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.
Southern Regional Research Center, ARS, USDA, New Orleans, Louisiana 70124.
A H
AH
Ullah
H C
HC
Dischinger
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