Kimberly M Mayer
Affiliation: University of North Carolina
- Linking enzyme sequence to function using Conserved Property Difference Locator to identify and annotate positions likely to control specific functionalityKimberly M Mayer
Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA
BMC Bioinformatics 6:284. 2005....
- Identification of amino acid residues involved in substrate specificity of plant acyl-ACP thioesterases using a bioinformatics-guided approachKimberly M Mayer
Brookhaven National Laboratory, Department of Biology, Upton, NY 11973, USA
BMC Plant Biol 7:1. 2007..Variants were expressed in E. coli strain K27 that allows determination of enzyme activity by GCMS analysis of fatty acids released into the medium...
- A structural model of the plant acyl-acyl carrier protein thioesterase FatB comprises two helix/4-stranded sheet domains, the N-terminal domain containing residues that affect specificity and the C-terminal domain containing catalytic residuesKimberly M Mayer
Biology Department, Brookhaven National Laboratory, Upton, New York 11973, USA
J Biol Chem 280:3621-7. 2005..Together these data corroborate the structural model and show that the hot dog fold is common to enzymes from both prokaryotes and eukaryotes and that this fold supports at least three different catalytic mechanisms...
- Exploring the diversity of marine-derived fungal polyketide synthasesKimberly M Mayer
Center for Marine Science, University of North Carolina at Wilmington, 5600 Marvin Moss Lane, Wilmington, NC 28409, USA
Can J Microbiol 53:291-302. 2007..Evaluating primer-binding sites was necessary to obtain KS domain fragments from putative PKSs while maintaining a level of sequence information adequate to properly classify and characterize them...