Synergistic allostery, a sophisticated regulatory network for the control of aromatic amino acid biosynthesis in Mycobacterium tuberculosis

Journal of Biological Chemistry

Volumn 285, Issue 40, 2010, Pages 30567-30576

  Webby, Celia J ^a   Jiao, Wanting ^c   Hutton, Richard D ^c   Blackmore, Nicola J ^c   Baker, Heather M ^b   Baker, Edward N ^b   Jameson, Geoffrey B ^a   Parker, Emily J ^c  

^a MASSEY UNIVERSITY   (New Zealand)

^b UNIVERSITY OF AUCKLAND   (New Zealand)

^c UNIVERSITY OF CANTERBURY   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; AROMATIC COMPOUNDS; BINDING ENERGY; BINDING SITES; BIOCHEMISTRY; BIOSYNTHESIS; ENZYME ACTIVITY; ENZYMES; LAWS AND LEGISLATION; ORGANIC ACIDS; REACTION KINETICS; TRACE ELEMENTS;

ALLOSTERY; AROMATIC AMINO ACID; BINDING LOOP; END-PRODUCTS; ENZYMIC ACTIVITY; FEEDBACK REGULATION; HILL COEFFICIENT; HOMOTETRAMERS; HOMOTROPIC COOPERATIVITY; INHIBITOR COMBINATION; INHIBITORY CONCENTRATION; MICHAELIS-MENTEN KINETIC; MODE OF CONTROL; MYCOBACTERIUM TUBERCULOSIS; POTENTIAL DRUG; REGULATORY NETWORK; SHIKIMATE PATHWAY; SMALL DISPLACEMENT; SYNERGISTIC INHIBITION; SYNTHASES; TETRAMERS; TYPE II;

AROMATIZATION;

3 DEOXY 7 PHOSPHOHEPTULONATE SYNTHASE; AROMATIC AMINO ACID; ERYTHROSE 4 PHOSPHATE; PHENYLALANINE; PHOSPHATE; SHIKIMIC ACID; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; ERYTHROSE 4-PHOSPHATE; SUGAR PHOSPHATE;

ALLOSTERISM; AMINO ACID SYNTHESIS; ARTICLE; BACTERIAL GROWTH; BINDING SITE; CATALYSIS; CHEMICAL REACTION; CHEMICAL REACTION KINETICS; COMPLEX FORMATION; CONTROLLED STUDY; DRUG TARGETING; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SUBSTRATE; FEEDBACK SYSTEM; MICHAELIS MENTEN KINETICS; MYCOBACTERIUM TUBERCULOSIS; PRIORITY JOURNAL; STRUCTURE ANALYSIS; ANTAGONISTS AND INHIBITORS; BIOSYNTHESIS; KINETICS; METABOLISM; PHYSIOLOGY;

MYCOBACTERIUM TUBERCULOSIS;

3-DEOXY-7-PHOSPHOHEPTULONATE SYNTHASE; ALLOSTERIC REGULATION; AMINO ACIDS, AROMATIC; BACTERIAL PROTEINS; KINETICS; MYCOBACTERIUM TUBERCULOSIS; SUGAR PHOSPHATES;

EID: 77957276754     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.111856     Document Type: Article

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