Amino acid residues involved in autophosphorylation and phosphotransfer activities are distinct in nucleoside diphosphate kinase from Mycobacterium tuberculosis

Journal of Biological Chemistry

Volumn 279, Issue 42, 2004, Pages 43595-43603

  Tiwari, Sangeeta ^a,b   Radha Kishan, K V ^a   Chakrabarti, Tapan ^a   Chakraborti, Pradip K ^a  

^a INSTITUTE OF MICROBIAL TECHNOLOGY   (India)

^b NATIONAL CHEMICAL LABORATORY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; GEL PERMEATION CHROMATOGRAPHY; MICROORGANISMS; MONOMERS; MUTAGENESIS;

AUTOPHOSPHORYLATION; HEXAMERS; RECOMBINANT PROTEINS;

ENZYMES;

AMINO ACID; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; NUCLEOSIDE DIPHOSPHATE KINASE;

ARTICLE; AUTOPHOSPHORYLATION; ENZYME PHOSPHORYLATION; GEL PERMEATION CHROMATOGRAPHY; MOLECULAR CLONING; MOLECULAR WEIGHT; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION;

AMINO ACIDS; BASE SEQUENCE; CLONING, MOLECULAR; DNA PRIMERS; ESCHERICHIA COLI; KINETICS; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; NUCLEOSIDE-DIPHOSPHATE KINASE; PHOSPHORYLATION; PHOSPHOTRANSFERASES; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; RESTRICTION MAPPING;

ACTINOBACTERIA (CLASS); BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS; PROKARYOTA; PSEUDOMONAS; PSEUDOMONAS AERUGINOSA; UNCULTURED ACTINOMYCETE;

EID: 6344237576     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M401704200     Document Type: Article

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