Ontology highlight
ABSTRACT:
SUBMITTER: Puhl AA
PROVIDER: S-EPMC2206706 | biostudies-literature | 2007 Jul
REPOSITORIES: biostudies-literature
Puhl Aaron A AA Gruninger Robert J RJ Greiner Ralf R Janzen Timothy W TW Mosimann Steven C SC Selinger L Brent LB
Protein science : a publication of the Protein Society 20070613 7
PhyA from Selenomonas ruminantium (PhyAsr), is a bacterial protein tyrosine phosphatase (PTP)-like inositol polyphosphate phosphatase (IPPase) that is distantly related to known PTPs. PhyAsr has a second substrate binding site referred to as a standby site and the P-loop (HCX5R) has been observed in both open (inactive) and closed (active) conformations. Site-directed mutagenesis and kinetic and structural studies indicate PhyAsr follows a classical PTP mechanism of hydrolysis and has a broad sp ...[more]