Aspergillus ficuum phytase: complete primary structure elucidation by chemical sequencing.
The primary structure of Aspergillus ficuum phytase was deduced from overlaps in peptide sequences. The unglycosylated enzyme is a 441 residue protein with a molecular mass of 48.5-KDa, as calculated from the total covalent structure. The estimated pl of the protein is about 4.76. Of the 19 Asn residues, 9 were found to be glycosylated. The phytase consists of 37% non-polar, 42% polar, 11.5% acidic, and 9.5% basic amino acids. The putative active site of the enzyme containing the sequence RHG is located at the N-terminal region of the molecule and shows homology to the active site of both microbial and mammalian acid phosphatases, and phosphoglycerate mutase.
Ullah
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Southern Regional Research Center, ARS, USDA, New Orleans, Louisiana 70124.
Dischinger
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D010832:6-Phytase / Q000737:chemistry*; D000595:Amino Acid Sequence; D001230:Aspergillus / Q000201:enzymology*; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017433:Protein Structure, Secondary
D010832:6-Phytase