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Title:The prlC Suppressor Phenotype and Its Relation to Oligopeptidase a Specificity
Author(s):Flores, Theresa M.
Doctoral Committee Chair(s):Miller, Charles G.
Department / Program:Microbiology
Discipline:Microbiology
Degree Granting Institution:University of Illinois at Urbana-Champaign
Degree:Ph.D.
Genre:Dissertation
Subject(s):Biology, Molecular
Abstract:Comparisons of the prlC mutations with the crystal structure of Neurolysin reveal that the mutations are clustered in regions which are believed to affect access of substrates to the active site, not the active site itself. The prlC mutations may allow previously-restricted substrates to present their N-termini to the active site of OpdA. Because the PrlC mutant proteins suppress many different signal peptide mutations with no changes in the active site of OpdA, it is likely that wildtype OpdA also recognizes substrates of different lengths and sequences.
Issue Date:2001
Type:Text
Language:English
Description:102 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2001.
URI:http://hdl.handle.net/2142/86629
Other Identifier(s):(MiAaPQ)AAI3023057
Date Available in IDEALS:2015-09-28
Date Deposited:2001


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