Dipeptidyl-peptidase IV secreted by Aspergillus fumigatus, a fungus pathogenic to humans.
A dipeptidyl-peptidase IV was purified from the culture medium of the human-pathogenic fungus Aspergillus fumigatus. The enzyme has an apparent molecular mass of 95 kDa and contained approximately 10 kDa of N-linked carbohydrate. This glycoprotein is antigenic and has all characteristics of the class IV dipeptidyl-peptidases: removal of Xaa-Pro and to a lesser extent Xaa-Ala dipeptides from the N termini of peptides, including bioactive peptides such as neuropeptide Y, [des-Arg1] bradykinin, and glucagon-like peptide 1, activity at neutral pH, and presence in the amino acid sequence of the Gly-X-Ser-X-Gly consensus motif of the serine-hydrolases and the putative catalytic triad (Ser613, Asp690, His725) of the dipeptidyl-peptidases. Moreover, the last 200 amino acids displayed 60 to 65% similarity with the other dipeptidyl-peptidases IV from rat, mouse, human, and yeast. However, unlike the other dipeptidyl-peptidases, the dipeptidyl-peptidase IV of A. fumigatus is a secreted enzyme with a cleavable signal peptide. Expression of a recombinant dipeptidyl-peptidase IV of A. fumigatus has been attained in the yeast Pichia pastoris.
Beauvais
A
A
Laboratoire des Aspergillus, Institut Pasteur, Paris, France.
Monod
M
M
Wyniger
J
J
Debeaupuis
J P
JP
Grouzmann
E
E
Brakch
N
N
Svab
J
J
Hovanessian
A G
AG
Latgé
J P
JP
D000595:Amino Acid Sequence; D000818:Animals; D015703:Antigens, CD / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D001232:Aspergillus fumigatus / Q000201:enzymology*; D001483:Base Sequence; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D010843:Pichia / Q000235:genetics; D051381:Rats; D011994:Recombinant Proteins / Q000096:biosynthesis
D015703:Antigens, CD; D011994:Recombinant Proteins