The Thermoplasma acidophilum Lon protease has a Ser-Lys dyad active site

European Journal of Biochemistry

Volumn 271, Issue 22, 2004, Pages 4361-4365

  Besche, Henrike ^a   Zwickl, Peter ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

AAA+ protease; Archaea; Lon(La) endopeptidase; Lon(La) protease; Ser Lys dyad

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL ENZYME; ECLON PROTEASE; ENDOPEPTIDASE LA; LONA PROTEASE; LONB PROTEASE; LYSINE; PROTEINASE; SERINE; TALON PROTEASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; ATPASE DOMAIN; BACTERIAL GENE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME PURIFICATION; ESCHERICHIA COLI; GEL FILTRATION; GENOME; GRAM POSITIVE BACTERIUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; THERMOPLASMA ACIDOPHILUM;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARCHAEAL PROTEINS; BINDING SITES; ESCHERICHIA COLI; FLUORESCEIN-5-ISOTHIOCYANATE; KINETICS; LYSINE; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MUTAGENESIS, SITE-DIRECTED; PROTEASE LA; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SERINE; THERMOPLASMA;

ARCHAEA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; POSIBACTERIA; THERMOPLASMA; THERMOPLASMA ACIDOPHILUM;

EID: 9644272639     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04421.x     Document Type: Article

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