Differential effects of temperature and hydrostatic pressure on the formation of quinonoid intermediates from L-Trp and L-Met by H463F mutant Escherichia coli tryptophan indole-lyase

Biochemistry

Volumn 44, Issue 43, 2005, Pages 14289-14297

  Phillips, Robert S ^a   Holtermann, Georg ^b  

^a UNIVERSITY OF GEORGIA   (United States)

^b MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIUM COMPOUNDS; CATALYSIS; DIMERS; ENZYMES; HYDROSTATIC PRESSURE; QUANTUM THEORY; RATE CONSTANTS;

PROTEIN MOTION; QUANTUM MECHANICAL TUNNELING; QUINONOID INTERMEDIATES; TRYPTOPHAN INDOLE-LYASE;

ESCHERICHIA COLI;

AMMONIUM DERIVATIVE; BACTERIAL ENZYME; CYSTEINE DERIVATIVE; DIMER; ENZYME INHIBITOR; IMINE; INDOLE DERIVATIVE; LYASE; METHIONINE; MUTANT PROTEIN; PYRIDOXAL 5 PHOSPHATE; PYRUVIC ACID DERIVATIVE; QUINONE DERIVATIVE; S (2 NITROPHENYL)CYSTEINE; S ETHYLCYSTEINE; TRYPTOPHAN; TRYPTOPHAN INDOLE LYASE; UNCLASSIFIED DRUG;

ABSORPTION SPECTROSCOPY; ARTICLE; BACTERIUM MUTANT; BIOSYNTHESIS; CATALYST; CHEMICAL REACTION; COMPLEX FORMATION; CONCENTRATION RESPONSE; CONTROLLED STUDY; ELIMINATION REACTION; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SUBSTRATE; EQUILIBRIUM CONSTANT; ESCHERICHIA COLI; HYBRID; HYDROSTATIC PRESSURE; MOLECULAR INTERACTION; NONHUMAN; PARAMETER; PRESSURE; PRIORITY JOURNAL; PROTEIN TRANSPORT; PROTON TRANSPORT; QUANTUM MECHANICS; REACTION ANALYSIS; SPECTROPHOTOMETRY; TEMPERATURE DEPENDENCE; WILD TYPE;

AMINO ACID SUBSTITUTION; BINDING, COMPETITIVE; ESCHERICHIA COLI; HISTIDINE; HYDROSTATIC PRESSURE; KINETICS; METHIONINE; MUTATION; PHENYLALANINE; QUINONES; TEMPERATURE; TRYPTOPHAN; TRYPTOPHANASE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 27444442894     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051062a     Document Type: Article

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