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.
Rockefeller University, New York, NY 10021.
H S
HS
Ip
A
A
Orn
D G
DG
Russell
G A
GA
Cross
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