ThYme: a database for thioester-active enzymes

Nucleic Acids Res. 2011 Jan;39(Database issue):D342-6. doi: 10.1093/nar/gkq1072. Epub 2010 Nov 2.

Abstract

The ThYme (Thioester-active enzYme; http://www.enzyme.cbirc.iastate.edu) database has been constructed to bring together amino acid sequences and 3D (tertiary) structures of all the enzymes constituting the fatty acid synthesis and polyketide synthesis cycles. These enzymes are active on thioester-containing substrates, specifically those that are parts of the acyl-CoA synthase, acyl-CoA carboxylase, acyl transferase, ketoacyl synthase, ketoacyl reductase, hydroxyacyl dehydratase, enoyl reductase and thioesterase enzyme groups. These groups have been classified into families, members of which are similar in sequences, tertiary structures and catalytic mechanisms, implying common protein ancestry. ThYme is continually updated as sequences and tertiary structures become available.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Acyltransferases / chemistry
  • Acyltransferases / classification
  • Acyltransferases / metabolism
  • Amino Acid Sequence
  • Carbon-Carbon Ligases / chemistry
  • Carbon-Carbon Ligases / classification
  • Carbon-Carbon Ligases / metabolism
  • Catalytic Domain
  • Databases, Protein*
  • Fatty Acids / biosynthesis*
  • Hydro-Lyases / chemistry
  • Hydro-Lyases / classification
  • Hydro-Lyases / metabolism
  • Ligases / chemistry
  • Ligases / classification
  • Ligases / metabolism
  • Macrolides / metabolism*
  • Oxidoreductases / chemistry
  • Oxidoreductases / classification
  • Oxidoreductases / metabolism
  • Protein Structure, Tertiary
  • Thiolester Hydrolases / chemistry
  • Thiolester Hydrolases / classification
  • Thiolester Hydrolases / metabolism

Substances

  • Fatty Acids
  • Macrolides
  • Oxidoreductases
  • Acyltransferases
  • Thiolester Hydrolases
  • Hydro-Lyases
  • Ligases
  • Carbon-Carbon Ligases
  • acyl-CoA carboxylase