Bioinformatic and Biochemical Characterizations of C–S Bond Formation and Cleavage Enzymes in the Fungus Neurospora crassa Ergothioneine Biosynthetic Pathway | Zendy

Wen Jun Hu | Zendy; Heng Song | Zendy; Ampon Sae Her | Zendy; Daniel W. Bak | Zendy; Nathchar Naowarojna | Zendy; Sean J. Elliott | Zendy; Qin Li | Zendy; Xiaoping Chen | Zendy; Pinghua Liu | Zendy

Open Access

Bioinformatic and Biochemical Characterizations of C–S Bond Formation and Cleavage Enzymes in the Fungus Neurospora crassa Ergothioneine Biosynthetic Pathway

Author(s) -

Wen Jun Hu,

Heng Song,

Ampon Sae Her,

Daniel W. Bak,

Nathchar Naowarojna,

Sean J. Elliott,

Qin Li,

Xiaoping Chen,

Pinghua Liu

Publication year - 2014

Publication title -

organic letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.94

H-Index - 239

eISSN - 1523-7060

pISSN - 1523-7052

DOI - 10.1021/ol502596z

Subject(s) - ergothioneine , neurospora crassa , chemistry , biochemistry , enzyme , biosynthesis , stereochemistry , neurospora , cysteine , lyase , gene , mutant , antioxidant

Ergothioneine is a histidine thiol derivative. Its mycobacterial biosynthetic pathway has five steps (EgtA-E catalysis) with two novel reactions: a mononuclear nonheme iron enzyme (EgtB) catalyzed oxidative C-S bond formation and a PLP-mediated C-S lyase (EgtE) reaction. Our bioinformatic and biochemical analyses indicate that the fungus Neurospora crassa has a more concise ergothioneine biosynthetic pathway because its nonheme iron enzyme, Egt1, makes use of cysteine instead of γ-Glu-Cys as the substrate. Such a change of substrate preference eliminates the competition between ergothioneine and glutathione biosyntheses. In addition, we have identified the N. crassa C-S lyase (NCU11365) and reconstituted its activity in vitro, which makes the future ergothioneine production through metabolic engineering feasible.

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