Conservation of cysteine residues in fungal histidine acid phytases.
Amino acid sequence analysis of fungal histidine acid phosphatases displaying phytase activity has revealed a conserved eight-cysteine motif. These conserved amino acids are not directly associated with catalytic function; rather they appear to be essential in the formation of disulfide bridges. Their role is seen as being similar to another eight-cysteine motif recently reported in the amino acid sequence of nearly 500 plant polypeptides. An additional disulfide bridge formed by two cysteines at the N-terminus of all the filamentous ascomycete phytases was also observed. Disulfide bridges are known to increase both stability and heat tolerance in proteins. It is therefore plausible that this extra disulfide bridge contributes to the higher stability found in phytase from some Aspergillus species. To engineer an enhanced phytase for the feed industry, it is imperative that the role of disulfide bridges be taken into cognizance and possibly be increased in number to further elevate stability in this enzyme.
Mullaney
Edward J
EJ
Southern Regional Research Center, Agricultural Research Service, United States Department of Agriculture, New Orleans, LA 70124, USA. emul@srrc.ars.usda.gov
Ullah
Abul H J
AH
D010832:6-Phytase / Q000737:chemistry*; D000135:Acid Phosphatase / Q000737:chemistry*; D000595:Amino Acid Sequence; D001232:Aspergillus fumigatus / Q000201:enzymology*; D001234:Aspergillus niger / Q000201:enzymology*; D017124:Conserved Sequence; D003545:Cysteine / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry; D006639:Histidine / Q000737:chemistry*; D008969:Molecular Sequence Data; D016415:Sequence Alignment / Q000379:methods; D020539:Sequence Analysis, Protein / Q000379:methods*; D017386:Sequence Homology, Amino Acid
D004220:Disulfides; D006639:Histidine; D000135:Acid Phosphatase; D010832:6-Phytase; D003545:Cysteine