of-the-sites mechanism

FEBS Letters

Volumn 441, Issue 2, 1998, Pages 247-250

  Schörken, Ulrich ^a   Jia, Jia ^b   Sahm, Hermann ^a   Sprenger, Georg A ^a   Schneider, Gunter ^b  

^a FORSCHUNGSZENTRUM JÜLICH   (Germany)

^b KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Class I aldolase; Half of the sites mechanism; Protein crystallography; Site directed mutagenesis; Transaldolase

Indexed keywords

TRANSALDOLASE;

AMINO ACID SUBSTITUTION; ARTICLE; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBUNIT; ESCHERICHIA COLI; HYDROGEN BOND; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; X RAY ANALYSIS;

AMINO ACID SUBSTITUTION; BASE SEQUENCE; CATALYSIS; CRYSTALLOGRAPHY; DNA PRIMERS; ESCHERICHIA COLI; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; KINETICS; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; TRANSALDOLASE;

ESCHERICHIA COLI;

EID: 0242592798     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(98)01521-X     Document Type: Article

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