Pintus, F., Spano, D., Corongiu, S. et al. Biochemistry Moscow (2011) 76: 694. doi:10.1134/S0006297911060101
A purple acid phosphatase was purified to homogeneity from Euphorbia characias latex. The native protein has a molecular mass of 130 ± 10 kDa and is formed by two apparently identical subunits, each containing one Fe(III) and one Zn(II) ion. The two subunits are connected by a disulfide bridge. The enzyme has an absorbance maximum at 540 nm, conferring a characteristic purple color due to a charge-transfer transition caused by a tyrosine residue (Tyr172) coordinated to the ferric ion. The cDNA nucleotide sequence contains an open reading frame of 1392 bp, and the deduced sequence of 463 amino acids shares a very high degree of identity (92–99%) to other purple acid phosphatases isolated from several higher plants. The enzyme hydrolyzes well p-nitrophenyl phosphate, a typical artificial substrate, and a broad range of natural phosphorylated substrates, such as ATP, ADP, glucose-6-phosphate, and phosphoenolpyruvate. The enzyme displays a pH optimum of 5.75 and is inhibited by molybdate, vanadate, and Zn2+, which are typical acid phosphatase inhibitors.
acid phosphataseEuphorbia characiasiron ionmetalloenzymespurple phosphatasezinc ion
Euphorbia latex purple acid phosphatase (protein)
purple acid phosphatases
reverse transcription-polymerase chain reaction
sodium dodecyl sulfate polyacrylamide gel electrophoresis