A 7-dimethylallyl tryptophan synthase from a fungal Neosartorya sp.: biochemical characterization and structural insight into the regioselective prenylation

Bioorg Med Chem. 2014 Apr 15;22(8):2517-28. doi: 10.1016/j.bmc.2014.02.031. Epub 2014 Mar 12.

Abstract

A putative 7-dimethylallyl tryptophan synthase (DMATS) gene from a fungal Neosartorya sp. was cloned and overexpressed as a soluble His6-fusion protein in Escherichia coli. The enzyme was found to catalyze the prenylation of L-tryptophan at the C7 position of the indole moiety in the presence of dimethylallyl diphosphate; thus, it functions as a 7-DMATS. In this study, we describe the biochemical characterization of 7-DMATS from Neosartorya sp., referred to as 7-DMATS(Neo), and the structural basis of the regioselective prenylation of L-tryptophan at the C7 position by comparison of the three-dimensional structural models of 7-DMATS(Neo) with FgaPT2 (4-DMATS) from Aspergillus fumigatus.

Keywords: 7-Dimethylallyl tryptophan synthase (7-DMATS); Neosartorya sp.; Prenylated indole derivatives; Regioselective prenylation; Three-dimensional structural models.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkyl and Aryl Transferases / chemistry*
  • Alkyl and Aryl Transferases / genetics
  • Alkyl and Aryl Transferases / metabolism
  • Amino Acid Sequence
  • Aspergillus fumigatus / enzymology
  • Catalytic Domain
  • Escherichia coli / metabolism
  • Fungal Proteins / chemistry*
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism
  • Kinetics
  • Neosartorya / enzymology*
  • Prenylation
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Stereoisomerism
  • Substrate Specificity
  • Tryptophan / metabolism*

Substances

  • Fungal Proteins
  • Recombinant Proteins
  • Tryptophan
  • Alkyl and Aryl Transferases
  • tryptophan dimethylallyltransferase