Identification of Active-Site Residues in Aspergillus ficuum Extracellular pH 2.5 Optimum Acid Phosphatase
Copyright policy )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.
- Southern Regional Research Center United States
- Agricultural Research Service United States
Binding Sites, Sequence Homology, Amino Acid, Acid Phosphatase, Molecular Sequence Data, Serine Endopeptidases, Hydrogen-Ion Concentration, Peptide Mapping, Cysteine Endopeptidases, Aspergillus, Humans, Amino Acid Sequence
Binding Sites, Sequence Homology, Amino Acid, Acid Phosphatase, Molecular Sequence Data, Serine Endopeptidases, Hydrogen-Ion Concentration, Peptide Mapping, Cysteine Endopeptidases, Aspergillus, Humans, Amino Acid Sequence
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