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A Bioinformatic Exploration of Alkaline Phosphatase Structure and Mechanism: a Complement to the Traditional Kinetics Laboratory
Author(s) -
Grunwald Sandra
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.a976-a
Subject(s) - alkaline phosphatase , kinetics , enzyme , phosphatase , chemistry , biochemistry , enzyme kinetics , active site , physics , quantum mechanics
Laboratory exercises that utilize alkaline phosphatase as a model enzyme have been developed and used extensively in the undergraduate biochemistry laboratory to illustrate enzyme steady‐state kinetics. A bioinformatic laboratory exercise for the Biochemistry laboratory, which complements the traditional alkaline phosphatase kinetics laboratory, was developed and implemented. In this exercise students examine the structure of alkaline phosphatase using the free online bioinformatic protein‐modeling program Protein Explorer and in doing so examine the active site residues of alkaline phosphatase and propose functions for these residues. Furthermore, by examining the mechanism of alkaline phosphatase and by using published kinetic data, students propose specific roles for several active site residues of alkaline phosphatase. Formative assessment of student learning demonstrates increased understanding of enzyme kinetic constants and increased understanding of active site residue functions after completing this exercise.