Isothermal titration microcalorimetry reveals the cooperative and noncompetitive nature of inhibition of Sinorhizobium meliloti L5-30 dihydrodipicolinate synthase by (S)-lysine

Biochemistry

Volumn 47, Issue 30, 2008, Pages 7779-7781

  Phenix, Christopher P ^a,b   Palmer, David R J ^a  

^a UNIVERSITY OF SASKATCHEWAN   (Canada)

^b TRIUMF   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CALORIMETERS; ENZYMES; FOOD ADDITIVES; TITRATION; VOLUMETRIC ANALYSIS;

ALDOLASE; CLASS I; DIHYDRODIPICOLINATE SYNTHASE; INHIBITOR BINDING; ISOTHERMAL TITRATION MICROCALORIMETRY (ITM); PYRUVATE; SINORHIZOBIUM MELILOTI;

AMINO ACIDS;

2 OXOBUTYRIC ACID; APOENZYME; BACTERIAL ENZYME; DIHYDRODIPICOLINATE SYNTHASE; LYSINE; PYRUVIC ACID; SYNTHETASE;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENERGY TRANSFER; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME STRUCTURE; ISOTHERMAL TITRATION CALORIMETRY; MICROCALORIMETRY; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; SINORHIZOBIUM MELILOTI; THERMODYNAMICS;

BUTYRIC ACIDS; CALORIMETRY; HYDRO-LYASES; LYSINE; PROTEIN BINDING; PYRUVIC ACID; SINORHIZOBIUM MELILOTI; THERMODYNAMICS;

SINORHIZOBIUM MELILOTI;

EID: 48249120348     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800629n     Document Type: Article

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