Amino-terminal extension present in the methionine aminopeptidase type 1c of Mycobacterium tuberculosis is indispensible for its activity

BMC Biochemistry

Volumn 12, Issue 1, 2011, Pages

  Kanudia, Pavitra ^a   Mittal, Monica ^a   Kumaran, Sangaralingam ^a   Chakraborti, Pradip K ^a  

^a INSTITUTE OF MICROBIAL TECHNOLOGY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; METHIONYL AMINOPEPTIDASE; METHIONYL AMINOPEPTIDASE TYPE 1C; PROLINE; UNCLASSIFIED DRUG; VALINE; AMINOPEPTIDASE; HISTIDINE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL GENE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME METABOLISM; ENZYME STABILITY; MOLECULAR CLONING; MOLECULAR DYNAMICS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; CHEMISTRY; CIRCULAR DICHROISM; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; METABOLISM; MUTATION;

ESCHERICHIA COLI; EUKARYOTA; MYCOBACTERIUM TUBERCULOSIS; PROKARYOTA;

AMINOPEPTIDASES; CATALYTIC DOMAIN; CIRCULAR DICHROISM; CLONING, MOLECULAR; ENZYME STABILITY; ESCHERICHIA COLI; HISTIDINE; MUTATION; MYCOBACTERIUM TUBERCULOSIS; PROLINE; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; VALINE;

EID: 79959830296     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-12-35     Document Type: Article

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