Biochemistry (Moscow)

, Volume 73, Issue 1, pp 87–91 | Cite as

An essential tryptophan residue in alkaline phosphatase from pearl oyster (Pinctada fucata)

  • Li-Ping Xie
  • Guang-Rui Xu
  • Wei-Zhong Cao
  • Jin Zhang
  • Rong-Qing ZhangEmail author


Alkaline phosphatases are ubiquitous enzymes found in most species including the pearl oyster, Pinctada fucata, where it is presumably involved in nacreous biomineralization processes. In the present study, we have purified alkaline phosphatases from the pearl oyster and modified the tryptophan residues using N-bromosuccinimide (NBS). We show that the resulting inactivation of purified alkaline phosphatase by NBS is dependent on modification of only one of five tryptophan residues in the enzyme. Substrate protection experiments showed that the tryptophan residue was not located at the substrate-binding site but was involved in the catalytic activity.

Key words

alkaline phosphatase Pinctada fucata chemical modification kinetics 



alkaline phosphatase




Pinctada fucata alkaline phosphatase


p-nitrophenyl phosphate


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Copyright information

© Pleiades Publishing, Ltd. 2008

Authors and Affiliations

  • Li-Ping Xie
    • 1
    • 2
  • Guang-Rui Xu
    • 1
  • Wei-Zhong Cao
    • 1
  • Jin Zhang
    • 1
  • Rong-Qing Zhang
    • 1
    • 2
    Email author
  1. 1.Institute of Marine Biotechnology, Department of Biological Sciences and BiotechnologyTsinghua UniversityBeijingChina
  2. 2.Protein Science Laboratory of the Ministry of EducationTsinghua UniversityBeijingChina

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