Brugia pahangi: identification and characterization of an aminopeptidase associated with larval molting.
The third-stage larvae (L3) of the filarid parasite Brugia pahangi were surveyed for protease activity beginning with release from the mosquito vector through molting to the fourth-stage larvae (L4). A metalloaminopeptidase with a substrate preference for phenylalanine was released during the molting process. A screen of aminopeptidase inhibitors identified H-boroPhenylalanine-(pinacol) as highly effective, with a Ki of 1.3 x 10(-11) M. This peptidase inhibitor also arrested molting of L3 larvae in vitro at a concentration of 100 microM.
Hong
X
X
Department of Veterans Affairs Medical Center, Anatomic Pathology Service--113B, San Francisco, California 94121.
Bouvier
J
J
Wong
M M
MM
Yamagata
G Y
GY
McKerrow
J H
JH
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D001896:Boron Compounds / Q000494:pharmacology; D017179:Brugia pahangi / Q000201:enzymology* / Q000254:growth & development; D006020:Glycopeptides / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007814:Larva / Q000201:enzymology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000494:pharmacology; D010649:Phenylalanine / Q000378:metabolism; D013379:Substrate Specificity
D001896:Boron Compounds; D006020:Glycopeptides; C080316:H-borophenylalanyl-(pinacol); D009842:Oligopeptides; D010649:Phenylalanine; D000626:Aminopeptidases; C008890:phosphoramidon