title: Substrate specificity and screening of the integral membrane protease Pla.
abstract: This paper reports a study to find small peptide substrates for the important virulence factor of Yersinia pestis, plasminogen activator, Pla. The method used to find small substrates for this protease is reported along with studies examining the ability of these peptides to inhibit activity of the enzyme. Through the use of parallel synthesis and positional scanning, small tripeptides were identified that are viable substrates for the protease.
authors.affiliation: Chemical Biology Program, Department of Pharmacology and Toxicology, The University of Texas Medical Branch, 301 University Boulevard, Galveston, TX 77555-0650, USA.
authors.forename: Anton
authors.initials: A
authors.lastname: Agarkov
authors.forename: Sadhana
authors.initials: S
authors.lastname: Chauhan
authors.forename: Pedro J
authors.initials: PJ
authors.lastname: Lory
authors.forename: Scott R
authors.initials: SR
authors.lastname: Gilbertson
authors.forename: Vladimir L
authors.initials: VL
authors.lastname: Motin
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D005470:Fluorometry; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D010960:Plasminogen Activators / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D011480:Protease Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D015010:Yersinia pestis / Q000201:enzymology
chemical_list: D001426:Bacterial Proteins; D009842:Oligopeptides; D010455:Peptides; D011480:Protease Inhibitors; C078140:Pla protease, Yersinia pestis; D010960:Plasminogen Activators