pheA (Rv3838c) of Mycobacterium tuberculosis encodes an allosterically regulated monofunctional prephenate dehydratase that requires both catalytic and regulatory domains for optimum activity

Journal of Biological Chemistry

Volumn 280, Issue 21, 2005, Pages 20666-20671

  Prakash, Prachee ^a   Pathak, Niteen ^a   Hasnain, Seyed E ^a,b  

^a CENTRE FOR DNA FINGERPRINTING AND DIAGNOSTICS   (India)

^b JAWAHARLAL NEHRU CENTRE FOR ADVANCED SCIENTIFIC RESEARCH   (India)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYST ACTIVITY; GENES; PROTEINS; PULMONARY DISEASES;

BIOCHEMICAL PROPERTIES; MUTASE ACTIVITY; MYCOBACTERIUM TUBERCULOSIS; REGULATORY DOMAINS;

BACTERIA;

AROMATIC AMINO ACID; CHORISMATE MUTASE; IRON; PHENYLALANINE; PREPHENATE DEHYDRATASE; TRYPTOPHAN; TYROSINE;

ALLOSTERISM; AMINO ACID SYNTHESIS; ARTICLE; BACTERIAL GENE; CATALYSIS; CONTROLLED STUDY; ENTEROBACTERIACEAE; ENZYME ACTIVITY; ENZYME REGULATION; GENE EXPRESSION; IN VITRO STUDY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PHEA GENE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION;

ALLOSTERIC REGULATION; AMINO ACIDS, AROMATIC; BINDING SITES; CATALYSIS; CHORISMATE MUTASE; CHROMATOGRAPHY, GEL; CLONING, MOLECULAR; ENZYME ACTIVATION; ESCHERICHIA COLI; GENE EXPRESSION; GENES, BACTERIAL; MOLECULAR WEIGHT; MYCOBACTERIUM TUBERCULOSIS; PHENYLALANINE; PREPHENATE DEHYDRATASE; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SODIUM CHLORIDE; SPECTROMETRY, FLUORESCENCE; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSFECTION;

BACTERIA (MICROORGANISMS); ENTERIC BACTERIA; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS;

EID: 20144367379     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M502107200     Document Type: Article

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