Acetyl xylan esterase II from Penicillium purpurogenum is similar to an esterase from Trichoderma reesei but lacks a cellulose binding domain

Rodrigo Gutiérrez, Ella Cederlund, Lars Hjelmqvist, Alessandra Peirano, Francisco Herrera, Debashis Ghosh, William Duax, Hans Jörnvall, Jaime Eyzaguirre

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Penicillium purpurogenum produces at least two acetyl xylan esterases (AXE I and II). The AXE II cDNA, genomic DNA and mature protein sequences were determined and show that the axe 2 gene contains two introns, that the primary translation product has a signal peptide of 27 residues, and that the mature protein has 207 residues. The sequence is similar to the catalytic domain of AXE I from Trichoderma reesei (67% residue identity) and putative active site residues are conserved, but the Penicillium enzyme lacks the linker and cellulose binding domain, thus explaining why it does not bind cellulose in contrast to the Trichoderma enzyme. These results point to a possible common ancestor gene for the active site domain, while the linker and the binding domain may have been added to the Trichoderma esterase by gene fusion.

Original languageEnglish
Pages (from-to)35-38
Number of pages4
JournalFEBS Letters
Volume423
Issue number1
DOIs
Publication statusPublished - 13 Feb 1998

Keywords

  • Acetyl xylan esterase
  • Cellulose binding domain
  • Gene fusion
  • Penicillium purpurogenum

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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