Asp 280 residue is important in the activity of the Escherichia coli leader peptidase

Experimental and Molecular Medicine

Volumn 31, Issue 2, 1999, Pages 65-70

  Sung, Meesook ^a   Park, Kwangsook ^b  

^a Catholic Kwandong University   (South Korea)

^b Korea University   (South Korea)

Author keywords

Escherichia coli; Leader peptidase (signal peptidase) site directed mutagenesis

Indexed keywords

ALANINE; ARGININE; ASPARAGINE; GLUTAMIC ACID; GLYCINE; MEMBRANE PROTEIN; SIGNAL PEPTIDASE; SIGNAL PEPTIDE; ASPARTIC ACID; MICROCOCCAL NUCLEASE; OLIGONUCLEOTIDE; OUTER MEMBRANE PROTEIN; PRO OMPA NUCLEASE A; PRO-OMPA NUCLEASE A; PROTEIN PRECURSOR; SERINE PROTEINASE; TYPE I SIGNAL PEPTIDASE;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONSENSUS SEQUENCE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE SEQUENCE; SITE DIRECTED MUTAGENESIS; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; RETRACTED ARTICLE; STRUCTURE ACTIVITY RELATION; WESTERN BLOTTING;

ESCHERICHIA COLI;

ASPARTIC ACID; BACTERIAL OUTER MEMBRANE PROTEINS; BLOTTING, WESTERN; ESCHERICHIA COLI; MEMBRANE PROTEINS; MICROCOCCAL NUCLEASE; MUTAGENESIS, SITE-DIRECTED; OLIGONUCLEOTIDES; PROTEIN PRECURSORS; SERINE ENDOPEPTIDASES; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0033617819     PISSN: 12263613     EISSN: 20926413     Source Type: Journal    
DOI: 10.1038/emm.1999.11     Document Type: Article

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