title: An essential tryptophan residue in alkaline phosphatase from pearl oyster (Pinctada fucata).
abstract: 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.
authors.affiliation: Institute of Marine Biotechnology, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing, 100084, China.
authors.forename: Li-Ping
authors.initials: LP
authors.lastname: Xie
authors.forename: Guang-Rui
authors.initials: GR
authors.lastname: Xu
authors.forename: Wei-Zhong
authors.initials: WZ
authors.lastname: Cao
authors.forename: Jin
authors.initials: J
authors.lastname: Zhang
authors.forename: Rong-Qing
authors.initials: RQ
authors.lastname: Zhang
mesh_terms: D000469:Alkaline Phosphatase / Q000737:chemistry*; D000818:Animals; D001974:Bromosuccinimide / Q000737:chemistry; D007700:Kinetics; D049911:Pinctada / Q000201:enzymology*; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D014364:Tryptophan / Q000737:chemistry*
chemical_list: D014364:Tryptophan; D000469:Alkaline Phosphatase; D001974:Bromosuccinimide