A Comparative Study of the Substrate Specificities of Peptidases A, B, and N From Salmonella Typhimurium

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.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Microbiology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Mathew, Zacharia

Contributors dc:contributor

• Miller, Charles G.

• Biology, Microbiology

Language dc:language

eng

Identifier

(MiAaPQ)AAI9953090

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/86749