Purified recombinant hypothetical protein coded by open reading frame Rv1885c of Mycobacterium tuberculosis exhibits a monofunctional AroQ class of periplasmic chorismate mutase activity

Journal of Biological Chemistry

Volumn 280, Issue 20, 2005, Pages 19641-19648

  Prakash, Prachee ^a   Aruna, Bandi ^a   Sardesai, Abhijit A ^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

BACTERIA; BIOCHEMISTRY; DISEASE CONTROL; ENZYMES; ESCHERICHIA COLI; GENETIC ENGINEERING; PURIFICATION; YEAST;

CHORISMATE MUTASE; ENZYME STRUCTURE; MYOBACTERIUM TUBERCULOSIS (MTB); PROTEOLYTIC CLEAVAGE;

PROTEINS;

CHORISMATE MUTASE; LIGAND; OXIDOREDUCTASE; PREPHENATE DEHYDRATASE; PROTEIN AROQ; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; BACTERIAL DNA; BACTERIAL PROTEIN; SIGNAL PEPTIDE;

ALLOSTERISM; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL GENOME; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME REGULATION; ENZYME STRUCTURE; ESCHERICHIA COLI; IN VITRO STUDY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; SEQUENCE HOMOLOGY; YEAST; CLASSIFICATION; COMPARATIVE STUDY; CYTOPLASM; DIMERIZATION; ENZYMOLOGY; GENETICS; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MYCOBACTERIUM TUBERCULOSIS;

ALLOSTERIC REGULATION; BACTERIAL PROTEINS; BASE SEQUENCE; CHORISMATE MUTASE; DIMERIZATION; DNA, BACTERIAL; ESCHERICHIA COLI; KINETICS; LIGANDS; MYCOBACTERIUM TUBERCULOSIS; OPEN READING FRAMES; PERIPLASM; PROTEIN SORTING SIGNALS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS;

EID: 21244483507     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M413026200     Document Type: Article

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