Global ETD Search

Expanding our knowledge of protein tyrosine phosphatase-like phytases : mechanism, substrate specificity and pathways of myo-inositol hexakisphosphate dephosphorylation

Puhl, Aaron A., University of Lethbridge. Faculty of Arts and ScienceLethbridge, Alta. : University of Lethbridge, Faculty of Arts and Science, 20062006

A novel bacterial protein tyrosine phosphatase (PTP)-like enzyme has recently been isolated that has a PTP-like active site and fold and the ability to dephosphorylate myo-inositol hexakisphosphate. In order to expand our knowledge of this novel class of enzyme, four new representative genes were …

lethbridge Repository record for Expanding our knowledge of protein tyrosine phosphatase-like phytases : mechanism, substrate specificity and pathways of myo-inositol hexakisphosphate dephosphorylation (opens in a new tab)

The characterization of two novel PTP-enzymes from Bdellovibrio bacteriovorus and Pseudomonas syringae pv. tomato DC3000

Thibault, John L, University of Lethbridge. Faculty of Arts and Science2010

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Structure and function of PhyA from Desulfovibrio magneticus and use of its product in affinity pull-down experiments

Cleland, Colyn P., University of Lethbridge. Faculty of Arts and ScienceLethbridge, Alta. : University of Lethbridge, Dept. of Chemistry & Biochemistry2019

… X-ray crystallographic structure of a divergent PTPLP from Desulfovibrio magneticus has been determined in the presence and absence of InsP6 substrate in order to identify the structural features that give rise to its 3-4-5 substrate specificity. These include a novel Phy loop conformation and …

lethbridge Repository record for Structure and function of PhyA from Desulfovibrio magneticus and use of its product in affinity pull-down experiments (opens in a new tab)