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B6db references: 25275953

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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