Global ETD Search

Understanding PTPLP specificity: from atomic resolution to rational mutagenesis

Cleland, Colyn P., University of Lethbridge. Faculty of Arts and Science2025

lethbridge

Structure and substrate specificity of myo-inositol phosphatases at atomic resolution

Bruder, Lisza M.Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry2013

… phosphatase-like myo-inositol phosphatases (PTPLPs) follow an ordered, sequential dephosphorylation pathway that utilizes the abundant myo-inositol- 1,2,3,4,5,6-hexakisphosphate (InsP6) to produce less-phosphorylated myo-inositol phosphates (IPs) containing between one and five phosphoryl …

lethbridge Repository record for Structure and substrate specificity of myo-inositol phosphatases at atomic resolution (opens in a new tab)

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)

Specificity of a novel myo-inositol phosphatase towards less-phosphorylated myo-inositol phosphates

Van Herk, Peter2014

lethbridge

Rapid kinetic studies of PhyA from Selenomonas ruminantium, and a simplified means of production of a phosphate biosensor

Smith, Dustin D., University of Lethbridge. Faculty of Arts and Science2016

lethbridge