Site-directed mutagenesis analysis of amino acids critical for activity of the type I signal peptidase of the archaeon Methanococcus voltae.
Site-directed mutagenesis studies of the signal peptidase of the methanogenic archaeon Methanococcus voltae identified three conserved residues (Ser52, His122, and Asp148) critical for activity. The requirement for one conserved aspartic acid residue distinguishes the archaeal enzyme from both the Escherichia coli and yeast Sec11 enzymes.
Bardy
Sonia L
SL
Department of Microbiology and Immunology, Queen's University, Kingston, ON, Canada K7L 3N6.
Ng
Sandy Y M
SY
Carnegie
David S
DS
Jarrell
Ken F
KF
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D019843:Archaeal Proteins / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D001483:Base Sequence; D017124:Conserved Sequence; D017931:DNA Primers; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D017017:Methanococcus / Q000201:enzymology*; D016297:Mutagenesis, Site-Directed; D016415:Sequence Alignment; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism*
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D017931:DNA Primers; D008565:Membrane Proteins; D012697:Serine Endopeptidases; C026515:type I signal peptidase