The Lon protease from Mycobacterium smegmatis: Molecular cloning, sequence analysis, functional expression, and enzymatic characterization

Biochemistry

Volumn 37, Issue 1, 1998, Pages 377-386

  Roudiak, Stanislav G ^a   Seth, Anjali ^a   Knipfer, Nancianne ^a   Shrader, Thomas E ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALANINE; BACTERIAL ENZYME; BACTERIAL PROTEIN; CHYMOTRYPSIN; CYSTEINE; DEOXYADENOSINE TRIPHOSPHATE; PEPTIDASE; PROTEASOME; PROTEINASE; SERINE; THREONINE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SUBSTRATE; ESCHERICHIA COLI; MOLECULAR CLONING; MYCOBACTERIUM SMEGMATIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; ATP-DEPENDENT PROTEASES; BINDING SITES; CLONING, MOLECULAR; CONSERVED SEQUENCE; CYSTEINE ENDOPEPTIDASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENES, BACTERIAL; GENETIC COMPLEMENTATION TEST; HEAT-SHOCK PROTEINS; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; MYCOBACTERIUM; PROTEASE LA; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PYRIMIDINE NUCLEOTIDES; RECOMBINANT FUSION PROTEINS; SERINE ENDOPEPTIDASES; SPECIES SPECIFICITY; SUBSTRATE SPECIFICITY;

EID: 0032488632     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971732f     Document Type: Article

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