Ej. Mullaney et Ahj. Ullah, IDENTIFICATION OF A HISTIDINE ACID-PHOSPHATASE (PHYA)-LIKE GENE IN ARABIDOPSIS-THALIANA, Biochemical and biophysical research communications (Print), 251(1), 1998, pp. 252-255
A close examination of the protein sequence encoded by the Arabidopsis
thaliana gene F21M12.26 reveals the gene product to be a phosphomonoe
sterase, acid optimum (EC 3.1.3.2). A subclass of this broad acid phos
phatase is also known as 'histidine acid phosphatase.' This is the fir
st sequence-based evidence for a 'histidine acid phosphatase' in a dic
otyledon. One important member of this class of enzymes is Aspergillus
niger (ficuum) phytase, which came into prominence for its commercial
application as a feed additive. The putative protein from A. thaliana
gene F21M12.26 shares many important features of Aspergillus phytase,
namely, size, active-site sequence, catalytic dipeptide and ten cyste
ine residues located in the key areas of the molecule, but lacks all n
ine N-glycosylation sites. (C) 1998 Academic Press.