Journal article
Two Conserved Histidine Residues Are Critical to the Function of the TagF-like Family of Enzymes*
Abstract
The TagF protein from Bacillus subtilis 168 is the poly(glycerol phosphate) polymerase responsible for the synthesis of wall teichoic acid and is the prototype member of a poorly understood family of similar teichoic acid synthetic enzymes. Here we describe in vitro and in vivo characterization of TagF, which localizes the active site to the carboxyl terminus of the protein and identifies residues that are critical for catalysis. We also …
Authors
Schertzer JW; Bhavsar AP; Brown ED
Journal
Journal of Biological Chemistry, Vol. 280, No. 44, pp. 36683–36690
Publisher
Elsevier
Publication Date
November 2005
DOI
10.1074/jbc.m507153200
ISSN
0021-9258
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Amino Acid SequenceBacillus subtilisBinding SitesBlotting, WesternConserved SequenceDNA Mutational AnalysisGenetic Complementation TestGlycerophosphatesHistidineKineticsMolecular Sequence DataMutagenesis, Site-DirectedMutationProtein BindingRecombinant ProteinsSequence Homology, Amino AcidTemperatureTransferases (Other Substituted Phosphate Groups)