Moonlighting function of glutamate racemase from Mycobacterium tuberculosis: Racemization and DNA gyrase inhibition are two independent activities of the enzyme

Microbiology

Volumn 154, Issue 9, 2008, Pages 2796-2803

  Sengupta, Sugopa ^a   Ghosh, Soumitra ^a   Nagaraja, Valakunja ^a,b  

^a INDIAN INSTITUTE OF SCIENCE   (India)

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

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CIPROFLOXACIN; DNA TOPOISOMERASE (ATP HYDROLYSING); GLUTAMATE RACEMASE; RACEMASE; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; GLUTAMIC ACID; ISOMERASE; PEPTIDOGLYCAN;

ANTIBIOTIC SENSITIVITY; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INHIBITION; ENZYME REGULATION; GENE OVEREXPRESSION; IN VIVO STUDY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA INTERACTION; RACEMIZATION; ANTIBIOTIC RESISTANCE; BACTERIAL GENE; CELL WALL; DRUG ANTAGONISM; DRUG EFFECT; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; METABOLISM; MYCOBACTERIUM SMEGMATIS; SITE DIRECTED MUTAGENESIS;

BACTERIA (MICROORGANISMS); MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS;

AMINO ACID ISOMERASES; ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; CELL WALL; CIPROFLOXACIN; DNA GYRASE; DRUG RESISTANCE, BACTERIAL; ESCHERICHIA COLI; GENES, BACTERIAL; GLUTAMIC ACID; MUTAGENESIS, SITE-DIRECTED; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; PEPTIDOGLYCAN;

EID: 53449086920     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.2008/020933-0     Document Type: Article

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