Your browser doesn't support javascript.
loading
Urzymology: experimental access to a key transition in the appearance of enzymes.
Carter, Charles W.
Affiliation
  • Carter CW; Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260. Electronic address: carter@med.unc.edu.
J Biol Chem ; 289(44): 30213-30220, 2014 Oct 31.
Article in En | MEDLINE | ID: mdl-25210034
ABSTRACT
Urzymes are catalysts derived from invariant cores of protein superfamilies. Urzymes from both aminoacyl-tRNA synthetase classes possess sophisticated catalytic mechanisms pre-steady state bursts, significant transition-state stabilization of both amino acid activation, and tRNA acylation. However, they have insufficient specificity to ensure a fully developed genetic code, suggesting that they participated in synthesizing statistical proteins. They represent a robust experimental platform from which to articulate and test hypotheses both about their own ancestors and about how they, in turn, evolved into modern enzymes. They help reshape numerous paradigms from the RNA World hypothesis to protein structure databases and allostery.
Subject(s)
Key words

Full text: 1 Database: MEDLINE Main subject: Evolution, Molecular / Amino Acyl-tRNA Synthetases Language: En Journal: J Biol Chem Year: 2014 Type: Article

Full text: 1 Database: MEDLINE Main subject: Evolution, Molecular / Amino Acyl-tRNA Synthetases Language: En Journal: J Biol Chem Year: 2014 Type: Article