Conservation of structure and mechanism within the transaldolase enzyme family

FEBS Journal

Volumn 279, Issue 5, 2012, Pages 766-778

  Samland, Anne K ^a   Baier, Shiromi ^a   Schürmann, Melanie ^b   Inoue, Tomoyuki ^a   Huf, Sabine ^a   Schneider, Gunter ^c   Sprenger, Georg A ^a   Sandalova, Tatyana ^c  

^a UNIVERSITY OF STUTTGART   (Germany)

^b FORSCHUNGSZENTRUM JÜLICH   (Germany)

^c KAROLINSKA INSTITUTE   (Sweden)

Author keywords

mechanism; structure; substrate specificity; thermostability; transaldolase

Indexed keywords

DIMER; MONOMER; PHOSPHATASE; TRANSALDOLASE;

ARTICLE; BACILLUS SUBTILIS; BINDING SITE; CATALYSIS; CONTROLLED STUDY; CORYNEBACTERIUM GLUTAMICUM; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ESCHERICHIA COLI; MESOPHILIC BACTERIUM; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN FOLDING; THERMOPHILIC BACTERIUM; THERMOSTABILITY;

AMINO ACID SEQUENCE; BACILLUS SUBTILIS; BINDING SITES; CLONING, MOLECULAR; CORYNEBACTERIUM GLUTAMICUM; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHYLOGENY; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TRANSALDOLASE;

BACILLUS SUBTILIS; CORYNEBACTERIUM GLUTAMICUM; ESCHERICHIA COLI;

EID: 84857645075     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08467.x     Document Type: Article

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