Probing the catalytic allosteric mechanism of rabbit muscle pyruvate kinase by tryptophan fluorescence quenching

European Biophysics Journal

Volumn 41, Issue 7, 2012, Pages 607-614

  Li, Feng ^a   Yu, Ting ^a   Zhao, Yuwei ^a   Yu, Shaoning ^a  

^a FUDAN UNIVERSITY   (China)

Author keywords

Allosteric mechanism; Catalysis; Conformational change; Fluorescence; Glycolytic pathway; Pyruvate kinase; Quenching

Indexed keywords

PYRUVATE KINASE; TRYPTOPHAN;

ALLOSTERISM; AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; GENETICS; MOLECULAR GENETICS; MUSCLE; RABBIT; SITE DIRECTED MUTAGENESIS; SPECTROFLUOROMETRY;

ALLOSTERIC REGULATION; ALLOSTERIC SITE; AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUSCLES; MUTAGENESIS, SITE-DIRECTED; PYRUVATE KINASE; RABBITS; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

ORYCTOLAGUS CUNICULUS;

EID: 84866378057     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-012-0828-2     Document Type: Article

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