Cloning and characterization of filamentous fungal S-nitrosoglutathione reductase from Aspergillus nidulans

Yao Zhou, Shengmin Zhou, Haijun Yu, Jingyi Li, Yang Xia, Baoyi Li, Xiaoli Wang, Ping Wang

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


S-Nitrosoglutathione reductase (GSNOR) metabolizes S-nitrosoglutathione (GSNO) and has been shown to play important roles in regulating cellular signaling and formulating host defense by modulating intracellular nitric oxide levels. The enzyme has been found in bacterial, yeast, mushroom, plant, and mammalian cells. However, to date, there is still no evidence of its occurrence in filamentous fungi. In this study, we cloned and investigated a GSNOR-like enzyme from the filamentous fungus Aspergillus nidulans. The enzyme occurred in native form as a homodimer and exhibited low thermal stability. GSNO was an ideal substrate for the enzyme. The apparent Km and kcat values were 0.55 mM and 34, 100 min-1, respectively. Substrate binding sites and catalytic center amino acid residues based on those from known GSNORs were conserved in this enzyme, and the corresponding roles were verified using site-directed mutagenesis. Therefore, we demonstrated the presence of GSNOR in a filamentous fungus for the first time.

Original languageEnglish (US)
Pages (from-to)928-937
Number of pages10
JournalJournal of Microbiology and Biotechnology
Issue number5
StatePublished - May 2016

Bibliographical note

Publisher Copyright:
© 2016 by The Korean Society for Microbiology and Biotechnology.


  • Aspergillus nidulans
  • Denitrosation
  • Nitric oxide
  • Nitrosation
  • S-nitrosoglutathione reductase


Dive into the research topics of 'Cloning and characterization of filamentous fungal S-nitrosoglutathione reductase from Aspergillus nidulans'. Together they form a unique fingerprint.

Cite this