Monitoring active site alterations upon mutation of yeast pyruvate kinase using 205Tl+ NMR.

doi:10.1074/jbc.M306068200

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Article

Monitoring active site alterations upon mutation of yeast pyruvate kinase using 205Tl+ NMR.

The Journal of biological chemistry - 17 Oct 2003

Susan-Resiga Delia, Nowak Thomas

Abstract excerpt

The interaction of the monovalent cation with wild type (WT) yeast pyruvate kinase (YPK) and with the T298S, T298C, and T298A mutants was investigated by 205Tl+ NMR to monitor possible structural alterations at the active site by Thr-298 mutation. TlNO3 activates WT YPK with a kcat value similar to that obtained with KCl and an apparent Ka of 0.96 +/- 0.07 mm in the presence of Mn2+ and fructose 1,6-bisphosphate....

Topics

Animals
Binding Sites
Dose-Response Relationship, Drug
Fungal Proteins
Kinetics
Magnetic Resonance Spectroscopy
Models, Chemical
Mutation
Protein Conformation
Pyruvate Kinase
Rabbits
Thallium Radioisotopes

Source

Open in PubMed

Identifiers

PMID: 12882975
DOI: 10.1074/jbc.M306068200

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