A putative proline iminopeptidase of Thermotoga maritima is a leucine aminopeptidese with lysine-p-nitroanilide hydrolyzing activity

Enzyme and Microbial Technology

Volumn 32, Issue 3-4, 2003, Pages 414-421

  Ratnayake, Sunil ^a   Selvarkumar, Ponniah ^a   Hayashi, Kiyoshi ^a  

^a NATIONAL FOOD RESEARCH INSTITUTE   (Japan)

Author keywords

Cloning; Leucine aminopeptidase; Substrate specificity; Thermostability; Thermotoga maritima

Indexed keywords

AMINO ACIDS; CHROMATOGRAPHY; ENZYME INHIBITION; ENZYME KINETICS; ESCHERICHIA COLI; HIGH TEMPERATURE EFFECTS; MOLECULAR WEIGHT; PH EFFECTS; POSITIVE IONS;

ENZYME PURIFICATION;

ENZYMES;

ANILIDE; CADMIUM; CALCIUM ION; COBALT; COPPER ION; CYTOSOL AMINOPEPTIDASE; DIVALENT CATION; LEAD; MAGNESIUM ION; MANGANESE; PROLINE IMINOPEPTIDASE; ZINC ION;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME PURIFICATION; ENZYME STRUCTURE; ESCHERICHIA COLI; GENE EXPRESSION; HYDROLYSIS; ION EXCHANGE CHROMATOGRAPHY; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN EXPRESSION; PROTEIN FAMILY; TEMPERATURE DEPENDENCE; THERMOSTABILITY; THERMOTOGA MARITIMA;

ESCHERICHIA COLI; THERMOTOGA; THERMOTOGA MARITIMA;

EID: 0037416676     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(02)00311-3     Document Type: Article

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