Folding pathway of the pyridoxal 5′-phosphate C-S lyase MalY from Escherichia coli

Biochemical Journal

Volumn 389, Issue 3, 2005, Pages 885-898

  Bertoldi, Mariarita ^a   Cellini, Barbara ^a   Laurents, Douglas V ^b   Borri Voltattorni, Carla ^a  

^a UNIVERSITY OF VERONA   (Italy)

^b CSIC   (Spain)

Author keywords

Aggregates; Escherichia coli; Folding; MalY; Pyridoxal 5 phosphate; Urea

Indexed keywords

AGGREGATES; CROSSLINKING; DIMERS; ENZYMES; FLUORESCENCE; MALTOSE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ULTRAVIOLET RADIATION; UREA;

FOLDING; HOLOENZYMES; MALY; PYRIDOXAL 5′-PHOSPHATE;

ESCHERICHIA COLI;

8 ANILINO 1 NAPHTHALENESULFONIC ACID; APOENZYME; CYSTATHIONINE BETA LYASE; CYSTATHIONINE BETA LYASE MALY; PYRIDOXAL 5 PHOSPHATE; UNCLASSIFIED DRUG; UREA;

ARTICLE; CONCENTRATION RESPONSE; DIMERIZATION; ENZYME ACTIVE SITE; ESCHERICHIA COLI; FLUORESCENCE; GEL FILTRATION; HYDROPHOBICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SPECTROSCOPY; ULTRAVIOLET RADIATION;

BINDING SITES; CYSTATHIONINE GAMMA-LYASE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; PROTEIN BINDING; PROTEIN FOLDING; PYRIDOXAL PHOSPHATE; REPRESSOR PROTEINS; UREA;

ESCHERICHIA COLI;

EID: 23644461960     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20050279     Document Type: Article

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