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Title:A Comparative Study of the Substrate Specificities of Peptidases A, B, and N From Salmonella Typhimurium
Author(s):Mathew, Zacharia
Doctoral Committee Chair(s):Miller, Charles G.
Department / Program:Microbiology
Degree Granting Institution:University of Illinois at Urbana-Champaign
Subject(s):Biology, Microbiology
Abstract:To understand the function of Peptidase B (PepB) we have sequenced the pepB gene and purified its product. Two other peptidases, PepA and PepN, have also been purified to compare their substrate specificities with PepB. PepB has been assigned to the M17 family of peptidases on the basis of similarities in amino acid sequence and biochemical properties. PepB is a broad specificity aminopeptidase with a unique ability to remove Asp residues and a very efficient ability to remove Glu residues from the N-termini of peptides in than PepA and PepN. PepA, on the other hand, removes Pro residues, a function lacking in PepB and PepN. PepN has the unique ability of removing Gly residues from the N-terminus of peptides. The removal of amino acids from the N-terminus is also dependent on what kind of amino acid is present in the second position of the peptides. Neither PepA, PepB, nor PepN are processive in hydrolyzing their substrates. We have demonstrated the cooperation of PepA, PepB, and PepN in hydrolyzing some of their substrates.
Issue Date:1999
Description:150 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1999.
Other Identifier(s):(MiAaPQ)AAI9953090
Date Available in IDEALS:2015-09-28
Date Deposited:1999

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