Identification of active-site residues in Aspergillus ficuum extracellular pH 2.5 optimum acid phosphatase.
Primary structure elucidation of peptides generated by cyanogen bromide, endoproteinase Glu-C, and clostripain cleavage of an Aspergillus ficuum extracellular pH optimum 2.5 acid phosphatase identified a region which contains the active site of the enzyme. The 23-residue segment contains the fragment RHGXRXP, which is homologous to acid phosphatase from Saccharomyces spp., Aspergillus ficuum, mammals, and bacteria. Homologous or conservative substitutions are observed in the 10-amino acid fragment preceding this region.
Ullah
A H
AH
Southern Regional Research Center, ARS, USDA, New Orleans, Louisiana 70124.
Dischinger
H C
HC
D000135:Acid Phosphatase / Q000737:chemistry*; D000595:Amino Acid Sequence; D001230:Aspergillus / Q000201:enzymology*; D001665:Binding Sites; D003546:Cysteine Endopeptidases; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases
D000135:Acid Phosphatase; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D003546:Cysteine Endopeptidases; C019913:clostripain