|
type |
Journal Article |
authors |
Hu W, Song H, Sae Her A, Bak DW, Naowarojna N, Elliott SJ, Qin L, Chen X, Liu P |
title |
Bioinformatic and biochemical characterizations of C-S bond formation and cleavage enzymes in the fungus Neurospora crassa ergothioneine biosynthetic pathway |
journal |
Org Lett |
Activity |
4.4.1.36 |
Family |
4.4.1.36 |
sel |
selected |
ui |
25275953 |
year |
(2014) |
volume |
16 |
number |
20 |
pages |
5382-5 |
| |
keywords |
doi: 10.1021/ol502596z |
abstract |
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. |
last changed |
2017/12/21 12:55 |
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