Leishmania mexicana mexicana gp63 is a site-specific neutral endopeptidase.
Leishmania mexicana, like other species of the genus, has a major 63-kDa surface glycoprotein (gp63) that is an active protease. Reports differ as to whether gp63 is a neutral or an acidic protease. Using three radiolabeled synthetic peptide substrates, gp63 purified from L. m. mexicana is most active at pH 6.5-7.5, in three different buffer systems, and appears to be a sequence-specific endopeptidase. The full extent of sequence specificity is undetermined, but these experiments suggest a strong preference for cleavage at serine or threonine residues. In common with other metalloproteases, the cleavage is on the amino side of the recognition residue.
Ip
H S
HS
Rockefeller University, New York, NY 10021.
Orn
A
A
Russell
D G
DG
Cross
G A
GA
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002855:Chromatography, Thin Layer; D010450:Endopeptidases / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D007894:Leishmania mexicana / Q000032:analysis*; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D015800:Protozoan Proteins / Q000032:analysis*
D015800:Protozoan Proteins; D010450:Endopeptidases; D008666:Metalloendopeptidases; C055146:glycoprotein gp63, Leishmania