|
type |
Journal Article |
authors |
Xu B, Fan Z, Lei Y, Ping Y, Jaisi A, Xiao Y |
title |
Insights into Pipecolic Acid Biosynthesis in Huperzia serrata |
journal |
Org Lett |
Activity |
l-lysine.2-aminotransferase |
Family |
l-lysine.2-aminotransferase.b |
sel |
selected |
ui |
29589944 |
year |
(2018) |
volume |
20 |
number |
8 |
pages |
2195-2198 |
| |
keywords |
DOI: 10.1021/acs.orglett.8b00523 |
abstract |
For the biosynthesis of Pip in Huperzia serrata, the mechanistic studies were evaluated. Through a series of biochemical analyses, Pip is biosynthesized through a two-step cascade reaction. Three intermediates possibly exist simultaneously as an equilibrium matter in the first-step reaction catalyzed by HsAld1, while HsSard4 performs as a ketimine reductase and chemoselectively and stereoselectively takes 1,2-dehydropipecolic acid as the preferred substrate in vitro. PMID:
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last changed |
2018/08/28 14:33 |
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