Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Joseph L. Carlos"'
Publikováno v:
Biochemistry. 39:7276-7283
Type I signal peptidase (SPase I) catalyzes the hydrolytic cleavage of the N-terminal signal peptide from translocated preproteins. SPase I belongs to a novel class of Ser proteases that utilize a Ser/Lys dyad catalytic mechanism instead of the class
Autor:
Ross E. Dalbey, Greg Brubaker, Mark O. Lively, Andrew Karla, Guoqing Cao, Joseph L. Carlos, Patrick R. Bullinger, Christopher M. Ashwell, Mark Paetzel
Publikováno v:
The Journal of biological chemistry. 275(49)
Type I signal peptidase (SPase I) catalyzes the cleavage of the amino-terminal signal sequences from preproteins destined for cell export. Preproteins contain a signal sequence with a positively charged n-region, a hydrophobic h-region, and a neutral
Autor:
Tracy A. Schuenemann, James C. Samuelson, Joseph L. Carlos, Ross E. Dalbey, Natalie C. J. Strynadka, William R. Tschantz, Mark Paetzel, Philip A. Klenotic
Publikováno v:
The Journal of biological chemistry. 275(9)
Type I signal peptidases are integral membrane proteins that function to remove signal peptides from secreted and membrane proteins. These enzymes carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic ac